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  • Collagen
  • Springer  (35)
  • American Geophysical Union
  • American Physical Society
  • Taylor & Francis
  • 1975-1979  (27)
  • 1965-1969  (8)
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Keywords
Publisher
  • Springer  (35)
  • American Geophysical Union
  • American Physical Society
  • Taylor & Francis
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Year
  • 1
    Electronic Resource
    Electronic Resource
    The effect of some inhibitors on the nucleation and crystal growth of apatite (1969)
    Springer
    Calcified tissue international 3 (1969), S. 348-357 
    Details
    ISSN: 1432-0827
    Keywords: Inhibitors ; Nucleation ; Apatite ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé Des ions de Mg, Sr et F sont inhibitoires pour la formation de l'apatite quand on les ajoute à un tampon de calcification, séparément ou en combinaisons. La précipitation de l'apatite causée par des cristaux d'apatite est moins sensible à l'action inhibitrice que la nucléation spontanée et que la précipitation catalysée par la collagène d'os de mouton. La précipitation spontanée ou catalysée sont approximativement aussi sensibles. L'inhibition par des combinaisons de Mg avec des ions de Sr ou de F est additive. Ces résultats montrent que ces inhibiteurs ont acucune action spécifique sur la catalysation par la collagène de l'os de mouton qui soit différente de celle sur la nucléation de l'apatite en soi.
    Abstract: Zusammenfassung Mg, Sr und F Ionen hemmten die Fällung von Apatit wenn sie zu einem Calciumphosphatpuffer einzeln oder zusammen hinzugefügt wurden. Die Fällung von Apatit durch Apatitkeime war weniger empfindlich hinsichtlich der Hemmung als die spontane Nucleation und als die Fällung von Apatit, welche von Schafsknochenkollagen katalysiert werden kann. Die spontane und katalysierte Fällung sind ungefähr gleich empfindlich. Die Hemmung von Mg in Kombination mit Sr oder F Ionen war additiv. Diese Resultate weisen darauf hin, daß keine spezifischen Effekte bei der Katalyse von Knochenkollagen vorliegen, welche von den Effekten bei der Nucleation von Apatit an sich verschieden sind.
    Notes: Abstract Mg, Sr and F ions acted as inhibitors of apatite formation when added to a calcification buffer separately or in combinations. The precipitation of apatite under the influence of apatite seeds was less susceptible to inhibition than were spontaneous nucleation and apatite formation catalyzed by sheep bone collagen, while the latter two were about equally susceptible. Combinations of Mg with Sr or F ions showed additive effects. These results suggest that no specific effects of these inhibitors occurred on the catalytic action of the bone collagen different from their effects on the nucleation of apatite as such.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02058677
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  • 2
    Electronic Resource
    Electronic Resource
    A macromolecular inhibitor of in vitro calcification of tendon matrix (1978)
    Springer
    Calcified tissue international 25 (1978), S. 161-168 
    Details
    ISSN: 1432-0827
    Keywords: Tendon ; Calcification ; Collagen ; Inhibitors ; Proteoglycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Bovine and human tendon tissue do not induce calcification in vitro. However, extraction of those tissues with 3% Na2HPO4 converts them to calcifiable matrices. The supernatant fraction derived from the extraction contains a nondialyzable, perchloric acid soluble component that inhibits calcification of the extracted matrix. This inhibitory substance is characterized by a molecular weight in the range of 85,000–100,000. Exposure to pronase or hyaluronidase did not alter the inhibitory potency but did render the inhibitor dialyzable. Commercial sources of hyaluronic acid, chondroitin-6-sulfate, chrondroitin-4-sulfate, dermatan sulfate, heparin and lysozyme did not inhibit calcification of the extracted matrix. Phosvitin, a phosphoglycoprotein is a potent inhibitor. Although phosvitin and the tendon extract also inhibit calcification of previously calcified matrix, they have no detectable effect on the rate of decalcification. We conclude that the mechanism of inhibition is characterized by a degree of specificity and that phosvitin and a macromolecular component of tendon tissue blocks conversion of an intermediate matrix-bound CaP complex to crystalline apatite. It seems reasonable that the tendon inhibitor could function in situ and possibly in vivo to control calcification of tendon tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02010764
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  • 3
    Electronic Resource
    Electronic Resource
    A preliminary characterization of human cementum collagen (1977)
    Springer
    Calcified tissue international 23 (1977), S. 147-150 
    Details
    ISSN: 1432-0827
    Keywords: Collagen ; Cementum ; Human cementum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Human teeth were used to obtain cementum. Collagen could not be significantly solubilized from the cementum by salt and acetic acid extraction or by pepsin digestion. CNBr digestion (86%) of cementum and subsequent carboxymethyl cellulose chromatography suggests that human cementum consists of type I collagen only as identified by amino acid and hexose analyses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02012780
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  • 4
    Electronic Resource
    Electronic Resource
    Rabbit cranial sutures in vitro: A new experimental model for studying the response of fibrous joints to mechanical stress (1979)
    Springer
    Calcified tissue international 28 (1979), S. 137-144 
    Details
    ISSN: 1432-0827
    Keywords: Cranial sutures ; Organ culture ; Tensile mechanical stress ; Protein ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary An organ culture system has been developed whereby mechanical stress can be applied to cranial sutures under controlled experimental conditions. The application of a continuous tensile mechanical stress (30 g) to cranial sutures from newborn rabbits (1–2 days) was accompanied by a significant increase in the incorporation of3H-leucine and3H-proline into suture protein. The specific activities of3H-hydroxyproline indicated that mechanical stress produced a two-fold increase in the incorporation of3H-proline into collagen. However, the proportion of the total radioactivity recoverable in collagen (45.63±2.33% for nonstressed; 40.58±2.17% for stressed sutures) was not significantly different. These data suggest that the increase in collagen synthesis occurs as part of a general stimulation of protein synthesis, and do not support the view that mechanical stress is the principal mechanism regulating the turnover of collagen in fibrous joints. These initial studies demonstrate that an in vitro experimental model has considerable potential for investigating the morphological and metabolic response of fibrous joints to mechanical deformation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441232
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  • 5
    Electronic Resource
    Electronic Resource
    On the solid state of bone (1979)
    Springer
    Calcified tissue international 28 (1979), S. 33-36 
    Details
    ISSN: 1432-0827
    Keywords: Infrared, visible light ; Bone ; Collagen ; Apatite
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Photovoltaic effect (infrared and visible light) is observed in bone and its two major components, collagen and apatite, at room temperature. A dimunition in the magnitude of photovoltage is observed after exposure to ultraviolet light in all the cases. The drift mobility of the charge carriers is obtained by measuring I versus V relationships in sandwich samples and relating them to the permitivity of the medium. Lifetime of the injected carriers is measured in the usual way. The data are consistent with the hypothesis that the effects are due to protonic conduction phenomena.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441215
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  • 6
    Electronic Resource
    Electronic Resource
    Relationship between iron, calcium and phosphate during experimental cutaneous calcinosis (1969)
    Springer
    Calcified tissue international 4 (1969), S. 224-230 
    Details
    ISSN: 1432-0827
    Keywords: Calcinosis ; Calcium ; Iron ; Phosphate ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé La calcification de la peau (calciphylaxie) provoquée par l'administration sous-cutanée de chlorure de fer chez des rats sensibilisés par le dihydrotachystérol (DHT) est précédée par une déposition sélective de fer (décelable à la microscopie électronique) à la surface des fibres collagènes. Les analyses à la microsonde prouvent que les taux de calcium et de phosphore sont augmentés à l'endroit de l'injection du chlorure de fer même sans l'administration préalable de DHT; cependant, l'apatite ne se forme que chez les animaux prétraités par le DHT. La quantité et le degré de cristallinité de la matière inorganique sont presque identiques au sixième et au trentième jour de l'expérience.
