Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells (Q28209528)

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Ai-Zhen Xiao

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Robert G Newcomer

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Hyun I Park

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Tiebang Kang

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Mark G Swanson

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Haiyen E Zhau

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John Kurhanewicz

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Qing-Xiang Amy Sang

Journal of Biological Chemistry

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language of work or name

English

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publication date

25 April 2003

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published in

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volume

278

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issue

17

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page(s)

15056-64

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cites work

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Androgen-repressed phenotype in human prostate cancer

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Proteolytic and non-proteolytic activation of human neutrophil progelatinase B

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Expression of matrix metalloproteinase -2, -9 and tissue inhibitors of metalloproteinase -1, -2, -3 mRNAs in rat uterus during early pregnancy

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Functional characterization of MT3-MMP in transfected MDCK cells: progelatinase A activation and tubulogenesis in 3-D collagen lattice.

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Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites

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The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL.

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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

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Down-regulation of invasion and angiogenesis-related genes identified by cDNA microarray analysis of PC3 prostate cancer cells treated with genistein

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Matrix metalloproteinase activity, bone matrix turnover, and tumor cell proliferation in prostate cancer bone metastasis

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Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26

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Identifiers

DOI

10.1074/JBC.M210975200

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Consolidated OpenCitations Corpus – April 2017

4757637

4757637

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference