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Protein interactions with cdc37 in agonist stimulated bovine aortic endothelial cells
Author(s) -
Horst Kyle E,
Wilson Christopher G,
Harris M Brennan
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.965.11
Subject(s) - enos , protein kinase b , chemistry , hsp90 , medicine , nitric oxide , endocrinology , stimulation , bradykinin , microbiology and biotechnology , signal transduction , nitric oxide synthase , biology , biochemistry , receptor , heat shock protein , gene
Previously we have demonstrated that the cell division cycle 37 homolog, cdc37, interacts directly with the endothelial nitric oxide synthase (eNOS) and inhibits eNOS activity in vitro. In addition, cdc37 regulates interactions between other key regulators of eNOS activity including Hsp90 and Akt. Therefore, we investigated changes cdc37 interactions with eNOS, Hsp90, and Akt in bovine aortic endothelial cells (BAECs) stimulated with either vascular endothelial growth factor (VEGF) or bradykinin (BK). Treatment of BAECs with VEGF or BK for 0, 1, 5, 15, 30, or 60 min resulted in a biphasic change in cdc37/eNOS interaction. Cdc37 interaction with eNOS decreased upon stimulation but returned to basal levels by 15 min and then decreased by 30 and 60 min. Agonist stimulation also resulted in a transient increase in Hsp90 association with cdc37, however, no significant changes in cdc37 and Akt interaction were observed. These data coupled with our previous findings suggest that cdc37 initially inhibits basal eNOS activity through direct interaction and may play a role in agonist stimulated eNOS activity through its interaction with Hsp90. Supported by NIH R15 HL082649 (MBH) and an American Physiological Society Summer Undergraduate Research Fellowship (KEH).