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Role of protein tyrosine phosphatase...

Lin, Yi.

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Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility./
Author:	Lin, Yi.
Description:	115 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1043.
Contained By:	Dissertation Abstracts International64-03B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3085400

Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility.
Lin, Yi.

Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility. - 115 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1043.

Thesis (Ph.D.)--The University of Tennessee Health Science Center, 2003.

Migration of medial vascular smooth muscle cells is an essential feature of neointima formation. The increase in NO levels in vascular injury is thought to play a counter regulatory role in neointima formation by decreasing vascular smooth muscle cell motility. I found that NO donors increased the activity but not the protein levels of PTP-PEST. A cGMP analogue mimicked the effect of NO whereas a guanylyl cyclase inhibitor blocked it. Overexpression of wild type PTP-PEST mimicked, whereas overexpression of dominant negative PTP-PEST blocked the antimotogenic effect of NO. Overexpression of PTP-PEST also mimicked the capacity of NO to decrease phosphotyrosine levels in adapter protein p130cas, whereas dominant negative-PTP-PEST blocked the effect of NO. To investigate the functional significance of p130 cas dephosphorylation, I used an adenovirus expressing a substrate-domain-deleted p130cas allele and found that this protein decreased cell motility whereas use of adenovirus overexpressing wild type p130cas blocked the antimotogenic effect of NO. To investigate events downstream of p130cas, I measured the intracellular association of p130 cas with proto-oncogene Crk and found that NO decreased the coimmunoprecipitation of these two proteins. Moreover, overexpression of wild type PTP-PEST mimicked Cas-Crk dissociation whereas dominant negative-PTP-PEST blocked the Cas-Crk dissociation induced by NO. These results indicate that NO decreases aortic smooth muscle cell motility via a cGMP-mediated mechanism, involving upregulation of PTP-PEST, in turn inducing dephosphorylation of p130cas, and likely involving Cas-Crk dissociation as a downstream event. I also explored the role of PTP-PEST in insulin-stimulated cell motility. I found that overexpression of wild type PTP-PEST attenuated insulin-stimulated cell motility without influencing the level of phosphorylation in the insulin receptor beta chain. Moreover, insulin failed to alter the phosphotyrosine levels of p130 cas. These data suggest that PTP-PEST is not involved in directly modulating the insulin signaling pathway for regulation of cell motility.Subjects--Topical Terms:

1017686
Biology, Cell.

Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility.
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100 1 $a Lin, Yi. $3 881077
245 1 0 $a Role of protein tyrosine phosphatase-PEST in nitric oxide-induced inhibition of basal and insulin-stimulated cell motility.
300 $a 115 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1043.
500 $a Adviser: Aviv Hassid.
502 $a Thesis (Ph.D.)--The University of Tennessee Health Science Center, 2003.
520 $a Migration of medial vascular smooth muscle cells is an essential feature of neointima formation. The increase in NO levels in vascular injury is thought to play a counter regulatory role in neointima formation by decreasing vascular smooth muscle cell motility. I found that NO donors increased the activity but not the protein levels of PTP-PEST. A cGMP analogue mimicked the effect of NO whereas a guanylyl cyclase inhibitor blocked it. Overexpression of wild type PTP-PEST mimicked, whereas overexpression of dominant negative PTP-PEST blocked the antimotogenic effect of NO. Overexpression of PTP-PEST also mimicked the capacity of NO to decrease phosphotyrosine levels in adapter protein p130cas, whereas dominant negative-PTP-PEST blocked the effect of NO. To investigate the functional significance of p130 cas dephosphorylation, I used an adenovirus expressing a substrate-domain-deleted p130cas allele and found that this protein decreased cell motility whereas use of adenovirus overexpressing wild type p130cas blocked the antimotogenic effect of NO. To investigate events downstream of p130cas, I measured the intracellular association of p130 cas with proto-oncogene Crk and found that NO decreased the coimmunoprecipitation of these two proteins. Moreover, overexpression of wild type PTP-PEST mimicked Cas-Crk dissociation whereas dominant negative-PTP-PEST blocked the Cas-Crk dissociation induced by NO. These results indicate that NO decreases aortic smooth muscle cell motility via a cGMP-mediated mechanism, involving upregulation of PTP-PEST, in turn inducing dephosphorylation of p130cas, and likely involving Cas-Crk dissociation as a downstream event. I also explored the role of PTP-PEST in insulin-stimulated cell motility. I found that overexpression of wild type PTP-PEST attenuated insulin-stimulated cell motility without influencing the level of phosphorylation in the insulin receptor beta chain. Moreover, insulin failed to alter the phosphotyrosine levels of p130 cas. These data suggest that PTP-PEST is not involved in directly modulating the insulin signaling pathway for regulation of cell motility.
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710 2 0 $a The University of Tennessee Health Science Center. $3 1262886
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790 $a 0783
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3085400