MMP-1 Rabbit Polyclonal Antibody

Function

MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a linker region and a hemopexin-like domain. Two main nomenclatures for the primary structure are currently in use, the original one from which the first amino-acid starts with the signalling peptide and a second one where the first amino-acid starts counting from the prodomain (proenzyme nomenclature). MMPs are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Specifically, MMP-1 breaks down the interstitial collagens, types I, II, and III. Mechanical force may increase the expression of MMP1 in human periodontal ligament cells.

Background References

1. Maskos K, Bode W (November 2003). "Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases". Mol. Biotechnol. 25 (3): 241–66.

2. Huang SF, Li YH, Ren YJ, Cao ZG, Long X (August 2008). "The effect of a single nucleotide polymorphism in the matrix metalloproteinase-1 (MMP-1) promoter on force-induced MMP-1 expression in human periodontal ligament cells". Eur. J. Oral Sci. 116 (4): 319–23.

Sequence Similarity

Belongs to the peptidase M10A family.

Post-translational Modification

Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.; Tyrosine phosphorylated in platelets by PKDCC/VLK.

Subcellular Location

Secreted.

UNIPROT

SwissProt: P03956 Human

SwissProt: P81563 Rat

Synonyms