Metalloproteinase inhibitor 1

Definition:

Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.

References:

[1]. V Knäuper, et al. Biochemical characterization of human collagenase-3. J Biol Chem. 1996 Jan 19;271(3):1544-50. [Content Brief]

[2]. Soo Youn Lee, et al. TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling. Biochem J. 2014 May 1;459(3):565-76. [Content Brief]

[3]. J C Gasson, et al. Molecular characterization and expression of the gene encoding human erythroid-potentiating activity. Nature. 1985;315(6022):768-71. [Content Brief]

[4]. Ki-Kyung Jung, et al. Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. EMBO J. 2006 Sep 6;25(17):3934-42. [Content Brief]

[5]. A J Docherty, et al. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature. 1985 Nov;318(6041):66-9. [Content Brief]

[6]. L Chesler, et al. Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1. Blood. 1995 Dec 15;86(12):4506-15. [Content Brief]

[7]. A Osthues, et al. Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid. FEBS Lett. 1992 Jan 13;296(1):16-20. [Content Brief]

[8]. Moran Grossman, et al. The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function. Biochemistry. 2010 Jul 27;49(29):6184-92. [Content Brief]

[9]. Shalini Iyer, et al. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1. J Biol Chem. 2007 Jan 5;282(1):364-71. [Content Brief]

[10]. Jyotica Batra, et al. Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure. J Biol Chem. 2012 May 4;287(19):15935-46. [Content Brief]

[11]. M O'Shea, et al. Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13. Biochemistry. 1992 Oct 27;31(42):10146-52. [Content Brief]

[12]. V Knäuper, et al. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem. 1997 Mar 21;272(12):7608-16. [Content Brief]

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