    Abstract: Zusammenfassung Durch elektronenmikroskopische Untersuchungen wurde festgestellt, daß die durch subcutane Verabreichung von Eisenchlorid bei Dihydrotachysterin-sensibilisierten Ratten herbeigeführte Hautverkalkung durch eine selektive Eisenablagerung auf der Oberfläche der Kollagenfibrillen eingeleitet wird. Die Röntgenmikroanalyse zeigt an, daß die lokale Calciumund Phosphorkonzentration bereits nach Eiseninjektion allein ansteigt, während Apatitbildung nur in den mit DHT vorbehandelten Tieren erfolgt. Ausmaß und Menge der Kristallisation sind am 6. und 30. Tage nach Versuchsbeginn fast gleich.
    Notes: Abstract Calcification of the skin (calciphylaxis) induced by the subcutaneous administration of iron chloride to dihydrotachysterol (DHT)-sensitized rats is preceded by the selective deposition of iron (visible with electron microscopic techniques) on the surface of collagen fibrils. Electron probe X-ray microanalysis indicates that the injectionof iron alone suffices to increase local concentrations of calcium and phosphorus; however, apatite formation occurs only in animals pretreated with DHT. The amount and degree of crystallinity of the inorganic material is very similar on the sixth and thirtieth day after the beginning of the experiment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02279125
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  • 7
    Electronic Resource
    Electronic Resource
    The effect of electric current on rat tail tendon collagen in solution (1969)
    Springer
    Calcified tissue international 4 (1969), S. 330-338 
    Details
    ISSN: 1432-0827
    Keywords: Collagen ; Electric current ; Electrolysis ; Precipitation ; Bone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé L'effet du courant électrique sur la collagène soluble, en solution dans l'acide acétique dilué, a été étudié pour des voltages, variant de O à 25 volts. Au-dessus de 2,6 volts, la vormation des bandes collagéniques (définies dans ce travail) parait inversement proportionelle, dans le temps, au voltage appliqué. La formation des bandes parait liée au processus d'électrolyse. Les auteurs démontrent que les pH élevés se situent au niveau de la cathode et qu'ils sont suffisants pour induire une précipitation du collagène. Les résultats antérieurs, publiés dans la littérature, décrivant l'action de courant électrique implanté, sont interpretés en fonction du mécanisme étudié au cours de ce travail.
    Abstract: Zusammenfassung Die Wirkung eines elektrischen Stromes auf verdünnte essigsaure Lösungen von löslichem Kollagen wurde bei Spannungen zwischen O und 25 Volt untersucht. Über 2,6 Volt wurde die Bildung von Kollagenbanden (in der Arbeit näher beschrieben) beobachtet, und zwar nach Zeiten, die der angewandten Spannung entgegengesetzt proportional verliefen. Die Bandenbildung wird dem Elektrolyseprozeß zugeschrieben. Wir konnten zeigen, daß sich die hohen pH-Werte rund um die Kathode entwickelten und daß diese genügen, um die Kollagenfällung zu veranlassen. Die Natur dieses Vorganges ist solcher Art, daß erin vivo als Antwort auf durch Stress verursachte Biopotentiale nicht vorkommen kann. Der hier beschriebene Mechanismus erlaubt es, Literaturangaben über den Effekt von implantierten Spannungsquellen zu interpretieren.
    Notes: Abstract The effect of electric current on dilute acetic acid solutions of soluble collagen has been studied for impressed voltages of from 0 to 25 volts. Above 2.6 volts the formation of collagen bands (herein defined) were observed at times inversely proportional to the applied voltage. Band formation is attributed to the process of electrolysis. It has been shown that the high pH values are generated in the area of the cathode, and that they are sufficient to induce collagen to precipitate. The nature of the process is such that it cannot occurin vivo as a response to stress induced biopotentials. Reports in the literature describing the effect of implanted voltage sources are interpreted in terms of the mechanism described here.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02279135
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  • 8
    Electronic Resource
    Electronic Resource
    Self complementarity in messenger RNA of collagen (1976)
    Springer
    Journal of molecular evolution 8 (1976), S. 155-173 
    Details
    ISSN: 1432-1432
    Keywords: Self-Complementarity ; Messenger-RNA ; Collagen ; Secondary Structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The periodic protein collagen is of special interest for the study of the relationship which exists between the structure of a protein and that of its mRNA, because oligopeptides containing glycine, proline (hydroxyproline) and alanine occur with great frequency in it. Collagen is particularly rich in these amino acids, which have codons containing only G and/or C in the obligatory first and second positions. If unlimited choice of codons for all amino acids were to occur, the stretch of mRNA coding for anα-chain should contain about 40% G and 31% C (Bachra et al., 1974). These high values suggest that a considerable degree of secondary structure will occur, unless selective codon use would result in the avoidance of G and C in optional third codon positions. In the present paper putative secondary structure formation in collagen mRNA was studied. This was done by studying the positions and frequencies of hairpin structures which could contain stem sections composed of the coding triplets of the above mentioned amino acids and hairpin sections of 4-40 bases. Calculation of the free energy contributions of such hairpin structures, using published values for the contributions of base-pair stacking, hairpin, bulge and interior loops and also taking into account the possible minimum number of base-pairs required for helix nucleation from a single-strand RNA (3 adjacent AU-pairs or 1 or 2 adjacent GC-pairs) led to the following conclusions. A considerable number of alternative, mutually exclusive hairpins can be constructed. The stability and rate of nucleation of these will be reduced if: 1. G and C were avoided as third bases in the glycine, proline (hydroxyproline) and alanine triplets, 2. the glycine triplet used were preferentially either GGU or GGA and the proline triplet preferentially either CCU or CCA, 3. the alanine triplet did not contain a third base complementary to that used in the opposing glycine or proline triplet. If these conditions were not fulfilled a considerable degree of secondary structure could be expected to be present. Further studies of this kind may yield additional information which could also be useful in chemical work on the sequencing of collagen mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01739101
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  • 9
    Electronic Resource
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    Ultrastructure of collagen in sea urchin embryos (1979)
    Springer
    Development genes and evolution 186 (1979), S. 65-70 
    Details
    ISSN: 1432-041X
    Keywords: Sea urchin ; Embryo ; Collagen ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Collagen fibrils with a main period banding of 610 Å and 220 Å in width were observed in the blastocoel of 72-h embryos of the sea urchin,Strongylocentrotus purpuratus. Non-striated fibrils of 50 Å diameter were also observed. The collagen is seen in highest concentration in the vicinity of mesenchyme cells which are richly endowed with endoplasmic reticulum and secretory vesicles. A role for collagen in cell attachment, orientation and spicule formation is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00848108
