Primary structure of bovine interstitial collagenase deduced from cDNA sequence.
Interstitial collagenase (EC 3.4.24.7, MMP-1) is a member of a family of metalloproteinases and is though to play a role in extracellular matrix remodeling. We have isolated and sequenced a cDNA for bovine interstitial collagenase from a periodontium fibroblast cDNA library. An insert of the cDNA we isolated was 2,025 bp containing an open reading frame which encodes a sequence of 469 amino acids. The identity at the amino acid level between bovine and human interstitial collagenase was 88%, between bovine and rabbit 85% and between bovine and porcine 87%. However, sequence similarity of mouse and rat interstitial collagenases to that of bovine was revealed 55%.
Tamura
M
M
Department of Biochemistry, Faculty of Dentistry, Tokyo Medical and Dental University, Japan.
Shimokawa
H
H
Sasaki
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D017364:Collagenases / Q000737:chemistry / Q000235:genetics*; D018076:DNA, Complementary; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D020781:Matrix Metalloproteinase 1; D051379:Mice; D008969:Molecular Sequence Data; D010519:Periodontium / Q000166:cytology / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D017364:Collagenases; D020781:Matrix Metalloproteinase 1