Structure, function and expression of type V collagen.
Item
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Title
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Structure, function and expression of type V collagen.
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Identifier
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AAI9431348
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identifier
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9431348
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Creator
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Andrikopoulos, Konstantinos Ioannou.
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Contributor
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Adviser: Francesco Ramirez
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Date
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1994
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Genetics | Biology, Molecular | Biology, Cell
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Abstract
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The correct assembly of the fibrillar collagen networks plays a critical role in animal morphogenesis. Type V collagen is a minorly represented member of the fibrillar collagen family; it is believed that one of its functions is to regulate type I collagen fibrillogenesis. This study was designed to prove the validity of this hypothesis. We first cloned the mouse pro-{dollar}\alpha{dollar}2(V) collagen gene (col5a2) and examined its developmental expression pattern. During early embryonic stages, col5a2 expression is low and diffusely distributed in the peritoneal membranes, intestinal and craniofacial mesenchymes. At later stages, col5a2 gene expression is higher and more restricted to the primary ossified regions, perichondrium, joints, tendon, atrioventicular valve of the heart and selected portions of the head. Thus, this analysis provided further indirect evidence for the postulated cooperativity of types I and V collagens in the fibrillogenesis of non-cartilaginous matrices. In order to directly confirm this relationship, we targeted the col5a2 exon coding for the N-telopeptide by homologous recombination in mouse embryonic stem cells. Homozygous mice present a severe kyphotic phenotype, substantial skin fragility, and a defective corneal stroma. These abnormalities were correlated to ultrastructural deficiencies in type I collagen fibrillogenesis. We found that type I collagen fibrils of homozygous animals are thicker and more disorganized than those of wild type littermates. Altogether, the data provide proof that type V collagen plays a critical role in regulating the growth and tri-dimensional organization of type I collagen fibrils.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