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  • 10
    Electronic Resource
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    On the state of anionic groups of demineralized matrices of bone and dentine (1977)
    Springer
    Calcified tissue international 22 (1977), S. 275-284 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Calcium ; Collagen ; Dentine ; Phosphoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Calcium-binding and biochemical studies have been applied to characterize the state of the carboxylate and protein-bound phosphate groups in the EDTA-demineralized matrices of rat bone and dentine. The organic phosphate and carboxylate content of demineralized bone is virtually identical to that of purified steer skin collagen whereas demineralized dentine has a significantly higher phosphate and carboxylate content, presumably due to the presence of an acidic non-collagenous phosphoprotein. Two classes of calcium-binding sites can be detected in demineralized bone, demineralized dentine, and purified, reconstituted collagen. The number of strong calcium-binding sites correlates with the number of protein-bound phosphate groups. Depending on the preparative procedure, seven to nine such sites (per collagen molecule) are present in dentine, and one to two in the purified reconstituted collagen and in bone. The binding constant for the dentinal sites (1.1×104 M−1), however, is 20 times greater than that for bone or reconstituted collagen fibrils from skin. We tentatively conclude that the strong calcium-binding site in bone and reconstituted collagen is of the form protein-PO 4 − Ca++ whereas in dentine it is of the form the weak binding sites in bone and dentine are of the form protein-COO-Ca++; and that approximately 160 of the 217 carboxylate groups of the collagen molecules of dentine or bone are present as electrostatic linkages of the form protein-COO−+H3N-protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02010366
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  • 11
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    Effects of fluoride on in vitro calcification of tendon matrix (1978)
    Springer
    Calcified tissue international 26 (1978), S. 51-59 
    Details
    ISSN: 1432-0827
    Keywords: Collagen ; Calcification ; Fluoroapatite ; Nucleation ; Inhibitors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Ca2+ and Pi uptake induced in vitro by a collagenous matrix derived from bovine tendon is inhibited by 1×10−6 to 2×10−5 M NaF and stimulated by 2×10−5 to 2×10−3 M NaF. Fluoride uptake occurs only over the latter concentrtion range. The uptake of Ca2+, Pi, and F−1 progresses toward a limiting extent at which the molar Ca/P and Ca/F values are 1.6 to 1.7 and 4.5 to 5.7, respectively. Although the matrix-bound mineral, previously formed in the absence of NaF, readily undergoes dissolution when exposed to a Ca2+- and P-free medium of pH〈7.4, the bound mineral phase formed in the presence of NaF does not. We conclude that fluoroapatite is the primary matrix-bound mineral. The uptake of fluoride, Ca2+. and Pi by both uncalcified and previously calcified matrices is inhibited by methylenediphosphonate and by phosphonoacetate as is calcification in the absence of NaF. Kinetic studies indicate that formation of a CaP complex precedes the uptake of F−1 and suggest that F−1 and OH−1 compete for interation with the CaP complex during the calcification process. We concluded that fluoroapatite formation induced by the collagenous matrix occurs by a multistep pathway comparable to that proposed previously for hydroxyapatite formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02013234
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  • 12
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    A model for the distribution of HAP crystallites in bone—an hypothesis (1979)
    Springer
    Calcified tissue international 27 (1979), S. 53-56 
    Details
    ISSN: 1432-0827
    Keywords: Bone mineral model ; Crystallites ; Collagen ; TEM
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Previous study of the velocity of sound in hard tissues led to the hypothesis that collagen is stiffened because the intermolecular links between collagen molecules are embedded in mineral by the mineralizing process. Recently published available high-resolution electron microscope studies of biological apatitic crystals frequently show periodic lattice images of the crystal basal plane. Some of these images from bone and dentin display a sequence of etch pits strung linearly along the midline indicating a chain of screw dislocations. These are interpreted to be the loci of the embedded connecting links required by the collagen stiffening hypothesis. The particular crystallites seen in the micrographs probably are from the interfibril region. Most important, the periodic lattice images show the axes of the links must be parallel to the c-axis of the crystallite. The location of the crystallites and their orientation in situ indicate that the c-axis of the crystallites must be perpendicular to the collagen axis. X-ray diffraction studies available in the literature for a long time indicate the c-axis of HAP crystallites are parallel to the collagen molecular axes. A model of the crystallite distribution is presented which reconciles the two types of crystallite orientation. It is assumed there is only one physical mineralization process for all apatitic crystallites. Additional data from several sources, particularly the distribution of mineral between intra- and interfibril spaces deduced by Katz and Li, are used to develop a first-order model of mineral in bone. Hole filling crystallites between ends of colinear collagen molecules have their c-axes parallel to the molecular axis. The other crystallites must have their c-axes perpendicular to the collagen molecular axis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441161
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  • 13
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    Precipitation of calcium phosphates under conditions of double diffusion in collagen and gels of gelatin and agar (1979)
    Springer
    Calcified tissue international 27 (1979), S. 171-176 
    Details
    ISSN: 1432-0827
    Keywords: Calcium ; Phosphate ; Precipitation ; Double diffusion ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary One-dimensional double diffusion was applied to determine critical concentrations at which the precipitation of calcium phosphates occurs in reconstituted connective tissue collagen and agar gels at 37°C and in gelatin gels at 25°C. Experiments were performed in the presence of unbuffered 0.15 mol dm−3 NaCl, or 0.15 mol dm−3 NaCl-veronal adjusted to pH 7.4. It was found that critical concentrations of precipitation of both precipitating components, CaCl2 and phosphate buffer (pH 7.4), were equimolar and independent of the ratios of initial concentrations of the components. Critical concentrations of precipitation were not affected by the concentrations and kinds of gels used. The first-formed precipitates showed amorphous structure by X-ray diffraction analyses. Infrared (IR) spectra of the precipitates indicated CaHPO4 · H2O to be their predominant species. The molar Ca/P ratio obtained by chemical analyses was 1.08. This precipitate transformed in time into octacalcium phosphate. In all experiments, two very thin membranes of precipitate were formed in the gel column at the onset of precipitation simultaneously on both sides of the actual disc of precipitate. IR spectra and chemical analyses showed that both membranes were identical to the actual precipitation discs.
