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  • 1
    Electronic Resource
    Electronic Resource
    Rat liver fat-storing cell lines express sarcomeric myosin heavy chain mRNA and protein (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 26 (1993), S. 125-132 
    Details
    ISSN: 0886-1544
    Keywords: lipocytes ; liver cirrhosis ; myofibroblasts ; myosin gene ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fat-storing cells (FSC, lipocytes, or Ito cells) of liver store vitamin A and are the main producers of extracellular matrix in normal and cirrhotic liver. During liver injury, FSC undergo an activation process characterized by a decrease in vitamin A storage and an increase in cell proliferation and extracellular matrix deposition. This activation process also occurs upon culturing FSC from normal liver. In contrast to most cells of nonmuscle origin, activated FSC express two cytoskeletal proteins normally found in muscle, desmin, and smooth muscle α-actin. Based on their strategic perisinusoidal location, it has been hypothesized that FSC play a role in regulating blood flow. However, the nature of the contractile elements involved in this process remains to be determined. In this communication we demonstrate the presence of a sarcomeric myosin in proteins solubilized from liver biomatrix. In addition we demonstrate the expression of sarcomeric myosin heavy chain (MHC) mRNA and protein in two FSC clones derived from a CCl4-cirrhotic rat liver (CFSC). Through cloning the cDNA corresponding to the MHC gene expressed in these cells we demonstrate that it encodes fast IId skeletal MHC and thus represents a marker normally seen in adult muscle. The unexpected expression of an adult stage skeletal muscle molecular motor in FSC from cirrhotic liver is consistent with the proposed specialized contractile capacity of these cells. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970260204
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  • 2
    Electronic Resource
    Electronic Resource
    The three-dimensional structure of motor endplates in different fiber types of rat intercostal muscle (1985)
    Springer
    Cell & tissue research 241 (1985), S. 465-472 
    Details
    ISSN: 1432-0878
    Keywords: Striated muscle ; Muscle fiber type ; Schwann cells ; Motor endplate ; Scanning electron microscopy ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The three-dimensional organization of the motor end plates in the red, white and intermediate striated muscle fibers of the rat intercostal muscle was observed under a field-emission type scanning electron microscope after removal of connective tissue components by HCl hydrolysis. The motor endplate of the white fiber had terminal branches (or axon terminals), which were large, long and thin, and small but numerous nerve swellings (or terminal boutons). The motor endplate of the red fiber had terminal branches, which were small, short and thick, and had large but fewer nerve swellings. The motor endplate of the intermediate fiber was intermediate in size and structure between these two. In detached nerve-ending preparations, primary synaptic grooves with slit-like openings of the junctional folds appeared on the surface of the muscle fibers. The primary synaptic grooves were more developed in the white fiber than in the red fiber, and they were intermediate in the intermediate fiber. The numerical ratio of slit-like openings was 1∶1.8∶3.5 in the red, intermediate and white fiber, respectively. The Schwann cells and their processes were observed on the surface of the motor endplate, with the processes covering the upper orifices of the primary synaptic grooves and sealing the terminal branches. The number of Schwann cells was usually three in the white fiber, two in the intermediate fiber and one in the red fiber.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214564
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  • 3
    Electronic Resource
    Electronic Resource
    High -resolution scanning electron-microscopic studies on the three-dimensional structure of mitochondria and sarcoplasmic reticulum in the different twitch muscle fibers of the frog (1987)
    Springer
    Cell & tissue research 250 (1987), S. 489-497 
    Details
    ISSN: 1432-0878
