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Collagen - Wikipedia

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chaperones and enzymes of collagen biosynthesis.

In the early sixties, with the development of electron microscopy, Ross and Benditt (1962, 1965) observed in experimental scurvy a defective progression of labeled proline through the altered cysternae of the rough endoplasmic reticulum to the Golgi and the matrix. These results might be interpreted as impaired processing of collagen and storage of underhydroxylated molecules within the endoplasmic reticulum of fibroblasts. which were stimulated to synthesize collagen during wound healing in the absence of vitamin C. An enormous number of studies performed in the sixties demonstrated that the principal failure in wound healing during vitamin C deficiency is the scarce synthesis and secretion of collagen due to impaired hydroxylation of proline residues in collagen types I and III (Gould and Woessner, 1957; Gould, 1958).

OPC inhibits procollagen secretion from fibroblasts with no effects on cell ..

(2007), Quantitative analysis of the synthesis and secretion of type VII collagen in cultured human dermal fibroblasts with a sensitive sandwich enzyme-linked immunoassay.

Ascorbic Acid and Connective Tissue - Vita Flex

to increase collagen secretion ..

Hydration of keratinocytes modifies important paracrine interactions between keratinocytes and fibroblasts and reduces collagen‐1, which supports the hypothesis that hydration of the epidermis and restoration of water barrier function play an important role in scar formation.">

Hydration of keratinocytes modifies important paracrine interactions between keratinocytes and fibroblasts and reduces collagen‐1, which supports the hypothesis that hydration of the epidermis and restoration of water barrier function play an important role in scar formation.

by ascorbic acid in cultured human fibroblasts, ..

The most abundant proteins in the extracellular matrix are members of the collagen family

The collagen capsule that envelopes infected cells of encapsulated spp. appears to be host derived, yet conveys phylogenetic information that distinguishes major clades within the parasite genus. Debate continues on the origin of the collagen capsule. For instance, collagen gene expression is elevated in infected cells (), and the collagen capsule forms in muscles of nude mice which are compromised for T lymphocyte production and the inflammation that normally infiltrates infected muscle tissue of immunocompetent mammals. Hence, capsule formation does not appear to depend on the host immune response. Nevertheless, the potential remains for contribution to the collagen capsule from fibroblasts that infiltrate around infected cells (). Certainly, the maintenance of this feature throughout an evolutionary lineage suggests a function of basic importance which is lacking from nonencapsulated species.

Hydroxylation of prolyl and lysyl residues may also occur in vitro. Protocollagen, the unhydroxylaled form of collagen, was isolated from cells cultured in the presence of the iron chelator a,a-dipyridyl; moreover, the in vitro hydroxylation of prolyl residues by prolyl hydroxylase was shown to be dependent on the structure of prolyl-containing substrate (Berg and Prockop, 1973a). Therefore, during the formation of procollagen, prolyl and lysyl hydroxylases serve to prepare the molecule to assume the correct conformation necessary for its thermal stability and secretion (Uitto and Prockop, 1974). In fact, underhydroxylated and underglycosylated collagen has been shown to be retained within the cell and to accumulate into large cyloplasmic vacuoles (Koss and Benditt, 1965; Olsen and Prockop, 1974: Harwood et al., 1975). The persistence within the endoplasmic reticulum could be explained, at least partially, by the fact that the underhydroxylated chains undergo a delay in the triple helix formation and may stably associate with protein disulfide isomerase, a multifactoral endoplasmic reticulum resident enzyme, which is the b-subunit of prolyl-4-hydroxylase (Bassuk and Berg, 1989). Therefore, prolyl-4-hydroxylase specifically binds the non-triple helical procollagen chain, playing a role in its intracellular retention (Olsen et al., 1973). Similar retention has been observed in a strain of fibroblasts harboring a deletion of 180 amino acids in the pro-a2(I) chain, which causes a delay in the molecule folding into the triple helix and in collagen maturation (Chessler and Byers, 1992).

High Glucose Stimulates Proliferation and Collagen Type …
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