MMP2, MMP7, MMP9 bind CD44

Stable Identifier
Reaction [binding]
Homo sapiens
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Certain normally extracellular MMPs can transiently localize at the cell periphery in association with adhesion receptors or proteoglycans. ProMMP9, MMP9, MMP2 and MMP7 (Ahmed et al. 2002, Samanna et al. 2006, Yu et al. 2002) localize at the cell membrane with the single-pass transmembrane glycoprotein CD44, known to be involved in hyaluronan-cell interactions, lymphocyte homing and cell adhesion (Toole 1990). Membrane-associated MMP7 can bring about the shedding of several membrane proteins such as epidermal growth factor (EGF), soluble Fas ligand (FasL), E-cadherin and TNF-alpha from their membrane-bound precursors, thereby promoting cancer progression (Li et al. 2006). CD44-anchored MMP9 cleaves and activates transforming growth factor beta (TGF-β ), degrades extracellular matrix components such as laminin, and regulates function of several membrane bound proteins (Yu Q & Stamenkovic I 2000; reviewed by Augoff K et al. 2022). MMP9 is able to cleave CD44 as shown in neurons (Bijata M et al. 2017). The CD44:MMP9 interaction is thought to promote tumor invasion and metastatic ability (Yu Q & Stamenkovic I 2000; Peng ST et al. 2007).
Literature References
PubMed ID Title Journal Year
16631740 Alpha-V-dependent outside-in signaling is required for the regulation of CD44 surface expression, MMP-2 secretion, and cell migration by osteopontin in human melanoma cells

Chellaiah, MA, Wei, H, Ego-Osuala, D, Samanna, V

Exp. Cell Res. 2006
11872628 Overexpression of alpha(v)beta6 integrin in serous epithelial ovarian cancer regulates extracellular matrix degradation via the plasminogen activation cascade

Quinn, MA, Mok, S, Agrez, MV, Baker, MS, Ahmed, N, Rice, GE, Clyde, R, Murthi, P, Pansino, F

Carcinogenesis 2002
1707285 Hyaluronan and its binding proteins, the hyaladherins

Toole, BP

Curr. Opin. Cell Biol. 1990
Orthologous Events
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