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. 1989 Sep 1;109(3):1371–1379. doi: 10.1083/jcb.109.3.1371

Expression of mRNAs coding for the alpha 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II, and III

PMCID: PMC2115744  PMID: 2768343

Abstract

This paper describes the topographic distribution of the multiple mRNAs coding for a novel human short-chain collagen, the alpha 1 chain of type XIII collagen. To identify the tissues and cells expressing these mRNAs, human fetal tissues of 15-19 gestational wk were studied by Northern and in situ hybridizations. The distribution pattern of the type XIII collagen mRNAs was compared with that of fibrillar collagen types I, II, and III using specific human cDNA probes for each collagen type. Northern hybridization showed the bone, cartilage, intestine, skin, and striated muscle to contain mRNAs for type XIII collagen. An intense in situ hybridization signal was obtained with the type XIII collagen cDNAs in the epidermis, hair follicles, and nail root cells of the skin, whereas the fibrillar collagen mRNAs were detected in the dermis. Cells in the intestinal mucosal layer also appeared to contain high levels of alpha 1(XIII) collagen mRNAs, but contained none of the fibrillar collagen mRNAs. In the bone and striated muscle, alpha 1(XIII) collagen mRNAs were detected in the mesenchymal cells forming the reticulin fibers of the bone marrow and endomycium. The hybridization signal obtained with the alpha 1(XIII) collagen cDNA probe in cartilaginous areas of the growth plates was similar, but less intense, to that obtained with the type II collagen probe. A clear hybridization signal was also detected at the (pre)articular surfaces and at the margins of the epiphyses, whereas it was weaker in the resting chondrocytes in the middle of the epiphyses. The brain, heart, kidney, liver, lung, placenta, spleen, testis, tendon, and thymus did not appear to contain alpha 1(XIII) collagen mRNAs.

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Selected References

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  1. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  2. Elima K., Vuorio T., Vuorio E. Determination of the single polyadenylation site of the human pro alpha 1(II) collagen gene. Nucleic Acids Res. 1987 Nov 25;15(22):9499–9504. doi: 10.1093/nar/15.22.9499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ellender G., Feik S. A., Carach B. J. Periosteal structure and development in a rat caudal vertebra. J Anat. 1988 Jun;158:173–187. [PMC free article] [PubMed] [Google Scholar]
  4. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  5. Gibson G. J., Beaumont B. W., Flint M. H. Synthesis of a low molecular weight collagen by chondrocytes from the presumptive calcification region of the embryonic chick sterna: the influence of culture with collagen gels. J Cell Biol. 1984 Jul;99(1 Pt 1):208–216. doi: 10.1083/jcb.99.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gordon M. K., Gerecke D. R., Olsen B. R. Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6040–6044. doi: 10.1073/pnas.84.17.6040. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Miller E. J., Gay S. The collagens: an overview and update. Methods Enzymol. 1987;144:3–41. doi: 10.1016/0076-6879(87)44170-0. [DOI] [PubMed] [Google Scholar]
  8. Mäkelä J. K., Raassina M., Virta A., Vuorio E. Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain. Nucleic Acids Res. 1988 Jan 11;16(1):349–349. doi: 10.1093/nar/16.1.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Pihlajaniemi T., Myllylä R., Seyer J., Kurkinen M., Prockop D. J. Partial characterization of a low molecular weight human collagen that undergoes alternative splicing. Proc Natl Acad Sci U S A. 1987 Feb;84(4):940–944. doi: 10.1073/pnas.84.4.940. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Rowe D. W., Moen R. C., Davidson J. M., Byers P. H., Bornstein P., Palmiter R. D. Correlation of procollagen mRNA levels in normal and transformed chick embryo fibroblasts with different rates of procollagen synthesis. Biochemistry. 1978 May 2;17(9):1581–1590. doi: 10.1021/bi00602a001. [DOI] [PubMed] [Google Scholar]
  11. Sandberg M., Autio-Harmainen H., Vuorio E. Localization of the expression of types I, III, and IV collagen, TGF-beta 1 and c-fos genes in developing human calvarial bones. Dev Biol. 1988 Nov;130(1):324–334. doi: 10.1016/0012-1606(88)90438-1. [DOI] [PubMed] [Google Scholar]
  12. Sandberg M., Mäkelä J. K., Multimäki P., Vuorio T., Vuorio E. Construction of a human pro alpha 1(III) collagen cDNA clone and localization of type III collagen expression in human fetal tissues. Matrix. 1989 Mar;9(2):82–91. doi: 10.1016/s0934-8832(89)80025-3. [DOI] [PubMed] [Google Scholar]
  13. Sandberg M., Vuorio E. Localization of types I, II, and III collagen mRNAs in developing human skeletal tissues by in situ hybridization. J Cell Biol. 1987 Apr;104(4):1077–1084. doi: 10.1083/jcb.104.4.1077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sandberg M., Vuorio T., Hirvonen H., Alitalo K., Vuorio E. Enhanced expression of TGF-beta and c-fos mRNAs in the growth plates of developing human long bones. Development. 1988 Mar;102(3):461–470. doi: 10.1242/dev.102.3.461. [DOI] [PubMed] [Google Scholar]
  15. Schmid T. M., Linsenmayer T. F. Developmental acquisition of type X collagen in the embryonic chick tibiotarsus. Dev Biol. 1985 Feb;107(2):373–381. doi: 10.1016/0012-1606(85)90319-7. [DOI] [PubMed] [Google Scholar]
  16. Tikka L., Pihlajaniemi T., Henttu P., Prockop D. J., Tryggvason K. Gene structure for the alpha 1 chain of a human short-chain collagen (type XIII) with alternatively spliced transcripts and translation termination codon at the 5' end of the last exon. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7491–7495. doi: 10.1073/pnas.85.20.7491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Timpl R., Dziadek M. Structure, development, and molecular pathology of basement membranes. Int Rev Exp Pathol. 1986;29:1–112. [PubMed] [Google Scholar]
  18. Vuorio E. Connective tissue diseases: mutations of collagen genes. Ann Clin Res. 1986;18(5-6):234–241. [PubMed] [Google Scholar]
  19. Vuorio T., Mäkelä J. K., Kähäri V. M., Vuorio E. Coordinated regulation of type I and type III collagen production and mRNA levels of pro alpha 1(I) and pro alpha 2(I) collagen in cultured morphea fibroblasts. Arch Dermatol Res. 1987;279(3):154–160. doi: 10.1007/BF00413250. [DOI] [PubMed] [Google Scholar]

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