Abstract

Type IV collagen is a specific and major component of basement membranes. Expression of type IV collagen is developmentally regulated in vivo and is inducible in certain cell cultures and, therefore, provides a valuable model for studies on the control of gene expression. Recently, we isolated cloned cDNA sequences for the Alpha1-chain of mouse type IV collagen. In the present proposal these cDNA clones will be used to isolate genes coding for mouse type IV collagen. Characterization of these genes will help to determine the amino acid sequence and elucidate structural features of type IV collagen chains as well as provide valuable new information about the evolution of collagen genes in general. It will also open up studies for the control of their tissue specific and developmentally regulated expression. We will examine the control of type IV collagen gene expression in a model system using F9 mouse teratocarcinoma cell cultures and DNA-mediated gene transfer techniques.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM034090-04
Application #
3284558
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1984-07-01
Project End
1988-06-30
Budget Start
1987-07-01
Budget End
1988-06-30
Support Year
4
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of Medicine & Dentistry of NJ
Department
Type
Schools of Medicine
DUNS #
622146454
City
Piscataway
State
NJ
Country
United States
Zip Code
08854

  Publications

Tanaka, S; Kaytes, P; Kurkinen, M (1993) An enhancer for transcription of collagen IV genes is activated by F9 cell differentiation. J Biol Chem 268:8862-70
Otani, Y; Quinones, S; Saus, J et al. (1990) Cycloheximide induces stromelysin mRNA in cultured human fibroblasts. Eur J Biochem 192:75-9
Buttice, G; Kaytes, P; D'Armiento, J et al. (1990) Evolution of collagen IV genes from a 54-base pair exon: a role for introns in gene evolution. J Mol Evol 30:479-88
Saus, J; Quinones, S; MacKrell, A et al. (1989) The complete primary structure of mouse alpha 2(IV) collagen. Alignment with mouse alpha 1(IV) collagen. J Biol Chem 264:6318-24
Quinones, S; Saus, J; Otani, Y et al. (1989) Transcriptional regulation of human stromelysin. J Biol Chem 264:8339-44
Muthukumaran, G; Blumberg, B; Kurkinen, M (1989) The complete primary structure for the alpha 1-chain of mouse collagen IV. Differential evolution of collagen IV domains. J Biol Chem 264:6310-7
Saus, J; Quinones, S; Otani, Y et al. (1988) The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin. J Biol Chem 263:6742-5
Hostikka, S L; Kurkinen, M; Tryggvason, K (1987) Nucleotide sequence coding for the human type IV collagen alpha 2 chain cDNA reveals extensive homology with the NC-1 domain of alpha 1 (IV) but not with the collagenous domain or 3'-untranslated region. FEBS Lett 216:281-6
Boot-Handford, R P; Kurkinen, M; Prockop, D J (1987) Steady-state levels of mRNAs coding for the type IV collagen and laminin polypeptide chains of basement membranes exhibit marked tissue-specific stoichiometric variations in the rat. J Biol Chem 262:12475-8
Kurkinen, M; Condon, M R; Blumberg, B et al. (1987) Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen. J Biol Chem 262:8496-9

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