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    URL: http://dx.doi.org/10.1007/BF02441181
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  • 14
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    Mineral deposition in collagenin vitro (1968)
    Springer
    Calcified tissue international 2 (1968), S. 343-352 
    Details
    ISSN: 1432-0827
    Keywords: Nucleation ; Mineralization ; Bone ; Collagen ; Apatite
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé Nous avons utilisé de la collagène d'os de mounton et de tendons de queues de rats et des cristaux d'apatite pour étudier dans un système modèle la catalysation de la nucléation et la déposition de minéral dans un tampon métastabile. La collagène d'os de mouton se trouvait être un bon catalysateur, tandis que des expériences antérieures ont démontré que la collagène de tendons de queues de rats était un catalysateur très faible. Le phase rapide de la déposition de l'apatite dans la collagène se termine aussitôt que le contenu du minéral a attaint au plus 50 à 60 pour cent, bien que la supersaturation du tampon est encore bien èlevée. Les résultats montrent que dans un tel système modèle la quantité du depôt minéral est réglée par des facteurs semblables à ceux qui opèrent pendant la calcification biologique.
    Abstract: Zusammenfassung Kollagen aus Schafsknochen und Rattenschwanzsehnen und Apatitkeime wurden verwendet in einem Modell-System zur Untersuchung der katalytischen Nukleation und der Fällung von Mineral in einem metastabilen Calciumphosphatpuffer. Kollagen aus Schafsknochen war ein guter Katalysator für die Nukleation, während in früheren Versuchen sich herausstellte, daß Rattenschwanzkollagen ein ganz schlechter Katalysator ist. Die schnelle Phase der Apatitfällung im Kollagen war beendet, wenn der Mineralgehalt bis zu 50–60% angestiegen war, obwohl der Puffer noch stark übersättigt war. Die Resultate weisen daraufhin, daß die Menge des gefällten Minerals in einem solchen Modell-System von ähnlichen Faktoren reguliert wird wie die biologische Verkalkung.
    Notes: Abstract Sheep bone collagen, rat tail tendon collagen and apatite seeds were used in a model system to study nucleation catalysis and mineral deposition in a metastable calcification buffer. Sheep bone collagen was shown to be a good nucleation catalyst, while earlier experiments have shown that rat tail tendon collagen was a very poor catalyst. The rapid phase of apatite deposition in the collagen was terminated as soon as a mineral content of not more than 50–60 per cent was reached, although the buffer was still highly supersaturated. The results suggest that the amount of mineral deposited in such a model system is regulated by factors similar to those operating in biological calcification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02279222
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  • 15
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    Proteins of the periodontium (1977)
    Springer
    Calcified tissue international 23 (1977), S. 39-44 
    Details
    ISSN: 1432-0827
    Keywords: Dental cementum ; Collagen ; Protein ; Chemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Cyanogen bromide (CNBr) peptides were prepared of the insoluble collagen of bovine dental cementum. Following chromatographic separation, the peptides were identified by their amino-acid composition. Type I collagen ([α1(I)]2α2) accounted for more than 90% of the organic matrix, while Type III collagen ([α1(III)]3) was present at a level of approximately 5%. Amino-acid analyses revealed that the CNBr peptides from α1(I) and α2 chains of cementum closely resembled the corresponding peptides from calf skin. The only systematic difference was a higher level of hydroxylation of prolyl and lysyl residues of the cementum peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02012764
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  • 16
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    Absorption spectra of bone (1977)
    Springer
    Calcified tissue international 23 (1977), S. 113-114 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Absorption Spectra ; Collagen ; Hydroxyapatite
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Absorption spectra of human bone and its two major constituents (collagen and apatite) were obtained in the wavelength region extending from 2000 to 12,000 Å. In the last two cases a, minimum transmission (maximum absorption) was uniformly observed in the ultraviolet region. The two samples after exposure to ultraviolet radiations show a shift in the peak positions. Absorption peaks in the total bone spectra are not reproducible in its two constituents. After exposure to UV radiations the position of maximum absorption is displaced. A possible interpretation of the observed results is presented.
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    URL: http://dx.doi.org/10.1007/BF02012774
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  • 17
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    Comparison of effects of parathyroidectomy and ethane-1-hydroxy-1,1-diphosphonate (EHDP) administration upon bone synthesis of hydroxyproline and urinary excretion of hydroxyproline in rats (1977)
    Springer
    Calcified tissue international 23 (1977), S. 115-119 
    Details
    ISSN: 1432-0827
    Keywords: Parathyroidectomy ; Diphosphonates ; Bone ; Collagen ; Hydroxyproline
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Disodium ethane-1-hydroxy-1,1-diphosphonate (EHDP) may impair mineralization and reduce turnover of bone. However, its administration has been shown to lead to an accumulation of osteoid in both man and the rat. Using rats, the effects of surgical parathyroidectomy and administration of EHDP (30 mg EHDP/kg body weight by subcutaneous injection daily for 5 days) upon bone composition, uptake of3H-proline into hydroxyproline in bone and the subsequent urinary excretion of labelled and unlabelled hydroxyproline have been compared. Both parathyroidectomized (PTX) rats and EHDP-treated animals accumulated more hydroxyproline in bone and excreted less total urinary hydroxyproline than sham-PTX control animals, the changes induced by EHDP being of greater magnitude than those induced by surgical parathyroidectomy. Skeletal buildup of hydroxyproline was associated with decreased catabolism of mature collagen rather than enhanced synthesis of hydroxyproline in bone. EHDP administration, although decreasing urinary excretion of newly synthesised hydroxyproline, did not alter the skeletal synthesis of hydroxyproline as measured by uptake of3H-proline. In all parameters measured, responses to EHDP were similar in PTX and sham-PTX rats. It is concluded that depression of parathyroid hormone mediated bone turnover may have contributed to, but did not fully account for, the lowering of bone turnover and changes in bone composition induced by EHDP in sham-PTX rats in the present experiment.
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    Phosphophoryns—major noncollagenous proteins of rat incisor dentin (1978)
    Springer
    Calcified tissue international 25 (1978), S. 169-178 
    Details
    ISSN: 1432-0827
    Keywords: Phosphophoryn ; Phosphoproteins ; Dentin ; Mineralization ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Freshly excised rat incisors were immediately cleaned and demineralized in 0.5M ethylene diaminetetracetic acid at pH 7.5. The extracts were freed of calcium, diffusible phosphate and low molecular weight polypeptide components by dialysis in membranes with cut-off of 3500 molecular weight. The extract was resolved into at least 7 protein components by chromatography on DEAE-cellulose at pH 8.2. The composition of each protein component was determined. Two proteins, rich in serine, phosphorous and aspartic acid were unlike any proteins attributed to enamel, and hence were considered to be components of incisor dentin. These were the principal noncollagenous components of the teeth. Further purification was carried out under dissociative conditions on Sepharose CL-6B gel filtration columns in 3.0M guanidine hydrochloride. The two phsophoproteins have mol wts, by this method, of 71,000 and 65,000, respectively, and differ in content of apolar amino acids, although both contain 〉70 residue % of seryl (or phosphoseryl) and aspartyl residues. The name “phosphophoryns” is proposed to describe these dentinal proteins. The insoluble collagenous matrix remaining after the original demineralizing extraction was degraded with cyanogen bromide. Several non-collagenous protein components were released as well as the typical collagen derived peptides. Two collagen phosphoprotein complex peptides were also isolated, demonstrating as in bovine dentin, the probable direct covalent interaction of a dentin phosphoprotein with the collagen of the mineralized matrix.
