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  • Bone  (16)
  • Springer  (16)
  • American Association of Petroleum Geologists (AAPG)
  • 1980-1984  (16)
Collection
Keywords
Publisher
  • Springer  (16)
  • American Association of Petroleum Geologists (AAPG)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Bone histomorphometric reproducibility in normal patients (1981)
    Springer
    Calcified tissue international 33 (1981), S. 369-374 
    Details
    ISSN: 1432-0827
    Keywords: Histomorphometry ; Bone ; Reproducibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary To study bone histomorphometry reproducibility in normal subjects, we performed during orthopedic surgery bone biopsies in 16 post-menopausal women. Each woman had four bone biopsies, two at the usual site in the iliac crest, one on the left and one on the right side, and two other biopsies just behind the usual site, one at each side. We performed measurements of trabecular bone volume, relative osteoid volume, osteoid surfaces, osteoclastic resorption surfaces and calcification front. The average values of the 16 patients were compared, on the one hand, two by two, by a student test, and on the other hand, by a variance analysis. By these two methods the results showed no significant difference between the average values of the 16 patients at each location for any of the histomorphometric parameters studied. However, there was a location variation which was estimated by the intra-individual variation for a given patient. On the other hand, we calculated from the variance analysis the location variance for a group of 10 to 100 patients. In any case all the parameters had a location variation which was high for osteoclastic resorption surfaces and relative osteoid volume when expressed in % of the absolute value of these parameters. The variation of the trabecular bone volume was 0–46. 15% (95% confident limit interval) in a single patient and the hypothetical value of the location variation was 41.6% for a group of 10 patients and 13.0% for a group of 100 patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409458
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of active bone resorption by copper (1981)
    Springer
    Calcified tissue international 33 (1981), S. 35-39 
    Details
    ISSN: 1432-0827
    Keywords: Copper ; Resorption ; Bone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary An investigation of the role of copper in bone metabolism was undertaken. Explanted calvaria from 6-day-old mice were grown for 48 h in medium with and without the addition of copper sulfate. Active resorption was found to be significantly inhibited in the presence of copper sulfate concentrations of 10−6M and above. Copper sulfate concentrations of 10−5M and above inhibited hydroxyproline, protein, and DNA synthesis. Lower concentrations were ineffective. The effect of 5 × 10−6M copper sulfate on resorption was reversible. Several other compounds were tested for similar effects and at 5 × 10−6M were found to inhibit bone resorption in the order: copper sulfate 〉 brown gold chloride 〉 sodium aurothiomalate 〉 zinc sulfate 〉 sodium sulfate. The copper sulfate effect was twice that of sodium aurothiomalate, and sodium sulfate was not significantly inhibitory. The results suggest that the high serum copper levels associated with rheumatoid arthritis may reflect the activity of a hypothetical control mechanism of bone resorption. In the diseased state this would act to restore the normal rate of bone resorption.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409410
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  • 3
    Electronic Resource
    Electronic Resource
    Histological observations on the failure of rachitic rat bones to respond to 1,25/OH)2D3 (1980)
    Springer
    Calcified tissue international 31 (1980), S. 215-223 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; 1,25(OH)2D3 ; 25OHD3 ; Histology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Rachitic rats, maintained on diets with low or normal P contents, were given daily intraperitoneal doses of 1,25(OH)2D3 or 25OHD3 at levels of 100 or 200 ng. Plasma chemistry was measured and the ash content and histological appearance of the bones investigated. Using labeled material it was shown that the dosing levels of 1,25(OH)2D3 employed ensured a higher than normal plasma concentration of that metabolite over the period between doses. 1,25(OH)2D3 was not as effective as 25OHD3 in raising bone ash or reducing the amount of osteoid. The difference between the effects of the metabolites was evident at both dietary P levels, but more marked at the higher P level. In contrast, the metabolites reduced the width of the epiphyseal plate to an approximately similar degree, and this is possibly the reason why there are discrepancies between previous reports of the effectiveness of 1,25(OH)2D3 compared with 25OHD3 or vitamin D3. Dosing with 1,25(OH)2D3 failed to maintain a constant plasma Pi value over the period between doses in animals fed the low P diet.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02407184
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  • 4
    Electronic Resource
    Electronic Resource
    Neutral peptidase activities in matrix vesicles from bovine fetal alveolar bone and dog osteosarcoma (1983)
    Springer