    Keywords: Muscle cells ; Mitochondria ; Sarcoplasmic reticulum ; Scanning electron microscopy ; Frog (Rana n. nigromaculata)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The three-dimensional structure of the mitochondria and sarcoplasmic reticulum (SR) in the three types of twitch fibers, i.e., the red, white and intermediate skeletal muscle fibers, of the vastus lateralis muscle of the Japanese meadow frog (Rana nigromaculata nigromaculata Hallowell) was examined by high resolution scanning electron microscopy, after removal of the cytoplasmic matrices. The small red fibers have numerous mitochondrial columns of large diameter, while the large white fibers have a small number of mitochondrial columns of small diameter. In the medium-size intermediate fibers, the number and diameter of the mitochondrial columns are intermediate between those of the red and white fibers. In all three types of fibers, the terminal cisternae and transverse tubules form triads at the level of each Z-line. The thick terminal cisternae continue into much thinner flat intermediate cisternae, through a transitional part where a row of tiny indentations can be observed. Numerous slender longitudinal tubules originating from the intermediate cisternae, extend longitudinally or obliquely and form elongated oval networks of various sizes in front of the A-band, then fuse to form the H-band collar (fenestrated collar) around the myofibrils. On the surface of the H-band collar, small fenestrations as well as tiny hollows are seen. The three-dimensional structure of SR is basically the same in all three muscle fiber-types. However, the SR is sparse on the surface of mitochondria, so the mitochondria-rich red fiber has a smaller total volume of SR than the mitochondria-poor white fiber. The volume of SR of the intermediate fiber is intermediate between other the two.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218939
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  • 4
    Electronic Resource
    Electronic Resource
    High resolution scanning electron-microscopic study on the three-dimensional structure of the sarcoplasmic reticulum in the slow (tonic) muscle fibers of the frog, Rana nigromaculata (1989)
    Springer
    Cell & tissue research 255 (1989), S. 669-672 
    Details
    ISSN: 1432-0878
    Keywords: Muscle, striated, skeletal ; Slow muscle fibers ; Muscle cells ; Sarcoplasmic reticulum ; Scanning electron microscopy ; Rana n. nigromaculata (Anura)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The three-dimensional structure of the sarcoplasmic reticulum (SR) in the slow (tonic) fibers of the reclus abdominis muscle of the Japanese meadow frog (Rana nigromaculata nigromaculata Hallowell) was examined by high resolution scanning electron microscopy, after removal of the cytoplasmic matrices by the osmium-DMSO-osmium procedure. The SR forms a repetitive network throughout these fibers. At the level of the Z-line, a slender transverse tubule (T-tubule) runs transversely to the longitudinal axis of the myofibril. Small, spherical or ovoid terminal cisternae couple laterally with the T-tubule at intervals of 0.4–1.0 μm, and form a “terminal cisterna-T-tubule complex” on whose surface tiny indentations are occasionally seen. Each terminal cisterna gives rise to a few sarcotubules that run in various directions, divide frequently and form circular or oval meshes of diverse sizes in front of the A- and I-bands. The sarcotubules usually form small meshes in the middle of the A-band, but occasionally fuse and form a poorly developed H-band (fenestrated) collar.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218807
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  • 5
    Electronic Resource
    Electronic Resource
    Scanning electron-microscopic studies on the three-dimensional structure of sarcoplasmic reticulum in the mammalian red, white and intermediate muscle fibers (1985)
    Springer
    Cell & tissue research 242 (1985), S. 461-467 
    Details
    ISSN: 1432-0878
    Keywords: Muscle cells ; Sarcoplasmic reticulum ; Three-dimensional structure ; Scanning electron microscopy ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The three-dimensional structure of the sarcoplasmic reticulum (SR) in the red, white and intermediate striated muscle fibers of the extensor digitorum longus muscle of the rat was examined under a field-emission type scanning electron microscope after removal of cytoplasmic matrices by the osmium-DMSO-osmium procedure. In all three types of fibers, the terminal cisternae and transverse tubules form triads at the level of the A-I junction. Numerous slender sarcotubules, originating from the A-band side terminal cisternae, extend obliquely or longitudinally and form oval or irregular shaped networks of various sizes in front of the A-band, then become continuous with the tiny mesh (fenestrated collar) in front of the H-band. The A-and H-band SR appears as a single sheet of anastomotic tubules. Numerous sarcotubules, originating from the I-band side terminal cisternae, extend in threedimensional directions and form a multilayered network over the I-band and Z-line regions. At the I-band level, paired transversely oriented mitochondria partly embrace the myofibril. The I-band SR network is poorly developed in the narrow space between the paired mitochondria, but is well developed in places devoid of these mitochondria. The three-dimensional structure of the SR is basically the same in all three muscle fiber-types. However, the SR is sparse on the surface of mitochondria, so the mitochondria-rich red fiber has a much smaller total volume of SR than the mitochondria-poor white fiber. Moreover, the volume of SR of the intermediate fiber is intermediate between the two.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225410
