MeSH

A member of the metalloproteinase family of enzymes that is principally responsible for cleaving FIBRILLAR COLLAGEN. It can degrade interstitial collagens, types I, II and III.

Year introduced: 2007(2000)

A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the action of PROPROTEIN CONVERTASES such as FURIN. Matrix metalloproteinase 14 plays a direct role in the cleavage of proteins in the pericellular environment. In addition, it can function indirectly by enzymatically activating the proprotein form of MATRIX METALLOPROTEINASE 15.

Year introduced: 2007(1994)

RefSeq NM_001134530

Date introduced: December 17, 2012

a Matrix metalloproteinase-1 inhibitor from the stem bark of Styrax japonica S.; structure in first source

Date introduced: April 25, 2005

a Matrix metalloproteinase-1 inhibitor from the stem bark of Styrax japonica S.; structure in first source

Date introduced: April 25, 2005

An extracellular endopeptidase of vertebrate tissues similar to MATRIX METALLOPROTEINASE 1. It digests PROTEOGLYCAN; FIBRONECTIN; COLLAGEN types III, IV, V, and IX, and activates procollagenase. (Enzyme Nomenclature, 1992)

Year introduced: 2007(1997)

RefSeq NM_002421

Date introduced: August 29, 2007

may be involved in last stages of senescene in cucumber; amino acid sequence in first source; GenBank AJ133371

Date introduced: October 13, 2000