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Nucleic Acids Research, 1984, Vol. 12, No. 24 9383-9394
© 1984

MOLECULAR BIOLOGY

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

Helen R. Loidl1, Jane M. Brinker1, Mary May2, Taina Pihlajaniemi3, Scott Morrow2, Joel Rosenbloom2 and Jeanne C. Myers1,4,*

1Connective Tissue Research Institute, University of Pennsylvania Philadelphia, PA 19104 2School of Dental Medicine, University of Pennsylvania Philadelphia, PA 19104 3Dept. Biochemistry, Rutgers Medical School Piscataway, NJ 08854 4Dept. Medicine and Human Genetics, University of Pennsylvania Philadelphia, PA 19104, USA

*To whom correspondence should be addressed: Connective Tissue Research Institute and University of Pennsylvania 3624 Market Street, Philadelphia, PA 19104

Received September 10, 1984. Accepted November 14, 1984.

Two human cDNA libraries prepared from normal fibroblast (GM3348) and rhabdomyosarcoma (CCL136) mRNAs were screened under cross hybridization conditions with a genomic fragment coding for exons 2 and 3 of the avian type III procollagen COOH-propeptide (Yamada, Y., Mudryj, M., Sullivan, M. and deCrombrugghe, B. (1983) J. Biol . Chem. 258, 2758–2761). One cDNA clone containing a 1.12 kb insert was isolated from the CCL136 library and later used to identify a GM3348 derived clone with a 2.4 kb insert. Comparison of the human and avian type III C-terminal propeptides revealed much more divergence in the first 54 amino acids following the terminal cysteine of the triple helical region than is present in the {alpha}1(I) and {alpha}2(I) procollagen chains of these species. Analysis of poly (A+) RNA from normal human fibroblast and tumor cell lines showed that they differed greatly in the relative amounts of {alpha}1(I), {alpha}2(I), and {alpha}1(III) mRNAs. Furthermore, as we previously reported for the {alpha}1(I) and {alpha}2(I) transcripts, multiple mRNAs also hybridize to the cloned {alpha}1(III) DNA.


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