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  • 6
    Electronic Resource
    Electronic Resource
    Scanning electron-microscopic studies on the three-dimensional structure of mitochondria in the mammalian red, white and intermediate muscle fibers (1985)
    Springer
    Cell & tissue research 241 (1985), S. 251-256 
    Details
    ISSN: 1432-0878
    Keywords: Red muscle fibers ; Muscle fiber types ; Mitochondria ; Three-dimensional structure ; Scanning electron microscopy ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The three-dimensional structure and arrangement of mitochondria in the red, white and intermediate striated muscle fibers of the rat were examined under a field-emission type scanning electron microscope after removal of cytoplasmic matrices by means of the Osmium-DMSO-Osmium procedure. Beneath the sarcolemma, spherical or ovoid subsarcolemmal mitochondria show accumulations. The mitochondria are numerous and large in size in the red fibers, intermediate in the intermediate fibers, and few and small in the white fibers. Paired, slender I-band-limited mitochondria were located on both sides of the Z-line and partly embraced the myofibrils at the I-band level; they occurred in all three types of fibers. In the intermyofibrillar spaces, numerous mitochondria formed mitochondrial columns. These columns were classified into two types: 1) thick mitochondrial columns, formed by multiple mitochondria each with an intermyofibrillar space corresponding to one sarcomere in length, and 2) thin mitochondrial columns, established by single mitochondria corresponding to one sarcomere in length. In the red fibers mitochondrial columns were abundant and the ratio of the thick and thin columns was almost the same, while in the intermediate fibers most of the columns belonged to the thin type. The white fibers displayed rare, very thin columns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217168
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  • 7
    Electronic Resource
    Electronic Resource
    Heritable formation of neuroectodermal tumor in transgenic mice carrying the combined e1 region gene of adenovirus type 12 with the deregulated human renin promoter (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 691-700 
    Details
    ISSN: 0730-2312
    Keywords: adenovirus early 1 ; E1 region gene ; human renin promoter ; neuroectodermal tumor ; myc genes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Adenovirus early 1 (E1) region gene products, including E1A and E1B, are required for transcriptional regulation of viral and cellular promoters in infected and transfected culture cells and for transformation of primary rodent cells. Here, we established a line of transgenic mice carrying the E1 region gene of human adenovirus type 12 under the control of the human renin promoter, in which a neuroectodermal tumor derived from retroperitoneal, olfactory, and/or pelvic regions was heritably developed with varying degrees of incidence and the phenotype was successfully passed through six generations. The transgenes were located in the region E2-E3 bands of chromosome 7 with which no genetic linkage to neuroectodermal tumors was previously demonstrated, and expressed only in the tumors but not in another tissue examined. Notably, in addition to the expression of a neural marker gene N-CAM, the three nuclear oncogenes, c-, L-, and N-myc, were coexpressed in the tumors. These results suggest that E1A and E1B are cooperatively involved in the heritable formation of neuroectodermal tumors associated with co-expression of the three sets of myc family genes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240570414
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  • 8
    Electronic Resource
    Electronic Resource
    Humoral hypercalcemia of malignancy: Some enigmas on the clinical features (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 384-391 
    Details
    ISSN: 0730-2312