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    URL: http://dx.doi.org/10.1007/BF02010765
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    Chemical aspects of the matrix concept in calcified tissue organisation (1968)
    Springer
    Calcified tissue international 2 (1968), S. 1-19 
    Details
    ISSN: 1432-0827
    Keywords: Collagen ; Hydroxyapatite ; Keratin ; Enamel ; Calcification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02279189
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    Incorporation and release of85Sr and14C-proline-hydroxyproline in mineral and collagen of bone and incisor teeth of growing rats (1968)
    Springer
    Calcified tissue international 2 (1968), S. 106-110 
    Details
    ISSN: 1432-0827
    Keywords: Collagen ; 14C-Proline ; Growth ; Bone ; Teeth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Zusammenfassung Das Ausmaß, bis zu welchem Austausch- und Wiederverwendungsprozesse der mineralen Tracer die Messungen des mineralen Skelett-Auf- und Abbaues beeinflussen können, wurde ausgewertet; zu diesem Zweck wurde die Geschwindigkeit des Auftretens und Verschwindens von85Sr und von14C-Prolin-Hydroxyprolin in Knochen und Zähnen von wachsenden Ratten während der 12 auf die simultane parenterale Injektion dieser Tracer folgenden Tage verglichen. Der Ausdruck für die relative Geschwindigkeit des Kollagen-Auf- und Abbaues, bei welchem im Gegensatz zum Mineralmetabolismus kein Mitwirken des Austauschphänomens vermutet wird, basiert auf der Umwandlung von14C-Prolin zu14C-Hydroxyprolin; die spezifische Aktivität des letzteren wurde bestimmt. Aus der spezifischen Aktivität des Minerals sowie jener des Kollagens konnten die Geschwindigkeit und die Art des Wachstums der untersuchten Proben ersehen werden, d.h.schnelles Wachstum und ein kurzes Zeitintervall zwischen Bildung und Resorption des Gewebes imKnochen der Metaphyse, die auch die knorpelige Wachstumsplatte enthält, und andererseitslangsames Wachstum und längeres Zeitintervall (länger als die 12 Tage des Experimentes) zwischen Bildung und Resorption des Gewebes imKnochen der Diaphyse und in den Schneidezähnen. Immerhin fiel die spezifische Aktivität des Kollagen/Mineral-Anteils im Knochen der Metaphyse während dem 4–12tägigen Zeitintervall auf die Hälfte, im Gegensatz zum Knochen der Diaphyse und der Schneidezähne, bei welchen während dieser Zeitspanne kein Unterschied in diesem Verhältnis beobachtet wurde. Diese Ergebnisse zeigen, daß Kollagen in der Wachstumszone der Metaphyse durch Resorption verschwindet, bevor es ganz mineralisiert ist, und daß der Austausch ein relativ unwichtiger Faktor in der Kinetik auf lange Sicht des Knochenminerals ist.
    Notes: Abstract The extent to which exchange and reutilization processes of mineral tracers affect skeletal mineral accretion and resorption measurements was evaluated by comparing the rates of appearance and disappearance of85Sr and14C-proline-hydroxyproline in bones and teeth in growing rats for 12 days following simultaneous parenteral injection of these tracers. Expressions for the relative rates of collagen synthesis and breakdown, which unlike mineral metabolism are considered not to be complicated by exchange phenomena, were based on14C-proline conversion to14C-hydroxyproline; the specific activity of the latter was determined. Both the mineral and the collagen specific activities reflected the rates and patterns of growth of the samples assayed; rapid growth and a short interval of time between formation and resorption of tissue in themetaphyseal bone which contains the cartilagineous growth plate, slow growth and an interval of time between formation and resorption of tissue indiaphyseal bone and incisor teeth which is longer than the 12 days of the experiment. However, in metaphyseal bone the specific activity collagen/mineral ratio dropped by one half during the 4–12 day interval in contrast to diaphyseal bone and incisor teeth in which no change in this ratio was observed during this period of time. The data indicate that collagen in the metaphyseal growth zone is removed by resorption before it has become fully mineralized, and that exchange is a relatively unimportant factor in the long term kinetics of bone mineral.
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    Effect of disuse osteoporosis on bone composition: the fate of bone matrix (1968)
    Springer
    Calcified tissue international 2 (1968), S. 20-29 
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    ISSN: 1432-0827
    Keywords: Bone Atrophy ; Bone Resorption ; Calcium ; Collagen ; Osteoporosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé Atrophie osseuse d'immobilisation était induite par section de la plexus brachial et/ou désarticulation de la coude. Après 9 bis 12 semaines de désuétude huméri intactes furent examinés par rayons X et leur qualités physiques déterminés. Les humérientiers furent isolés, dégraissés, desséchés au poids constant, et leur teneur en cendre d'os et collagène déterminés. Huit des 10 huméri immobilisés monstrérent radiodensité diminué. La jambe inusitée monstra perte parallèle en poids sec et poids sans gras (−23.2%), en collagène (−25.3%), et en cendre d'os (−26.1%) en comparaison de la jambe normale. Les données monstrèrent que la portion plus grande du tissu osseux perdu en atrophie osseuse d'immobilisation est remplacée par de l'eau, du gras, et des autres matériels organiques inconnus plutôt que par tissu fibreux, et que collagène est perdu en proportion du minéral. La perte proportionellement plus grande du collagène et de la cendre d'os que du poids sec et poids san gras semble dû à une augmentation du matériel organique, non-collagéne, non-lipide, kprobablement protéine.
    Abstract: Zusammenfassung Immobilisations-Knochenatrophie wurde in 10 erwachsenen Hunden herbeigeführt durch Brachialplexusschnitt und/oder Ellenbogenexartikulation. Nach 9–12 Wochen der Immobilisation wurden die intakten Humeri unter Röntgenstrahlen untersucht und ihre physischen Eigenschaften bestimmt. Derintakte Humerus wurde isoliert, entfettet, zu konstantem Gewicht getrocknet und der Knochenaschengehalt und Kollagengehalt bestimmt. Acht der 10 experimentellen (immobilisierten) Humeri demonstrierte Beweis von verringerter Röntgendichte. Die immobilisierte Extremität zeigte ähnlichen Verlust in trockenem, fettfreiem Gewicht (−23,2%) in Kollagen (−25.3%) und Knochenasche (−26,1%) im Vergleich zur normalen Extremität. Die Date deuten an, daß der Hauptanteil des Verlustes des Knochengewebes (bei Immobilisations-Knochenatrophie) von Wasser, Fett und anderen unidentifizierten organischen Substanzen ersetzt wird, als von Faserngewebe und daß Kollagen und Knochenasche im gleichen Verhältnis verloren gehen. Der größere, proportionale Verlust an Kollagen und Knochenasche, eher als der Verlust an fettfreiem Gewicht, scheint in der Zunahme an nicht kollagener, nicht lipoider, organischer Substanz, vermutlich Protein, zu liegen.
