Molecular cloning and carboxyl-propeptide analysis of human type III procollagen

Loidl, H R; Brinker, Jane M.; May, Mary; Pihlajaniemi, Taina; Morrow, Scott D.; Rosenbloom, Joel; Myers, Jeanne C.

doi:10.1093/nar/12.24.9383

Cited by 104 publications

(54 citation statements)

References 38 publications

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“…The two clones used for in situ hybridization were isolated from a normal fibroblast cDNA library (24). Restriction endonuclease analysis of the al(III) and a2(V) cDNA clones is shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…1. E6 contains a 2.4-kilobase (kb) insert coding for =430 amino acids of the al(III) triple-helical region, the entire COOH-terminal propeptide, and several hundred nucleotides of the 3' untranslated region (24). Nucleotide and derived amino acid sequences of the COOH end of the a chain were obtained from the internal 385-bp Pst I fragment ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Preparation and screening of the cDNA library have been described (24). The source of template mRNA was a normal human fibroblast cell line, GM3348, obtained from the Human Genetic Mutant Cell Repository (Camden, NJ).…”

Section: Methodsmentioning

confidence: 99%

“…We have characterized cDNA clones encoding part of the al(III) and a2(V) procollagen chains (24,25) and compared the derived amino acid sequences with those reported for the human al(I) and a2(I) polypeptides (26,27). Immediately obvious is the maintenance of most charged positions in the uninterrupted Gly-Xaa-Yaa region and conserved functional domains within the carboxyl propeptides, indicating that these are closely related structural macromolecules.…”

Section: Introductionmentioning

confidence: 99%

“…Since the collagens seem to have arisen by duplication of a 54-base-pair (bp) primordial unit (21), it had been speculated that these may be the two main chromosomal sites where different members of the procollagen gene family reside. However, recent chromosomal mapping of al(II) genomic sequences (22) has identified chromosome 12 as a third procollagen locus (23), suggesting dispersion for at least the interstitial procollagen genes.We have characterized cDNA clones encoding part of the al(III) and a2(V) procollagen chains (24,25) and compared the derived amino acid sequences with those reported for the human al(I) and a2(I) polypeptides (26,27). Immediately obvious is the maintenance of most charged positions in the uninterrupted Gly-Xaa-Yaa region and conserved functional domains within the carboxyl propeptides, indicating that these are closely related structural macromolecules.…”

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Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Emanuel¹,

Cannizzaro²,

Seyer³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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The multigene procollagen family encodes probably >20 genetically distinct but structurally related polypeptide chains. Recent characterization of human procollagen clones has allowed determination of functional domains within the proteins, genomic organization, and chromosomal location. Previously, we assigned the coordinately expressed type I genes (al and a2) to chromosomes 17 and 7, respectively, and now other investigators have mapped the type II gene to chromosome 12 [Strom, C. M., Eddy, R. L. & Shows, T. B. (1984) Somatic CeU Genet. 10, 651-655]. Recently, we isolated cDNA clones encoding the fourth interstitial procollagen, type III, and the a2 chain of the type V cytoskeletal components. To determine whether these genes were clustered with al(I), a2(I), or al(II) or were further dispersed in the genome, in situ hybridization of the a1(Ill) and a2(V) probes to metaphase chromosomes was carried out. Here we report a fourth autosome with procollagen gene loci but the first cytological evidence for linkage. By using normal and translocated cell lines, our results show that both the ail(llI) and a2(V) procollagen genes map to the q24.3--q31 region of chromosome 2.The procollagens constitute a group of proteins responsible for the structural integrity of connective tissue (see refs. 1-4 for reviews). The polypeptide chains are generally composed of a large collagenous domain with the repeating Gly-X-Y sequence flanked by smaller amino-and carboxyl-extension peptides. More than five major and five minor types of collagen have been identified, which consist of one, two, or three different chains folded into a triple-helical molecule (1-9). While several types have a unique tissue distribution (II in cartilage and IV in basement membrane), others (I, III, and V) are usually coexpressed but at different levels depending on the cell type (1-4). We have been studying the structure and regulation of these latter three collagens normally found together in the proportion I > III > V. Whereas type I is the major collagen species in skin, bone, tendon, placenta, lung, and liver, type III appears to predominate in blood vessels and internal organs (1-4, 10, 11). Little is currently known about the minor component, type V, except for its distribution in pericellular regions (12).Isolation of DNA clones encoding different procollagen chains has allowed determination of the amino acid sequence, genomic organization, and chromosomal assignment (see refs. 4 and 13 for reviews). For example, the sizes of the al(I) and a2(I) genes (13-15) are inversely proportional to the 2:1 ratio of the mRNAs in cultured fibroblasts, reflecting the subunit composition of type I collagen (16). Interestingly, these two carefully regulated coding units, both interrupted by -50 introns, are located on the long arm of chromosomes 17 and 7, respectively, as determined from somatic cell and in situ hybridization (17)(18)(19)(20). Since the collagens seem to have arisen by duplication of a 54-base-pair (bp) primordial unit (21), it had been ...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Emanuel¹,

