title: Molecular characteristics of equine stromelysin and the tissue inhibitor of metalloproteinase 1.
abstract: OBJECTIVE
  To clone the entire coding sequence of equine matrix metalloproteinase-3 (MMP-3, stromelysin) and tissue inhibitor of metalloproteinase-1 (TIMP-1) and compare their nucleotide and amino acid sequences with those of MMP-3 and TIMP-1 from other species.
  
  
  METHODS
  Articular cartilage harvested from the joints of 4 foals, 2 yearlings, and 3 adult horses.
  
  
  METHODS
  A cDNA library was constructed from mRNA extracted from equine chondrocytes. The library was screened and clones selected that contained the cDNA for MMP-3 and TIMP-1. The cDNA was sequenced and the nucleotide and deduced amino acid sequences compared with known sequences in other species. Northern blot analysis was performed, using the resulting cDNA clones.
  
  
  RESULTS
  An 1803-bp cDNA for MMP-3 including the entire coding sequence of 1434 bases was cloned and sequenced. A 744-bp cDNA for TIMP-1 including the entire coding sequence of 624 bases was cloned and sequenced. Northern analysis revealed MMP-3 to hybridize to a single mRNA species at approximately 2.1 kb. TIMP-1 hybridized to a single mRNA species at approximately 0.8 kb.
  
  
  CONCLUSIONS
  MMP-3 and TIMP-1 were highly homologous to that of other species at the nucleotide and amino acid level although each had unique residues in part of the peptide that is generally conserved.
  
  
  CONCLUSIONS
  Understanding the molecular structure of MMP-3 and TIMP-1 and the availability of their cDNA should allow a more detailed understanding of their balance in cartilage and the degradative processes in joint disease.
authors.affiliation: Department of Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square 19348-1692, USA.
authors.forename: D W
authors.initials: DW
authors.lastname: Richardson
authors.forename: G R
authors.initials: GR
authors.lastname: Dodge
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002358:Cartilage, Articular / Q000201:enzymology / Q000378:metabolism*; D017124:Conserved Sequence; D018076:DNA, Complementary; D015723:Gene Library; D006736:Horses; D006801:Humans; D019278:Matrix Metalloproteinase 3 / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*
chemical_list: D018076:DNA, Complementary; D012333:RNA, Messenger; D011994:Recombinant Proteins; D019715:Tissue Inhibitor of Metalloproteinase-1; D019278:Matrix Metalloproteinase 3