    Notes: Abstract Disuse bone atrophy was induced in 10 adult dogs by means of brachial plexus section and/or elbow disarticulation. After 9 to 12 weeks of disuse intact humeri were examined by X-ray, and their physical properties determined. Thewhole humeri were isolated, defatted, dried to constant weight, and their mineral and collagen content determined. Eight out of 10 experimental (non-used) humeri demonstrated evidence of decreased radiodensity. The non-used limb demonstrated parallel loss in dry, fat-free weight (−23.2%), in collagen (−25.3%), and in mineral (−26.1%), as compared to the normal limb. The data indicated that the major portion of the lost bone tissue in disuse osteoporosis is replaced by water, fat, and other unidentified organic materials rather than fibrous tissue, and that collagen is lost in equal proportion to mineral. The proportionatelly greater loss of collagen and mineral than of dry, fat-free weight appears to be due to an increase of non-collagenous, non-lipid organic material, presumably protein.
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    Experimental factors that influence collagen calcificationin vitro (1968)
    Springer
    Calcified tissue international 2 (1968), S. 214-228 
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    ISSN: 1432-0827
    Keywords: Calcinosis ; Calcification ; Cartilage ; Collagen ; Mineral metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Description / Table of Contents: Résumé Les facteurs, influençant la vitesse et l'intensité du phénomène d'association des ions calcium et phosphates avec des fibres contenant du collagène, et préparés à partir du tendon de boeuf par deux méthodes d'extraction différentes, ont été étudiés. Les fibres, obtenues par ces deux méthodes, nécessitent spécifiquement du phosphate pour absorber du calcium et vice versa. L'absorption ionique des deux préparations est inhibée par du Mg++, du pyrophosphate et un peptide acidique, isolé du sérum humain. Alors que les fibres contenant du collagène, préparées selon les deux méthodes, présentent une absorption ionique à des vitesses sensiblement identiques, seule une des méthodes donne une matrice réagissant positivement à la technique de coloration au nitrate d'argent de von Kossa. Etant donné que les deux critères de calcification sont intéressés de façon identique par des conditions de réaction et par des inhibiteurs, il apparait que les deux facteurs sont des manifestations de différents stades de calcification et que des études d'absorption ionique fournissent une base quantitative d'appréciation de la calcification, pouvant être d'importance pour l'étude du mécanisme et de contrôle de la minéralisation tissulaire.
    Abstract: Zusammenfassung Überprüft wurden die Faktoren, welche Geschwindigkeit und Ausmaß der Erscheinung beeinflussen, wobei Calcium- und Phosphationen sich mit den kollagenhaltigen, durch zwei verschiedene Extraktionsmethoden aus Rindersehnen gewonnenen Fasern eng zusammenbinden. Die mit beiden Methoden zubereiteten Fasern benötigen spezifisch Phosphat für die Calciumaufnahme und Calcium für die Phosphataufnahme. Die Ionenaufnahme beider Arten wird durch Mg++, Pyrophosphat und saure, aus dem menschlichen Serum isolierte Peptide gehemmt. Während die nach beiden Methoden präparierten kollagenhaltigen Fasern eine Ionenaufnahme von beinahe gleicher Geschwindigkeit verursachen, ergibt nur eine dieser Methoden eine Matrix, die mit der Silbernitratfärbung nach vonKossa positiv reagiert. Da beide Calcifikationskriterien gleicherweise durch Reaktionsbedingungen und Inhibitoren beeinflußt werden, wird daraus geschlossen, daß beide Erscheinungen verschiedener Stadien des Gesamtcalcifikationsprozesses sind. Untersuchungen über die Ionenaufnahme ergeben eine quantitative Angabe der Verkalkung, welche für die Erforschung des Mechanismus und der Kontrolle der Mineralisation der Gewebe wichtig sein könnte.
    Notes: Abstract Factors that influence the rate and extent of the phenomenon in which calcium and phosphate ions become firmly associated with collagen-containing fibers prepared from beef tendon by two different extraction methods have been investigated. The fibers produced by both methods specifically require phosphate for calcium uptake and calcium is required for phosphate uptake. Ion uptake by both types is inhibited by Mg++, pyrophosphate, and an acidic peptide isolated from human serum. Whereas the collagen-containing fibers prepared by both methods induce ion uptake at nearly identical rates, only one of the methods produced a matrix that gives a positive response to the silver nitrate staining technique of von Kossa. Since both criteria of calcification are similarly influenced by reaction conditions and inhibitors, it is concluded that both are manifestations of different stages of the overall calcification process and that studies of ion uptake provide a quantitative assessment of calcification which could be of importance for investigating the mechanism and control of tissue mineralization.
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    Structural changes in smooth muscle cells during isotonic contraction (1976)
    Springer
    Cell & tissue research 170 (1976), S. 187-201 
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    ISSN: 1432-0878
    Keywords: Smooth muscle ; Contraction ; Taenia coli ; Ultrastructure ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Smooth muscle cells of the guinea-pig taenia coli were studied in light and electron microscopy, in condition of mild stretch or of isotonic contraction. During contraction the cells increase in transverse sectional area and their packing density passes from 94,000 · mm-2 to 18,000 · mm-2. The percentage increase in transverse sectional area of the taenia is approximately the same as the percentage decrease in length. Measurements of cell transverse sectional area suggest that the individual cells shorten and fatten more than the taenia as a whole. Whereas stretched muscle cells run parallel to each other and show a fairly smooth surface, isotonically contracted cells are twisted and entwine around each other. Their surfaces are covered with myriad processes and folds. Longitudinal, transverse or oblique stripes are seen in light microscopy in the contracted muscle cells and it is suggested that they are related to the characteristics of the cell surface. In electron microscopy a complex pattern of interdigitating finger-like and laminar processes is observed. Caveolae are mainly found on the evaginated parts of the cell surface, dense patches are mainly (but not always) found on the invaginated parts. Desmosome-like attachments between contracted cells are frequent. The collagen fibrils run approximately parallel to the stretched muscle cells; on the other hand, they run obliquely and transversely around the isotonically contracted cells.