    Calcified tissue international 35 (1983), S. 791-797 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Osteosarcoma ; Matrix vesicles ; Alkaline phosphatase ; Aminopeptidase ; Naphthylamidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Extracellular matrix vesicles from bovine fetal alveolar bone and from a dog osteosarcoma were isolated by differential centrifugation and then fractionated on a discontinuous sucrose density gradient. The fractions were examined by electron microscopy and were analyzed for protein, alkaline phosphatase, aminotripeptidase, and four different β-naphthylamidase activities. The low-density peak of enzyme activities was shown by electron microscopy to be much more homogeneous than the crude matrix vesicle fraction. Two major peaks of protein and enzyme activities were present, one in the high and one in the low density layers. There was good correlation between the activities of alkaline phosphatase and the various peptidases in the fractions from the sucrose density gradient. These results indicate a coexistence of peptidase and alkaline phosphatase in matrix vesicles. On the other hand, there was generally no correlation between the peptidase and alkaline phosphatase activities in vesicular specimens from bovine liver obtained in the same way. Most of the peptidase activity and about half of the alkaline phosphatase activity were solubilized from bone matrix vesicles by detergents. The extracted alkaline phosphatase and alanyl β-naphthylamidase activities were separated from each other on a DEAE-cellulose column.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405125
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  • 5
    Electronic Resource
    Electronic Resource
    Occurrence of actin-like protein in extracellular matrix vesicles (1982)
    Springer
    Calcified tissue international 34 (1982), S. 376-381 
    Details
    ISSN: 1432-0827
    Keywords: Matrix vesicles ; Bone ; Actin ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Preliminary indications of the occurrence of actin and myosin in crude matrix vesicle preparations have been reported previously. In the present study extracellular matrix vesicles from rat alveolar bone were isolated. They were further purified by a sucrose density gradient. SDS-polyacrylamide gel electrophoresis of the purified vesicles revealed the presence of a polypeptide with a molecular weight of 43 K daltons and with electrophoretic mobility identical to that of blood platelet actin. The limited proteolysis of both 43 K dalton vesicular polypeptide and actin byStaphylococcus aureus-V8-protease revealed three fragments with identical electrophoretic mobility. In addition, the vesicular preparations inhibited the activity of DNase I, a property typical of actin monomers. Filamentous material extracted from matrix vesicles showed ultrastructural features of F-actin. Reaction of this material with heavy meromyosin resulted in arrowhead formation, which is characteristic of acto-heavy meromyosin. The occurrence of actin in extracellular matrix vesicles may account for their budding from the osteoblastic plasma membrane, their possible motility in the matrix, and maintenance of the spherical shape.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02411271
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  • 6
    Electronic Resource
    Electronic Resource
    Studies on extractable and resistant proteoglycans from metaphyseal and cortical bone and cartilage (1981)
    Springer
    Calcified tissue international 33 (1981), S. 89-99 
    Details
    ISSN: 1432-0827
    Keywords: Soluble proteoglycans ; Resistant proteoglycans ; Collagen ; Bone ; Cartilage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Soluble proteoglycans (SPG) were extracted from bovine (BCC) and human (HCC) costal cartilages by the dissociative method using 4 M guanidinium chloride (GuHCl). Proteoglycans which are resistant to extraction (RPG) were obtained following collagenase digestion or hydroxylamine treatment of the cartilage residues. Similarly, SPG were extracted from bovine metaphyseal and cortical bone using EDTA. The RPG were extracted from the bones using hydroxylamine. Density gradient fractionation under dissociative conditions of cartilage SPG and RPG followed by chromatography on Sepharose 2B revealed that A1D1 RPG are smaller than the SPG. SPG reacted with either collagenase or hydroxylamine are also smaller than the parent SPG. A1D1 fractions obtained from BCC-SPG and RPG or from mixtures of SPG and acid-soluble collagen are free of hydroxyproline. Hydroxyproline is not completely separated from HCC-RPG. Density gradient fractionation of bone proteoglycans and Sepharose chromatography of the A1 and A1D1 fractions showed that those obtained from metaphysis are larger than those from cortical bone. This was attributed to the presence of calcified cartilage in metaphyseal bone. The A1D1 fractions of the metaphyseal proteoglycans seemed to undergo self-association since this fraction is larger than the A1 fraction from which it is derived. Cortical bone proteoglycans do not behave similarly. Density gradient purification under dissociative conditions failed to separate hydroxyproline from the proteoglycans obtained from bone. It is hypothesized that in bone proteoglycans and collagen might be linked.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409419
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  • 7
    Electronic Resource
    Electronic Resource
    Radiographic evidence of disuse osteoporosis in the monkey (M. nemestrina) (1981)
