Bovine membrane-type 1 matrix metalloproteinase: molecular cloning and expression in the corpus luteum.

Academic Article


  • Matrix metalloproteinase-2 (MMP-2) is produced as a zymogen, which is subsequently activated by membrane-type 1 metalloproteinase (MT1-MMP). The objectives of the present study were to clone bovine MT1-MMP and to investigate its expression in the corpus luteum. Corpora lutea were harvested from nonlactating dairy cows on Days 4, 10, and 16 of the estrous cycle (Day 0 = estrus; n = 3 for each age). The bovine MT1-MMP cDNA contained an open reading frame of 1749 base pairs, which encoded a predicted protein of 582 amino acids. Northern blotting revealed no differences (P > 0.05) in MT1-MMP mRNA levels between any ages of corpora lutea. Western blotting demonstrated that two species of MT1-MMP, the latent form ( approximately 63 kDa) and the active form ( approximately 60 kDa), were present in corpora lutea throughout the estrous cycle. Active MT1-MMP was lower (P < 0.05) in early stages of the corpus luteum than the mid and late stages, where MMP-2 activity, as revealed by gelatin zymography, was also elevated. Furthermore, immunohistochemistry revealed that MT1-MMP was localized in endothelial, large luteal, and fibroblast cells of the corpus luteum at different stages. Taken together, the differential expression and localization of MT1-MMP in the corpus luteum suggest that it may have multiple functions throughout the course of the estrous cycle, including activation of pro-MMP-2.
  • Authors

  • Zhang, Bo
  • Yan, Li
  • Moses, Marsha A
  • Tsang, Paul
  • Status

    Publication Date

  • July 2002
  • Published In


  • Animals
  • Blotting, Northern
  • Blotting, Western
  • Cattle
  • Cloning, Molecular
  • Corpus Luteum
  • DNA, Complementary
  • Densitometry
  • Estrous Cycle
  • Female
  • Gelatin
  • Gene Expression Regulation, Enzymologic
  • Immunohistochemistry
  • Matrix Metalloproteinase 1
  • Matrix Metalloproteinase 2
  • Ovary
  • RNA, Messenger
  • Tissue Distribution
  • Digital Object Identifier (doi)

    Pubmed Id

  • 12080004
  • Start Page

  • 99
  • End Page

  • 106
  • Volume

  • 67
  • Issue

  • 1