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Issue 1041 coverRELAXIN AND RELATED PEPTIDES: Fourth International Conference Volume 1041 published May 2005
Ann. N.Y. Acad. Sci. 1041: 296–299 (2005). doi: 10.1196/annals.1282.044
Copyright © 2005 by the New York Academy of Sciences
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Articles by NGUYEN, B. T.
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Articles by NGUYEN, B. T.
Articles by DESSAUER, C. W.
Relaxin Stimulates cAMP Production in MCF-7 Cells upon Overexpression of Type V Adenylyl Cyclase

BAO T. NGUYEN AND CARMEN W. DESSAUER

Department of Integrative Biology and Pharmacology, University of Texas Health Science Center, Houston, Texas 77030, USA

Address for correspondence: Dr. Carmen W. Dessauer, Department of Integrative Biology and Pharmacology, University of Texas Health Science Center, Houston, TX 77030. Voice: 713-500-6308; fax: 713-500-7444. carmen.w.dessauer{at}uth.tmc.edu

Relaxin stimulates cAMP production and activation of ERK and PI3K in THP-1 cells. Relaxin also stimulates protein kinase C zeta (PKC{zeta}) translocation to the plasma membrane in a PI3K-dependent manner in THP-1 and MCF-7 cells. However, relaxin did not increase cAMP production in MCF-7 cells. We overexpressed different adenylyl cyclase (AC) isoforms in MCF-7 cells to examine coupling of endogenous relaxin receptors to cAMP production. Overexpression of types II and IV AC had no effect on cAMP production by relaxin. However, overexpression of type V AC, which is activated by PKC{zeta}, showed synergistic stimulation of cAMP by relaxin and forskolin.

Key Words: adenylyl cyclase • PI3K • PKC{zeta} • relaxin • cyclic AMP • ACV • ACII




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T.-Y. Ho, W. Yan, and C. A. Bagnell
Relaxin-induced matrix metalloproteinase-9 expression is associated with activation of the NF-{kappa}B pathway in human THP-1 cells
J. Leukoc. Biol., May 1, 2007; 81(5): 1303 - 1310.
[Abstract] [Full Text] [PDF]



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