MMP-1 Products

Description

Human interstitial collagenase (matrix metalloproteinase-1, MMP-1), an enzyme whose only known physiologic substrate has heretofore been believed to be the extracellular matrix molecule, collagen. Data indicate that matrix metalloproteinase-1 displays an expanded substrate repertoire that supports the existence of a new interface between connective tissue turnover and serine proteinase inhibitors (1). It has been shown that the MMP-1 functions as a protease agonist of Protease-activated receptors (PAR1) cleaving the receptor at the proper site to generate PAR1-dependent Ca2+ signals and migration. These results demonstrate that MMP-1 in the stromal-tumor microenvironment can alter the behavior of cancer cells through PAR1 to promote cell migration and invasion (2). It has also been suggested that increased levels of MMP-1 due to tobacco smoking plays a major role in the aging process of skin since MMP-1 degrades collagen, which accounts for at least 70% of the dry weight of dermis. Significantly more MMP-1 has been detected in the skin of smokers than non-smokers whereas no difference was seen for the tissue inhibitor of metalloproteinases 1 (3).

Bioinformatics

Entrez	4312 Human 432357 Rat
Uniprot	AAH13875 Human NM_002421 Human NP_002412 Human NP_002412.1 Human P03956 Human
Product By Gene ID	4312
Alternate Names	CLGmatrix metalloprotease 1 CLGN EC 3.4.24 EC 3.4.24.7 Fibroblast collagenase interstitial collagenase matrix metallopeptidase 1 (interstitial collagenase) matrix metalloproteinase 1 (interstitial collagenase) Matrix metalloproteinase-1 MMP-1

Research Areas for MMP-1

Find related products by research area and learn more about each of the different research areas below.

Angiogenesis
Cancer
Cell Biology
Cellular Markers
Cytoskeleton Markers
Extracellular Matrix