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  • 1
    Electronic Resource
    Electronic Resource
    Impaired myocardial angiogenesis and ischemic cardiomyopathy in mice lacking the vascular endothelial growth factor isoforms VEGF 164 and VEGF 188 (1999)
    [s.l.] : Nature America Inc.
    Nature medicine 5 (1999), S. 495-502 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The gene for vascular endothelial growth factor (VEGF) encodes three spliced isoforms. Although the heparin binding capacities of these isoforms differ, little is known about their differential functions in vivo. We generated mice expressing exclusively the VEGF120 isoform (VEGF 120/120 mice) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/8379
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Heterogeneity of smooth muscle-associated proteins in mammalian brain microvasculature (1995)
    Springer
    Cell & tissue research 279 (1995), S. 393-403 
    Details
    ISSN: 1432-0878
    Keywords: Pericytes ; Smooth muscle ; Endothelium ; Brain capillaries ; Pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In the brain, the microvascular system is composed of endothelial cells surrounded by a layer of pericytes. The lack of smooth muscle cells in this tissue suggests that any contractile function must be performed by one or both of these cell types. The present study was undertaken in order to identify cells in terminal blood vessels that contain smooth muscle-like contractile machinery. Endothelial cells were reactive with antibodies against smooth muscle myosin but showed no other smooth muscle-related features. In contrast, pericytes of intact microvessels showed a pattern of protein expression similar to that of smooth muscle cells. Pericytes also behaved in tissue culture like cultured smooth muscle cells, with regard to the changes in expression of smooth muscle-related proteins. These data confirm the close relationship between smooth muscle cells and pericytes, and point to their contractile function in the brain microvessels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318497
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Heterogeneity of smooth muscle-associated proteins in mammalian brain microvasculature (1995)
    Springer
    Cell & tissue research 279 (1995), S. 393-403 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Pericytes ; Smooth muscle ; Endothelium ; Brain capillaries ; Pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. In the brain, the microvascular system is composed of endothelial cells surrounded by a layer of peri-cytes. The lack of smooth muscle cells in this tissue suggests that any contractile function must be performed by one or both of these cell types. The present study was undertaken in order to identify cells in terminal blood vessels that contain smooth muscle-like contractile machinery. Endothelial cells were reactive with antibodies against smooth muscle myosin but showed no other smooth muscle-related features. In contrast, pericytes of intact microvessels showed a pattern of protein expression similar to that of smooth muscle cells. Pericytes also behaved in tissue culture like cultured smooth muscle cells, with regard to the changes in expression of smooth muscle-related proteins. These data confirm the close relationship between smooth muscle cells and peri-cytes, and point to their contractile function in the brain microvessels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050296
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Cardiomyocyte Cytoskeleton and Myofibrillogenesis in Healthy and Diseased Heart (2000)
    Springer
    Heart failure reviews 5 (2000), S. 259-269 
    Details
    ISSN: 1573-7322
    Keywords: myofibrillogenesis ; muscle cytoskeleton ; in-tercalated disk ; dilated cardiomyopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The unique cytoarchitecture of cardiomyocytes arises by complex interactions of different filamentous structures of the cytoskeleton. Intermediate filaments of the non-sarcomeric cytoskeleton are not essential for development but important for maintenance of myofibrils. Myofibrils consist of contractile proteins involved in force generation and the muscle cytoskeleton framework. The latter is essential for proper assembly and maintenance as well as for interaction with other cardiomyocytes or the extracellular matrix, thus being involved in force transmission. The information for sarcomere assembly is encoded in the proteins and some domains essential for faithful incorporation have been identified by epitope tagging experiments. Many KO mutations result in embryonic lethal phenotypes and new techniques e.g. using cardiomyocytes derived from ES cell-lines will have to be developed that allow to study such mutations in cardiomyocytes rather than whole organisms. Alterations in the expression levels of several proteins of the muscle cytoskeleton or impairment of their function by point mutations can result in increased mechanical stress in the cardiomyocytes which finally leads to cellular responses such as the development of dilated cardiomyopathy (DCM). MLP (muscle-LIM-protein) deficient mice develop DCM and changes in the mechanical coupling of cardiomyocytes result in alterations at the intercalated disks and enhanced accumulation of adherens junction proteins. Therefore, controlled interactions between proteins of the muscle cytoskeleton and contractile proteins are essential to ensure proper cardiac function and a more detailed insight in these processes might provide new tools to improve the contractile efficiency of the cardiomyocytes and thus working output in cardiomyopathies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009861504264
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  • 5
    Electronic Resource
    Electronic Resource
    Thick filament assembly occurs after the formation of a cytoskeletal scaffold (1999)
    Springer
    Journal of muscle research and cell motility 20 (1999), S. 569-579 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The development of myofibrils involves the formation of contractile filaments and their assembly into the strikingly regular structure of the sarcomere. We analysed this assembly process in cultured human skeletal muscle cells and in rat neonatal cardiomyocytes by immunofluorescence microscopy using antibodies directed against cytoskeletal and contractile proteins. In particular, the question in which temporal order the respective proteins are integrated into developing sarcomeres was addressed. Although sarcomeric myosin heavy chain is expressed as one of the first myofibrillar proteins, its characteristic A band arrangement is reached at a very late stage. In contrast, titin, then myomesin and finally C-protein (MyBP-C) gradually form a regularly arranged scaffold on stress fiber-like structures (SFLS), on non-striated myofibrils (NSMF) and on nascent striated myofibrils (naSMF). Immediately subsequent to the completion of sarcomere cytoskeleton formation, the labeling pattern of myosin changes from the continuous staining of SFLS to the periodic staining characteristic for mature myofibrils. This series of events can be seen most clearly in the skeletal muscle cell cultures and – probably due to a faster developmental progression – less well in cardiomyocytes. We therefore conclude that the correct assembly of a cytoskeletal scaffold is a prerequisite for correct thick filament assembly and for the integration of the contractile apparatus into the myofibril.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005569225773
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    Paper (German National Licenses)
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