    Keywords: cancer-associated hypercalcemia ; parathyroid hormone-related peptide (PTHRP) ; nude rat model ; bone remodeling ; gene regulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Humoral hypercalcemia of malignancy (HHM) is a common paraneoplastic syndrome mediated by tumor-derived parathyroid hormone-related peptide (PTHRP), which bears structural and functional similarities to PTH. Thus the clinical features of HHM are very similar to those of primary hyperparathyroidism (1° HPT), a prototype of humoral hypercalcemia caused by PTH. On the other hand, HHM syndrome differs from 1° HPT in several aspects, including serum 1,25(OH)2D levels, acid-base balance, and bone remodeling process, the reason of which remains largely unknown. We approached these questions using a unique animal model of HHM, nude rats implanted with PTHRP-overproducing human carcinomas. In this review we will summarize the results and discuss the implications in understanding the disease mechanism.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240570303
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  • 9
    Electronic Resource
    Electronic Resource
    Transforming growth factor-β1 regulation of bone sialoprotein gene transcription: Identification of a TGF-β activation element in the rat BSP gene promoter (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 501-512 
    Details
    ISSN: 0730-2312
    Keywords: bone sialoprotein ; gene regulation ; mineralized tissues ; TGF-β1 ; transcription ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Transforming growth factor-β (TGF-β) increases steady-state mRNA levels of several extracellular matrix proteins in mineralized connective tissues. Bone sialoprotein (BSP) is a major constituent of the bone matrix, thought to initiate and regulate the formation of mineral crystals. To determine the molecular pathways of TGF-β1 regulation of bone proteins, we have analyzed the effects of the TGF-β1 on the expression of the BSP in the rat osteosarcoma cell line (ROS 17/2.8). TGF-β1 at 1 ng/ml, increased BSP mRNA levels in ROS 17/2.8 cells ∼8-fold; the stimulation was first evident at 3 hr, reached maximal levels at 12 hr and slowly declined thereafter. Since the stability of the BSP mRNA was not significantly affected by TGF-β1, and nuclear “run-on” transcription analyses revealed only a ∼2-fold increase in the transcription of the BSP gene, most of the increase in BSP mRNA appeared to involve a nuclear post-transcriptional mechanism. Moreover, the effects of TGF-β1 were indirect, since the increase in BSP mRNA was abrogated by cycloheximide (28 μg/ml). To identify the site of transcriptional regulation by TGF-β1, transient transfection analyses were performed using BSP gene promoter constructs linked to a luciferase reporter gene. Constructs that included nt -801 to -426 of the promoter sequence were found to enhance transcriptional activity ∼1.8-fold in cells treated with TGF-β1. Within this sequence, ∼500 nt upstream of the transcription start site, a putative TGF-β activation element (TAE) was identified that contained the 5′-portion of the nuclearfactor-1 (NF-1) canonical sequence (TTGGC) overlapping a consensus sequence for activator protein-2 (AP-2). The functionality of the TAE was shown by an increased binding of a nuclear protein from TGF-β1 stimulated cells in gel mobility shift assays and from the attenuation of TGF-β1-induced luciferase activity when cells were co-transfected with a double-stranded TAE oligonucleotide. Competition gel mobility shift analyses revealed that the nuclear protein that binds to the TAE has similar properties to, but is distinct from, NF-1 nuclear protein. These studies have therefore identified a TGF-β activation element (TAE) in the rat BSP gene promoter that mediates the stimulatory effects of TGF-β1 on BSP gene transcription. J. Cell. Biochem. 65:501-512. © 1997 Wiley-Liss Inc.
    Additional Material: 8 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Studies on the cell-cycle dependency of the actions of insulin-like growth factor-I in Balb/c 3T3 cells (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 143 (1990), S. 529-533 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The present study was conducted to determine the cell-cycle dependency of various actions of IGF-I in Balb/c 3T3 cells. When autophosphorylation of the IGF-I receptor was determined in [32P]-labelled cells, IGF-I increased radioactivity in a 100 K-Da phosphoprotein, presumably β-subunit of the IGF-I receptor, both in quiesent and in primed competent cells. Likewise, IGF-I stimulated uptake of [3H]deoxyglucose independent of the cell cycle. In contrast, IGF-I increased calcium entry, radioactivity in [3H]diacylglycerol, and [3H]thymidine incorporation in primed competent cells while these reactions were not induced by IGF-I in quiescent cells. The latter three reactions were attenuated when cells were pretreated with pertussis toxin. These results indicate that some, but not all, of the actions of IGF-I are dependent on the cell cycle in Balb/c 3T3 cells. They also suggest that a pertussis-toxin-sensitive G protein may be involved in the cellcycle-dependent actions of IGF-I.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041430318
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