Gas6-mediated signaling is dependent on the engagement of its gamma-carboxyglutamic acid domain with phosphatidylserine (Q24309100)

negative regulation of endothelial cell apoptotic process

GOA release 2020-03-11

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Biochemical and Biophysical Research Communications

GOA release 2020-03-11

author name string

Isabelle Rajotte

series ordinal

1

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Ines Hasanbasic

series ordinal

2

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Mark Blostein

series ordinal

3

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language of work or name

English

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publication date

7 November 2008

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published in

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volume

376

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page(s)

70-3

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issue

1

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cites work

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Partial activation of the factor VIIIa-factor IXa enzyme complex by dihexanoic phosphatidylserine at submicellar concentrations

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Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6

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Deficiency or inhibition of Gas6 causes platelet dysfunction and protects mice against thrombosis.

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Requirement of gamma-carboxyglutamic acid residues for the biological activity of Gas6: contribution of endogenous Gas6 to the proliferation of vascular smooth muscle cells

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A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody. Localization of phosphatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarboxylase

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A putative phosphatidylserine binding motif is not involved in the lipid regulation of protein kinase C.

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Soluble phosphatidylserine triggers assembly in solution of a prothrombin-activating complex in the absence of a membrane surface.

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The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade

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