Plasminogen activator inhibitor-1 and -3 increase cell adhesion and motility of MDA-MB-435 breast cancer cells. (Q44102084)

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12 November 2019

title

Plasminogen activator inhibitor-1 and -3 increase cell adhesion and motility of MDA-MB-435 breast cancer cells (English)

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12 November 2019

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2

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12 November 2019

author name string

Diane Palmieri

series ordinal

1

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12 November 2019

Rudy L Juliano

series ordinal

3

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12 November 2019

Frank C Church

series ordinal

4

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12 November 2019

language of work or name

English

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publication date

9 August 2002

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Journal of Biological Chemistry

12 November 2019

published in

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12 November 2019

volume

277

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12 November 2019

issue

43

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12 November 2019

page(s)

40950-40957

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cDNA cloning of human plasminogen activator-inhibitor from endothelial cells

12 November 2019

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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature

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Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?

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The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin

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Plasmin and plasminogen activator inhibitor type 1 promote cellular motility by regulating the interaction between the urokinase receptor and vitronectin

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Promigratory effect of plasminogen activator inhibitor-1 on invasive breast cancer cell populations.

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Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen

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Thrombospondin-induced tumor cell migration: haptotaxis and chemotaxis are mediated by different molecular domains

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Plasminogen-activator inhibitor type 1 is a potent natural inhibitor of extracellular matrix degradation by fibrosarcoma and colon carcinoma cells

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Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization.

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Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.

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Maspin acts at the cell membrane to inhibit invasion and motility of mammary and prostatic cancer cells

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M202333200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12176977%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

1 reference