國家衛生研究院 NHRI:Item 3990099045/4608

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Title:	Involvement of protein tyrosine phosphatase SHP-1 in the inhibition of membrane-bound guanylate cyclase GC-A activity stimulated by atrial natriuretic factor
Authors:	Chang, CH;Chang, GD;Yang, SR;Chen, CY;Chung, WY
Contributors:	Division of Gerontology Research
Abstract:	We examined whether SHP-1 can regulate the activation of membrane-bound guanylate cyclase GC-A by atrial natriuretic factor (ANF). Co-immunoprecipitation experiments indicated that SHP-1 associated with GC-A in an ANF-dependent manner. Transfection of SHP-1 into CHO and MCF-7 cells inhibited ANF-stimulated GC-A activity. GC-A contains two SHP-1 substrate consensus sequences (amino acids 816-821 and 1014-1020) in its catalytic domain (GC-c). Transfection studies showed that SHP-1 inhibited the activity of GC-c, indicating that SHP-1 interacts with the catalytic domain. Interestingly, substitution of Phe at Tyr 818 or Tyr 1017 on GC-c led to the loss of enzyme activity. Examination of the tyrosine phosphorylation state of GC-A reveals that GC-A is not dephosphorylated by SHP-1. Transfection of v-Src enhanced ANF-stimulated GC-A activity in MCF-7 cells, whereas inhibition of Src activity decreased it. Co-immunoprecipitation experiments indicate that transfection of SHP-1 disrupts the association of Src with GC-A. These results indicate that SHP-1 is a GC-A associated protein, and that SHP-1 inhibits the activity of GC-A at least partly by disrupting the association of Src with GC-A.
Date:	2007-04
Relation:	FASEB Journal. 2007 Apr;21(6):A797.
Link to:	http://www.fasebj.org/cgi/content/meeting_abstract/21/6/A797?sid=e532ec81-45e0-4fac-8ed1-b1461d816d5f
JIF/Ranking 2023:	http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0892-6638&DestApp=IC2JCR
Cited Times(WOS):	https://www.webofscience.com/wos/woscc/full-record/WOS:000245708700293
Appears in Collections:	[Chung-Ho Chang] Conference Papers/Meeting Abstract

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