ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2. (Q33241217)

24 July 2017

ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2. (English)

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24 July 2017

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Antoni X Torres-Collado

object named as

Antoni X Torres-Collado

1

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author name string

Walter Kisiel

2

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24 July 2017

Maria L Iruela-Arispe

3

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24 July 2017

Juan C Rodríguez-Manzaneque

4

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24 July 2017

language of work or name

English

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publication date

26 April 2006

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Journal of Biological Chemistry

24 July 2017

11

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inferred from page(s)

published in

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24 July 2017

281

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24 July 2017

26

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24 July 2017

17827-17837

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The ADAMTS metalloproteinases

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Adamts-1 is essential for the development and function of the urogenital system

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Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4

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Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor

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Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI towar

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Paradoxical pro-invasive effect of the serine proteinase inhibitor tissue factor pathway inhibitor-2 on human hepatocellular carcinoma cells.

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Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms

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Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen

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The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage

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Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing

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Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity

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HT-1080 fibrosarcoma cell matrix degradation and invasion are inhibited by the matrix-associated serine protease inhibitor TFPI-2/33 kDa MSPI.

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Identifiers

DOI

10.1074/JBC.M513465200

1 reference

24 July 2017

1 reference