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    The composition and protein metabolism in the immature rabbit intervertebral disc (1975)
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    Cell & tissue research 163 (1975), S. 223-238 
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    ISSN: 1432-0878
    Keywords: Intervertebral disc ; Collagen ; Non-collagenous proteins ; Metabolism ; Autoradiography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The nucleus pulposus (NP) and annulus fibrosus (AF) of immature rabbit intervertebral discs (IVD) have been subjected to the dissociative extraction procedure of Sajdera and Hascall (1969). The soluble, insoluble and unextracted fractions so obtained were analysed for total nitrogen, collagen, tyrosine, uronic acid, hexosamine and sialic acid content. A high proportion of non-collagenous protein, hexose and sialic acid in the NP insoluble fraction suggests the presence of glycopeptides associated with collagen and/or proteoglycans. The levels of proteoglycan in the soluble NP and AF fraction are similar. Immature (soluble) collagen, however, resides largely in the AF region. The metabolism of rabbit IVD protein components was also investigated both chemically and by autoradiography. l-Tyrosine-3,5-H3 was administered intraperitoneally (3 mc/kg) to 4 week-old rabbits. Animals were sacrificed at various time intervals and the harvested tissues extracted as before and lumbar discs collected. The levels of l-Tyrosine-3,5-H3 in the NP and AF insoluble and soluble fractions were determined using a tritium scintillation counting procedure and localisation by autoradiography. Pronounced extra-cellular activity of proteoglycan and glycoprotein is not evident before 24 hours. Soluble collagen, however, is synthesised and dispersed within 4 hours of isotope administration.
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    URL: http://dx.doi.org/10.1007/BF00221729
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    The structure of the tapetum of the eye of the sheep (1975)
    Springer
    Cell & tissue research 157 (1975), S. 73-91 
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    ISSN: 1432-0878
    Keywords: Eye (Sheep) ; Tapetum ; Collagen ; Microfibrils ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The structure of the tapetum of the sheep's eye has been examined by transmission electron microscopy. It consists of regularly arranged layers of collagen fibrils, estimated from the hydroxyproline content to make up about 60% of the dry weight of the tissue. There are several hundred of these layers in the whole depth, a majority being orientated in the same direction. The collagen is associated with strands of microfibrillar material as well as with cells of both fibrocyte and smooth muscle types.
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    Substrate dependence of cell migration from explanted neural tubes in vitro (1976)
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    Cell & tissue research 172 (1976), S. 325-330 
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    ISSN: 1432-0878
    Keywords: Neural crest ; Collagen ; Extracellular materials ; Cell migration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Embryonic chick neural tubes containing neural crest cells were cultured in vitro on tissue culture plastic and collagen. Two parameters, the time of onset of cell migration from the neural tube and the rate of movement of the cell front away from the neural tube explant, were determined. On collagen, cell migration consistently began after four to six h in vitro, about five h prior to the onset of cell migration on tissue culture plastic. The identity of the migrating cells as neural crest cells is established by their eventual differentiation into melanocytes. Ablation experiments reveal that collagen also causes the early onset of migration of cells not of neural crest origin. These results provide in vitro support for the idea that extracellular materials may alter cell migratory behaviour in morphogenesis.
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    URL: http://dx.doi.org/10.1007/BF00399515
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    Scanning electron microscopy of bone cells in culture (1976)
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    Cell & tissue research 166 (1976), S. 65-70 
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    ISSN: 1432-0878
    Keywords: Collagen ; Bone ; Cell culture ; Scanning electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Embryonic and young rat bone cells have been grown in culture and examined in the scanning electron microscope (SEM). Compared with cells fixed in situ and taken directly from the animal, the cultured osteoblastic cells were smoother, flatter and more extensive and showed tighter intercellular contacts. Some matrix is formed in culture and undergoes at least partial mineralization as judged by the accumulation of Ca and P measured by energy dispersive x-ray analysis. Findings concerning the morphology of the collagen arrangement were indecisive. Some superficial cells, free of surrounding matrix, resembled osteocytes in normal in vivo bone. This may indicate that a proportion of the extracellular matrix produced by the cultured cells failed to polymerise into recognizable bone matrix, and that osteocytic morphology is not dependent upon the physical characteristics of the bone matrix.
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    URL: http://dx.doi.org/10.1007/BF00215125
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    The ultrastructure of the byssal apparatus of Mytilus galloprovincialis (1976)
    Springer
    Cell & tissue research 166 (1976), S. 219-234 
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    ISSN: 1432-0878
    Keywords: Electron microscopy ; Byssus ; Collagen ; Mytilus galloprovincialis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ultrastructure of the byssus of Mytilus galloprovincialis was analysed by transmission electron microscopy in thin sections of either embedded or frozen samples. All parts of the byssus (stem core laminae, stem outer laminae, threads proximal and distal parts) appear to be formed by the same basic filamentous components organized in different ways at the submicroscopic level and embedded in a variable quantity of matrix. The filaments appear to consist of a central electron-lucent zone (3 nm in diameter), surrounded by an electron-dense rim (total diameter 7 nm). The matrix has a granular or microfilamentous structure. The stem and the threads differ greatly in their submicroscopic organization, but their basic constituents (filaments and matrix) are similar. Peculiar filamentous banded elements (FBE) were found mainly in the stem outer laminae. A relation between the ultrastructure and mechanical properties of the different parts of the byssus was established. The presence of collagen is discussed; since no morphological evidence of any of the known forms of collagen organization was revealed by electron microscopy, it is suggested that byssus collagen may be localized in the matrix and in the FBE.
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    URL: http://dx.doi.org/10.1007/BF00227043
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    Ultrastructural features of adult human tendon (1976)
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    Cell & tissue research 168 (1976), S. 247-259 
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    ISSN: 1432-0878
    Keywords: Tendons ; Connective tissue ; Collagen ; Human ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A variety of human tendons have been studied at the electron microscope level. The fibers of these tendons are composed of collagen fibrils that average 1,750 Å and 600 Å in diameter. A third population that measures 100 Å in diameter may represent immature collagen or filaments that are incorporated into tendon elastic fibers. The larger collagen fibrils vary in ratio with respect to one another, and are connected by interfibrillar bridges which in some cases appear to extend through the substance of the fibril. The collagen fibrils of the paratenon are less-well organized than those of the tendon proper and average 600 Å in diameter. Tendons that exhibit the property of lateral stretch (plantaris and palmaris) were compared at the ultrastructural level with tendons that do not have this property. No differences between the two tendon types could be determined in normal or spread preparations, indicating that the differences in physical characteristics are a result of fiber rather than fibril organization.
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    Accumulation of collagen-containing vacuoles in osteoblasts after administration of colchicine (1975)
    Springer
    Cell & tissue research 157 (1975), S. 353-365 
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    ISSN: 1432-0878
    Keywords: Collagen ; Secretion ; Osteoblast ; Colchicine ; Vinblastine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Embryonic mouse radii were cultured in the presence of colchicine or vinblastine and subsequently examined in the electron microscope. As a result of the administration of these drugs large numbers of vacuoles accumulated in the cytoplasm of the osteoblasts. The electron-dense contents of at least many of the vacuoles most probably consisted of collagen. This conclusion was based on the results of special staining methods and on the similarity of the vacuoles to collagen vacuoles described in the literature. The observations made in this study provide morphological evidence that colchicine and vinblastine disturb the secretion of collagen.
