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Characterization of a peptide inhibi...

Flowers, Lawrence O.

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Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function./
Author:	Flowers, Lawrence O.
Description:	85 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 3851.
Contained By:	Dissertation Abstracts International65-08B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3144192
ISBN:	0496022644

Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function.
Flowers, Lawrence O.

Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function. - 85 p.

Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 3851.

Thesis (Ph.D.)--University of Florida, 2004.

Tyrosine kinases are extremely important biological molecules involved in numerous cellular signal transduction events. Fidelity of these signal transduction events is essential for normal cellular functions. Many diseased states such as cancer and autoimmune diseases are associated with defective tyrosine kinases. Positive and negative regulation of cytokines such as gamma interferon (IFNgamma) is key to normal homeostatic function. Negative regulation of IFNgamma in cells occurs via proteins called suppressors of cytokine signaling (SOCS) 1 and 3. SOCS-1 inhibits IFNgamma function by binding to the autophosphorylation site of the tyrosine kinase JAK2.

ISBN: 0496022644Subjects--Topical Terms:

1017734
Biology, Microbiology.

Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function.
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020 $a 0496022644
035 $a (UnM)AAI3144192
035 $a AAI3144192
040 $a UnM $c UnM
100 1 $a Flowers, Lawrence O. $3 1901896
245 1 0 $a Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function.
300 $a 85 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 3851.
500 $a Chair: Howard M. Johnson.
502 $a Thesis (Ph.D.)--University of Florida, 2004.
520 $a Tyrosine kinases are extremely important biological molecules involved in numerous cellular signal transduction events. Fidelity of these signal transduction events is essential for normal cellular functions. Many diseased states such as cancer and autoimmune diseases are associated with defective tyrosine kinases. Positive and negative regulation of cytokines such as gamma interferon (IFNgamma) is key to normal homeostatic function. Negative regulation of IFNgamma in cells occurs via proteins called suppressors of cytokine signaling (SOCS) 1 and 3. SOCS-1 inhibits IFNgamma function by binding to the autophosphorylation site of the tyrosine kinase JAK2.
520 $a A short 12-mer peptide, WLVFFVIFYFFR (Tkip), was developed that bound to the autophosphorylation site of JAK2, resulting in inhibition of its autophosphorylation as well as its phosphorylation of IFNgamma receptor subunit IFNGR-1 tyrosine 440. The JAK2 tyrosine kinase inhibitor peptide (Tkip) did not bind to or inhibit tyrosine autophosphorylation of vascular endothelial growth factor receptor (VEGFR) or phosphorylation of a substrate peptide by the protooncogene tyrosine kinase c-src. Tkip also inhibited epidermal growth factor receptor (EGFR) autophosphorylation, consistent with the fact that EGFR is regulated by SOCS-1 and SOCS-3, similar to JAK2. Although Tkip binds to unphosphorylated JAK2 autophosphorylation peptide, it binds significantly better to tyrosine 1007 phosphorylated JAK2 autophosphorylation peptide. SOCS-1 only recognizes the JAK2 site in its phosphorylated state. Thus, Tkip recognizes the JAK2 autophosphorylation site similar to SOCS-1, but not precisely the same way.
520 $a Consistent with inhibition of JAK2, Tkip inhibited antiviral activity and MHC class I upregulation on cells at a concentration of approximately 10 muM. This is similar to the Kd of SOCS-3 for the erythropoietin receptor. These data represent a proof-of-concept demonstration of a peptide mimetic of SOCS-1 that regulates JAK2 tyrosine kinase function.
590 $a School code: 0070.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0410
690 $a 0379
690 $a 0982
710 2 0 $a University of Florida. $3 718949
773 0 $t Dissertation Abstracts International $g 65-08B.
790 1 0 $a Johnson, Howard M., $e advisor
790 $a 0070
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3144192