Journal article
Porcine Collagenase from Synovial Fibroblasts: cDNA Sequence and Modulation of Expression of RNA In Vitro by Various Cytokines
Abstract
Collagenase is a metalloproteinase that is important in extracellular matrix turnover and is produced by synovial fibroblasts in response to various cytokines and growth factors. Porcine collagenase cDNA was cloned and the sequence shows a 469-amino acid (AA) peptide with high homology to the human and rabbit enzyme (84% and 83.4% respectively). Predicted amino acid sequence from position #99-114 agree well with previously obtained NH2-terminal …
Authors
Richards CD; Rafferty JA; Reynolds JJ; Saklatvala J
Journal
Matrix Biology, Vol. 11, No. 3, pp. 161–167
Publisher
Elsevier
Publication Date
June 1991
DOI
10.1016/s0934-8832(11)80154-x
ISSN
0945-053X
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBase SequenceBlotting, NorthernCells, CulturedCloning, MolecularCytokinesDNAEpidermal Growth FactorFibroblastsGene Expression Regulation, EnzymologicHumansInterleukin-1Microbial CollagenaseMolecular Sequence DataRabbitsRecombinant ProteinsRestriction MappingSequence Homology, Nucleic AcidSwineSynovial MembraneTransforming Growth Factor betaTumor Necrosis Factor-alpha