Background: TIMP-1

TIMPs-1 through -4 regulate the activity of zinc metalloproteases known as MMPs, ADAMs and ADAMTSs. Structurally, TIMPs contain two domains. The N-terminal domain binds to the active site of mature metalloproteases via a 1:1 non-covalent interaction, blocking access of substrates to the catalytic site. In addition, The C-terminal domain of TIMP-1 and TIMP-2 binds to the hemopexin- like domain of pro-MMP-9 and pro-MMP-2, respectively. The latter binding is essential for the cell surface activation of MMP-2 by MMP-14.

• Long Name:

  Tissue Inhibitors of Metalloproteinases 1

• Entrez Gene IDs:

  7076 (Human); 21857 (Mouse); 116510 (Rat)

• Alternate Names:

  CLGI; Collagenase inhibitor; collagenase inhibitor); EPATIMP-1; EPO; erythroid potentiating activity; Erythroid-potentiating activity; Fibroblast collagenase inhibitor; FLJ90373; HCI; metalloproteinase inhibitor 1; TIMP metallopeptidase inhibitor 1; TIMP1; TIMP-1; TIMPtissue inhibitor of metalloproteinase 1 (erythroid potentiating activity; Tissue inhibitor of metalloproteinases 1