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  • 1
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pesin-resistant heterotrimers ; disulfide bonds ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Collagen biosynthesis is a complex process that begins with the association of three procollagen chains. A series of conserved intra- and interchain disulfide bonds in the carboxyl-terminal region of the procollagen chains, or C-propeptide, has been hypothesized to play an important role in the nucleation and alignment of the chains. We tested this hypothesis by analyzing the ability of normal and cysteine-mutated pro-α2(I) chains to assemble into type I collagen heterotrimers when expressed in a cell line (D2) that produces only endogenous pro-α1(I). Pro-α2(I) chains containing single or double cysteine mutations that disrupted individual intra- or interchain disulfide bonds were able to form pepsin resistant type I collagen with pro-α1(I), indicating that individual disulfide bonds were not critical for assembly of the pro-α2(I) chain with pro-α1(I). Pro-α2(I) chains containing a triple cysteine mutation that disrupted both intrachain disulfide bonds were not able to form pepsin resistant type I collagen with pro-α1(I). Therefore, disruption of both pro-α2(I) intrachain disulfide bonds prevented the production and secretion of type I collagen heterotrimers. Although none of the individual disulfide bonds is essential for assembly of the procollagen chains, the presence of at least one intrachain disulfide bond may be necessary as a structural requirement for chain association or to stabilize the protein to prevent intracellular degradation. J.Cell. Biochem. 71:233-242, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pepsin-resistant heterotrimers ; interspecies collagen molecule ; thermal stability ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Procollagen (Type I) contains a noncollagenous COOH-terminal propeptide (C-propeptide) hypothesized to be important in directing chain association and alignment during assembly. We previously expressed human pro-α2(I) cDNA in rat liver epithelial cells, W8, that produce only pro-α1(I) trimer collagen (Lim et al. [1994] MatrixBiol. 14: 21-30). In the resulting cell lines, α2(I) assembled with α1(I) forming heterotrimers. Using this cell system, we investigated the importance of the COOH-terminal propeptide sequence of the pro-α2(I) chain for normal assembly of type I collagen. Full-length human pro-α2(I) cDNA was cloned into expression vectors with a premature stop signal eliminating the final 10 amino acids. No triple-helical molecules containing α2(I) were detected in transfected W8 cells, although pro-α2(I) mRNA was detected. Additional protein analysis demonstrated that these cells synthesize small amounts of truncated pro-α2(I) chains detected by immunoprecipitation with a pro-α2(I) antibody. In addition, since the human-rat collagen was less thermostable than normal intraspecies collagen, wild-type and C-terminal truncated mouse cDNAs were expressed in mouse D2 cells, which produced only type I trimers. Results from both systems were consistent, suggesting that the last 10 amino acid residues of the pro-α2(I) chain are important for formation of stable type I collagen. J. Cell. Biochem. 71:216-232, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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