(Q28138867)

English

Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation

scientific article (publication date: 15 December 2000)

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scholarly article

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Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation (English)

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author name string

C M Overall

1

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E Tam

2

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G A McQuibban

3

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C Morrison

4

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U M Wallon

5

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H F Bigg

6

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A E King

7

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C R Roberts

8

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language of work or name

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publication date

15 December 2000

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Journal of Biological Chemistry

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275

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50

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39497-506

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Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity

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The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation

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The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

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TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads

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Cell surface binding of TIMP-2 and pro-MMP-2/TIMP-2 complex

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The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

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The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.

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Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes

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The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen

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Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation.

1 reference

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Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface

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Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen

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A novel genetic system to detect protein-protein interactions

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Differential stability of proteolytically active and inactive recombinant metalloproteinase in Chinese hamster ovary cells

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Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2

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Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3.

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Kinetic analysis of the mechanism of interaction of full-length TIMP-2 and gelatinase A: evidence for the existence of a low-affinity intermediate

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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

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Reactive site-modified tissue inhibitor of metalloproteinases-2 inhibits the cell-mediated activation of progelatinase A.

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10.1074/JBC.M005932200

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https://api.fatcat.wiki/v0/release/rpjwqpfejfgg3kfdpk6espidrq

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