    Springer
    Calcified tissue international 33 (1981), S. 631-639 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Osteopenia ; Noninvasive monitoring
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Radiological techniques were utilized for monitoring progressive changes in compact bone in the tibia of monkeys during experimentally induced osteopenia. Bone mass loss in the tibia during restraint was evaluated from radiographs, from bone mineral analysis, and from images reconstructed from gamma ray computerized tomography. The losses during 6 months of restraint tended to occur predominantly in the proximal tibia and were characterized by subperiosteal bone loss, intracortical striations, and scalloped endosteal surfaces. Bone mineral content in the cross section of the tibia declined 17–21%. Tomography demonstrated endosteal widening and reduced mineral content per unit of thickness of cortical bone. In 6 months of recovery, the mineral content of the proximal tibia remained depressed. Effects of the dynamic environment on local-regional changes in various skeletal areas are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409501
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  • 8
    Electronic Resource
    Electronic Resource
    X-ray diffraction studies of the crystallinity of bone mineral in newly synthesized and density fractionated bone (1983)
    Springer
    Calcified tissue international 35 (1983), S. 202-209 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Mineral ; Crystallinity ; Maturation ; Age
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The crystallinity of bone mineral at different stages of maturation has been measured by quantitative X-ray diffraction methods. Crystallinity measurements were made on tibial middiaphyses from 17-day embryonic chicks, newlyformed periosteal bone from embryonic chicks, and density-fractionated bone from post-hatch chickens from 5 weeks to 2 years of age. For a given animal age and degree of mineralization, crystallinity increases with animal age, indicating that changes in bone mineral occur even after mineralization is complete or nearly complete.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405032
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  • 9
    Electronic Resource
    Electronic Resource
    Human vertebral bone: Relation of strength, porosity, and mineralization to fluoride content (1980)
    Springer
    Calcified tissue international 32 (1980), S. 189-194 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Fluoride ; Strength ; Porosity ; Mineralization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Radiographically normal vertebral bone cylinders from 80 male subjects were tested mechanically by static compression and analyzed for porosity, fluoride and ash content. As a group, they had low fluoride content, suggesting little prior intake, consonent with this geographic area. Nevertheless, increasing levels of fluoride were associated with bulkier bone, less porosity, and less mineral per unit of bone, which in direction though not degree suggested changes similar to those of osteomalacia and opposite from those of osteoporosis without apparent threshold. The higher fluoride hard tissue was weaker in static tests than that with less fluoride, but the increased bulk apparently offset this, resulting in bones of unchanged static strength. Hence, water fluoridation should not alter static bone strength. There has, however, been a recent report suggesting that increased mineralization of bone renders it more brittle and thus more likely to fracture on impact. Therefore, the possibility that fluoridation may increase impact resistance by lessening mineralization can be entertained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02408540
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  • 10
    Electronic Resource
    Electronic Resource
    Density of a sample bovine cortical bone matrix and its solid constituent in various media (1981)
    Springer
    Calcified tissue international 33 (1981), S. 499-504 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Collagen ; Density
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The density of a bovine cortical bone matrix sample was found in water, several ethanol-water solutions, and in the dried state. Previously the density of the same mineralized bone was found fresh and when desiccated. The volume in each state was estimated from the dimensional changes axially, tangentially, and radially. Confirmation was found by determining the density of dried specimens upon immersion in xylene. The amount of imbibed xylene provided an estimate of the free pore volume in the dried matrix. The volume fraction of the solid constituent, S, in the wet matrix was found to be 0.57, from which the density of S in various solutions was calculated. Density of wet matrix in 0.15 M saline: 1.180 g/cc; for dried matrix, 1.246 g/cc. Density of wet S in saline: 1.33 g/cc; for dried S, 1.42 g/cc, which matches published values for collagen molecules. Dimensional changes between wet and dried state of matrix match published values for artificially cross-linked rat tail tendon fibers. Axially: 1.04, by area: 2.27; by volume: 2.62. Estimate of intrafibrillar volume, assuming 80% of mineral is within fibrils: 0.73 cc/g dry collagen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409480
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