New members of the collagen superfamily

Mayne, Richard; Brewton, Randolph G.

doi:10.1016/0955-0674(93)90039-s

Cited by 132 publications

(68 citation statements)

References 52 publications

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“…This is in agreement with earlier data of the prowl (XI) chain being able to associate with type V collagen chains in bone [8,23]. We have previously demonstrated by histomorphometry that the volume of the cartilaginous component in the fracture calluses of Dell mice is markedly reduced when compared with the control mice [5].…”

supporting

confidence: 93%

“…Clearly such information is needed for understanding the complex changes in the extracellular matrix during the fracture healing process. In this study we determined the mRNA levels for all three chains of type IX collagen, for the prowl chain of type XI collagen found in both cartilage and bone [8], and for the ~2 chain of type VI collagen, a ubiquitously expressed microfibrillar collagen [9]. We also analyzed the calluses for the presence of the alternatively processed/transcribed forms of proccl(II) and c~I(IX) collagen mRNAs.…”

Section: Introductionmentioning

confidence: 99%

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Expression of type VI, IX and XI collagen genes and alternative splicing of type II collagen transcripts in fracture callus tissue in mice

1995

FEBS Letters

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The levels of six mRNAs coding for constituent achains of three minor collagens of cartilage were analyzed in an experimental fracture model in normal and transgenic Dell mice harboring a deletion mutation of exon 7 in the type II collagen gene. Reduced and retarded chondrogenesis in Dell mice was evident in callus samples as reduced mRNA levels for the cartilage specific type IX and XI collagens at days 7 and 9 of fracture healing. Analysis of the calluses for alternative splicing of proal(II) collagen mRNA also suggested retarded chondrogenesis in Dell calluses. Another developmentally regulated step in limb development, a switch between alternative promoters of the al(IX) collagen gene, was also seen during fracture healing but was less obvious in Dell calluses. Finally, the current data suggest that the abnormality in bone remodelling in Dell mice involves activation of the genes coding for al(XI) and a2(VI) collagens.

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supporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Expression of type VI, IX and XI collagen genes and alternative splicing of type II collagen transcripts in fracture callus tissue in mice

1995

FEBS Letters

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“…In vertebrates, the matrix consists of collagens [4,5], proteoglycans [6], and other glycosylated and non-glycosylated proteins [1]. A common feature of many matrix macromolecules is their ability to interact with other components of the matrix during the formation of various supra-molecular aggregates, e.g.…”

Section: Introductionmentioning

confidence: 99%

Tyrosine‐rich acidic matrix protein (TRAMP) is a tyrosine‐sulphated and widely distributed protein of the extracellular matrix

et al. 1994

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Tyrosine-rich acidic matrix protein (TRAMP; 22 kDa extracellular matrix protein; dermatopontin) is a protein that co-purifies with lysyl oxidase and with dermatan sulphate proteoglycans, with possible functions in cell-matrix interactions and matrix assembly. Using a rabbit polyclonal antiserum raised against porcine TRAMP, which cross-reacts with both the human and murine forms of the protein, we show by immunoblotting that TRAMP has a widespread tissue distribution, including skin, skeletal muscle, heart, lung, kidney, cartilage and bone. In cultures of human skin fibroblasts, TRAMP incorporates both [35S]sulphate and [3H]tyrosine and is secreted into the medium, as shown by immunoprecipitation. Amino acid analysis of immunoprecipitated TRAMP demonstrates that many of the tyrosine residues in TRAMP are sulphated.

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“…Type XII collagen was initially described based on a cDNA clone from chick embryo fibroblasts (13). Type XII collagen molecules are homotrimers consisting of three identical ␣1(XII) chains with two triple-helical (COL1 and COL2) domains and three non-triplehelical (NC1, NC2, and NC3) domains (6,7). It is mainly localized in tissues containing type I collagen, such as tendons, bones, ligaments, dermis, and blood vessel walls (14 -16), but it is also detected in cartilage, which contains type II collagen as its major constituent (17).…”

mentioning

confidence: 99%

Involvement of Prolyl 4-Hydroxylase in the Assembly of Trimeric Minicollagen XII

Mazzorana

Snellman

Kivirikko

et al. 1996

Journal of Biological Chemistry

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We have shown previously that hydroxylation played a critical role in the trimer assembly and disulfide bonding of the three constituent ␣ chains of a minicollagen composed of the extreme C-terminal collagenous (COL1) and noncollagenous (NC1) domains of type XII collagen in HeLa cells (Mazzorana, M., Gruffat, H., Sergeant, A., and van der Rest, M. (1993) J. Biol. Chem. 268, 3029 -3032). We have further characterized the involvement of prolyl 4-hydroxylase in the assembly of the three ␣ chains to form trimeric disulfide-bonded type XII minicollagen in an insect cell expression system. For this purpose, type XII minicollagen was produced in insect cells from baculovirus vectors, alone or together with wild-type human prolyl 4-hydroxylase or with the human enzyme mutated in the catalytic site of its ␣ or ␤ subunits or with the individual ␣ or ␤ subunits. When type XII minicollagen was produced alone, negligible amounts of disulfide-bonded trimers were found to be produced by the cells. However, coproduction of the collagen with the two subunits of the wild-type human enzyme dramatically increased the amount of disulfidebonded trimeric type XII minicollagen molecules. In contrast, coproduction of the collagen with ␣ subunits that had a mutation completely inactivating the human enzyme failed to enhance the trimer assembly. These results directly show that an active prolyl 4-hydroxylase is required for the assembly of disulfide-bonded trimers of type XII minicollagen.

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New members of the collagen superfamily

Cited by 132 publications

References 52 publications

Expression of type VI, IX and XI collagen genes and alternative splicing of type II collagen transcripts in fracture callus tissue in mice

Expression of type VI, IX and XI collagen genes and alternative splicing of type II collagen transcripts in fracture callus tissue in mice

Tyrosine‐rich acidic matrix protein (TRAMP) is a tyrosine‐sulphated and widely distributed protein of the extracellular matrix

Involvement of Prolyl 4-Hydroxylase in the Assembly of Trimeric Minicollagen XII

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