Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis
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چکیده
منابع مشابه
Effects of decorin proteoglycan on fibrillogenesis, ultrastructure, and mechanics of type I collagen gels.
The proteoglycan decorin is known to affect both the fibrillogenesis and the resulting ultrastructure of in vitro polymerized collagen gels. However, little is known about its effects on mechanical properties. In this study, 3D collagen gels were polymerized into tensile test specimens in the presence of decorin proteoglycan, decorin core protein, or dermatan sulfate (DS). Collagen fibrillogene...
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Tenascin-X is an extracellular matrix protein initially identified because the gene encoding it overlaps with the human CYP21B gene. Because studies of gene and protein function of other tenascins had been poorly predictive of essential functions in vivo, we used a genetic approach that critically relied on an understanding of the genomic locus to uncover an association between inactivating ten...
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Following removal of most of the telopeptide regions with pepsin, bovine dermal collagen gelled more slowly to form fibrils with a weak banding pattern. The reduction in gelling rate reflected an increase in the length of the nucleation phase and a lower rate of turbidity increase during the growth phase; the activation energy of both phases was increased. Lanthanide ions, phosphate, or, to a l...
متن کاملTenascin-C expression by fibroblasts is elevated in stressed collagen gels
Chick embryo fibroblasts cultured on a collagen matrix exert tractional forces leading to the contraction of unrestrained, floating collagen gels and to the development of tension in attached, restrained gels. On a restrained, attached collagen gel the fibroblasts synthesize large quantities of tenascin-C, whereas in a floating, contracting gel tenascin-C synthesis is decreased. This regulation...
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ژورنال
عنوان ژورنال: Biophysical Chemistry
سال: 2010
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2009.12.011