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    URL: http://dx.doi.org/10.1007/BF00225526
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    Relationship between collagen fibril diameters and body size (1977)
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    Cell & tissue research 182 (1977), S. 119-131 
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    ISSN: 1432-0878
    Keywords: Fish ; Collagen ; Fibril diameter ; Age ; Body size
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Suspensions of collagen fibrils obtained from derma of Elasmobranchia and Actinopterygia of different body sizes and developmental stages were examined by transmission electron microscopy. Fibril diameters were measured and classified into groups comprising a 20 nm diameter interval. Diagrams showing fibril populations of each fish were made. The measurements were averaged and their confidence intervals and standard errors determined. For each species other diagrams were plotted in which the mean diameters were correlated to the body length of each sample. The results show that: 1) a correlation exists between an increase in diameter of collagen fibrils and somatic growth until sexual maturity is reached; 2) fibril populations are subsequently spread over a wider range due to the presence in the derma of classes of newly formed and therefore thinner fibrils. The deposition of new fibrils is possibly influenced by individual factors; 3) no relationship exists between mean fibril diameter and body size; 4) no relationship exists between phylogenetic position and pattern of diameter distribution.
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    Fine structure of isolated fibrils from the cuticle of Lumbricus sp. (1979)
    Springer
    Cell & tissue research 201 (1979), S. 459-466 
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    ISSN: 1432-0878
    Keywords: Electron microscopy ; Collagen ; Cuticle ; Lumbricus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A method has been developed to isolate and purify cuticular fibrils of Lumbricus. Polarizing microscopy confirms the collagenous nature of the isolated fibrils. Study in the electron microscope of isolated fibrils, negatively or positively stained, shows that they are cylindrical, unbranching and without periodic structure. Enzymatic treatment of cuticles with alpha-amylase and trypsin results in a more or less complete dissociation of the fibrils which appear clearly to be made up of helically wound bundles of filaments (30–40 Å). The structure of the cuticular fibrils is discussed in relation to biochemical and biophysical data and compared to the ultrastructural organization of other periodically cross-banded fibrils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00237004
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  • 33
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    The collagen of the vertebrate peripheral nervous system (1979)
    Springer
    Cell & tissue research 202 (1979), S. 453-460 
    Details
    ISSN: 1432-0878
    Keywords: Collagen ; Nerves ; Ganglia ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Nerves and ganglia from a variety of fish, amphibian, reptilian and mammalian species were studied by optical and electron microscopy. Observations using the Picrosirius-polarization method strongly suggest that two different types of collagen fibers are present in the connective tissues of nerves and ganglia. Electron microscopy of nerves and ganglia showed the presence of two different collagen fibril populations, distinguishable on the basis of diameter, located in different compartments of these structures. Thicker fibrils are present in nerve and ganglionic epineurium. Thinner fibrils are present in the endoneurium, surrounding nerve fibers and ganglionic cells, and between the concentric layers of perineurial cells. These results were consistently observed in all species studied and very probably represent a general phenomenon in vertebrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220437
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  • 34
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    Calcification of the collagenous axial skeleton of Veretillum cynomorium pall. (cnidaria: pennatulacea) (1978)
    Springer
    Cell & tissue research 192 (1978), S. 249-266 
    Details
    ISSN: 1432-0878
    Keywords: Calcification ; Calcite ; Collagen ; Pennatulid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Résumé L'axe squelettique de Veretillum cynomorium se compose d'une matrice fibrillaire de nature collagène, minéralisée par de la calcite. Le présent article fournit des données ultrastructurales et cristallographiques quant à l'organisation de cette structure et au dépôt du minéral dans la matrice. La pointe inférieure de l'axe constitue un gradient de calcification entre l'extrémité non minéralisée et le corps entièrement calcifié. Les dépôts initiaux de calcite, parfois associés à des débris cellulaires, donnent naissance à des nodules qui s'accroissent de façon rayonnée, par bourgeonnement de plusieurs lobes. Ces nodules fusionnent et forment le coeur de l'axe dont la croissance ultérieure en diamètre, se réalise par le développement de colonnes irrégulières de calcite à partir des nodules externes du coeur. Les surfaces minéralisées présentent une microarchitecture qui peut être reliée aux axes cristallographiques de la calcite. Les relations entre le minéral et la matrice ont particulièrement retenues notre attention. Les fibres de collagène, enrobées par la calcite et non imprégnées par elle, n'interviennent jamais comme initiateur de nucléation du minéral. L'orientation cristallographique ultérieure de la calcite est aussi totalement indépendante de la matrice.
    Notes: Summary The axial skeletal rod of Veretillum cynomorium consists of a fibrillar collagenous matrix calcified with calcite. The present paper describes ultrastructural and crystallographic details of its organization and deposition. At the inferior end of the rod is a calcification gradient between the noncalcified tip and the rest of the axis. Initial mineral deposits, which are sometimes associated with cell debris, give rise to calcitic nodules which enlarge by the radial growth of several lobes. These nodules fuse and form the core of the axis. Subsequent increase in diameter of the rod involves the radial development of irregular columns of calcite which arise from the peripheral nodules. Mineral surfaces exhibit a distinctive microarchitecture which can be related to the predominantly c-axis parallel growth of the calcite. Particular attention is paid to the relationship between mineral and matrix. The collagen fibrils, embedded in the calcite but never impregnated with it, are not responsible for the initial nucleation of mineral. The crystallographic orientation of the calcite also appears to be independent of these fibrils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220743
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  • 35
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    Arrangement of smooth muscle cells and intramuscular septa in the taenia coli (1977)
    Springer
    Cell & tissue research 184 (1977), S. 195-212 
    Details
    ISSN: 1432-0878
    Keywords: Taenia coli ; Guinea pig ; Smooth muscle ; Collagen ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Bands of electron-dense material beneath the cell membrane of smooth muscle cells of the guinea-pig taenia coli provide attachment to thin myofilaments and to intermediate (10 nm) filaments; about 50% of the cell membrane is occupied by dense bands in muscle cells transversely sectioned at the level of their nucleus, and between 50 and 100% in smaller cell profiles nearer the cell's ends. In addition to the known cell-to-cell junctions (intermediate contacts), more complex apparatuses anchor muscle cells together, either end-to-end or end-to-side or side-to-side. They consist of elaborate folds, invaginations and protrusions accompanied by large amounts of basal lamina material. In the end-to-end anchoring apparatuses numerous finger-like and laminar processes from the two cells interdigitate. Other muscle cells have a star-shaped profile in the last few microns of their length, or show longitudinal invaginations occupied by a thickened basal lamina and occasionally by collagen fibrils. The septa of connective tissue extend only for a few hundred microns along the length of the taenia. In taeniae fixed in condition of mild stretch the muscle cells form an angle of about 5° with the septa. In muscles fixed during isotonic contraction the angle increases to about 20–22°, and in longitudinal sections the muscle cells appear arranged in a herring-bone pattern. The collagen concentration in the taenia coli is 4–6 times greater that in skeletal and cardiac muscles. These various structures are discussed in terms of their possible role in the mechanism of force transmission.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00223068
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