Cannizzaro²,

Seyer³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Aberrant type I and type III collagen gene expression in human breast cancerin vivo

et al. 1998

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Type I procollagen synthesis is regulated by steroids and related hormones in human osteosarcoma cells

Jukkola

Risteli

et al. 1998

J. Cell. Biochem.

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Change in the synthesis of type I collagen, the major extracellular matrix component of skin and bone, are associated with normal growth, tissue repair processes, and several pathological conditions. Expression of the COL 1A1 gene is regulated by transcriptional and post-transcriptional mechanisms. However, the hormonal regulation of type I collagen synthesis in human bone has not been well characterized. We have studied the influence of calcitriol, dexamethasone, retinoic acid, and estradiol on the COL 1A1 gene expression by determining the secretion of the C-terminal propeptide (PICP) and the levels of alpha 1(I) procollagen mRNA in cultured human MG-63 and SaOs-2 osteoblast-like osteosarcoma cells. Similar experiments were also performed with respect to expression of the nuclear proto-oncogenes, c-fos and c-jun, in MG-63 cells. In MG-63 cells, calcitriol stimulated the synthesis and secretion of PICP. The alpha 1(I) procollagen mRNA level was elevated with no effect on message stability, indicating a transcriptional mechanism of regulation. In contrast, dexamethasone treatment was accompanied by an accelerated rate of alpha 1(I) procollagen mRNA turnover, observed as decreased amounts of the message and the secreted PICP, implying a posttranscriptional regulation. Retinoic acid, in turn, decreased the levels of alpha 1(I) procollagen mRNA and secreted PICP by slowing down transcription of the COL1A1 gene without any effect on message stability. The ability of these hormones to regulate the alpha 1(I) transcripts was sensitive to puromycin treatment, suggesting an involvement of an induced mediator protein in the action of the hormones on the COL1A1 gene. Both dexamethasone and calcitriol rapidly but transiently increased the expression of the c-fos and c-jun proto-oncogenes. Neither proto-oncogene responded to retinoic acid treatment with significant changes in mRNA levels. Estradiol treatment was found to have no influence on type I procollagen synthesis. In SaOs-2 cells, which are not as well differentiated as the MG-63 cells, calcitriol and dexamethasone did not influence type I procollagen synthesis. Retinoic acid as well as estradiol reduced collagen gene expression in these cells. These findings suggest that hormonal effects on type I procollagen synthesis may depend on the maturational state of the osteoblastic cells that express different regulatory factors and receptors, resulting in, in each case, a finely adjusted rate of gene expression.

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Molecular cloning and carboxyl-propeptide analysis of human type III procollagen

Cited by 104 publications

References 38 publications

Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Aberrant type I and type III collagen gene expression in human breast cancerin vivo

Type I procollagen synthesis is regulated by steroids and related hormones in human osteosarcoma cells

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