Barbara M. Sanborn, PhD Professor and Head Office: 102 Phyiology Building Member Education Link to a PubMed listing of Dr. Sanborn's
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Research Interests -- Hormonal Signal Transduction
Hormones are molecular signals that alter cell function. Understanding how hormones convey their signals is critical for understanding basic cell biology and disease states, and for designing intervention strategies. Research in my laboratory focuses on defining the molecular signal transduction pathways of hormone action relating to the control of differentiation and intracellular calcium dynamics in the myometrium (uterine smooth muscle).
Mechanisms involved in smooth muscle intracellular calcium control.
Signaling crosstalk: The control of uterine contraction/relaxation is critical to the maintenance of pregnancy and the efficient delivery of the neonate. Uterine contractants such as oxytocin increase intracellular calcium in uterine muscle cells by increasing influx and release from intracellular stores secondary to phospholipase C (PLC) activation. Relaxants oppose these actions by regulatory phosphorylation mechanisms. Some of these signaling pathways require scaffolding proteins that localize the components in the same region of the cell. We are determining the biochemical basis for the regulatory role of phosphorylation, the requirements for interaction with scaffolding proteins, and changes in key signaling pathways that occur during pregnancy. These changes involve alteration in the expression and intracellular localization of proteins. We use biochemical and cell and molecular biological approaches as well as studying muscle physiology.
Calcium dynamics: We are studying hormonal effects on intracellular calcium dynamics by single cell immunofluorescence and effects of hormones on ion channel activity and expression. We are using Q-RTPCR and siRNA suppression techniques to alter expression of specific channel proteins and determining the consequence on calcium dynamics.
Selected Publications
Zhong M, Parish B, Murtazina DA, Ku CY, Sanborn BM. 2007. Amino acids in the C-terminal region of the oxytocin receptor third intracellular domain are important for receptor function. Am J Physiol 292:E977-E984.
Sanborn BM, Zhong M, Parish BJ. 2006. Oxytocin receptor. AfCS-Nature Molecule Pages. (doi:10.1038/mp.a001705.01)
Ku CY, Babich L, Word RA, Zhong M, Ulloa A, Monga M, Sabnorn BM. 2006. Expression of transient receptor channel proteins in fundal myometrium in pregnancy. J Soc Gynecol Invest 13:217-225.
Zhong M, Ku CY, Sanborn BM. 2005. Pathways used by relaxin to regulate myometrial phospholipase C. Ann N Y Acad Sci 1041:300-304.
Sanborn BM, Ku CY, Shlykov S, Babich L. 2005. Molecular signaling through G-protein-coupled receptors and the control of intracellular calcium in myometrium. J Soc Gynecol Invest 12:479-487. (review)
Ku CY, Word RA, Sanborn BM. 2005. Differential expression of protein kinase A, AKAP79 and PP2B in pregnant human myometrial membranes prior to and during labor. J Soc Gynecol Invest 12:421-427.
Bathgate RA, Ivell R, Sanborn BM, Sherwood OD, Summers RJ. 2005. Receptors for relaxin family peptides. Ann NY Acad Sci 1041:61-76. (review)
Babich LG, Ku CY, Young HWJ, Huang H, Blackburn MR, Sanborn BM. 2004. Expression of capacitative calcium TrpC proteins in rat myometrium during pregnancy. Biol. Reprod. 79:919-924.
Zhong M, Navratil AM, Clay C, Sanborn BM. 2004. Residues in the hydrophilic face of putative helix 8 of oxytocin receptor are important for receptor function. Biochemistry 43:3490-3498.
Shlykov SG, Sanborn BM. 2004. Stimulation of intracellular Ca2+ by diacylglycerol in human myometrial cells. Cell Calcium 36:157-164.
Shlykov SG, Yang M, Alcorn JL, Sanborn BM. 2003. Capacitative cation entry in human myometrial cells and augmentation by hTrpC3 overexpression. Biol Reprod 69:647-655.
Zhong M, Yang M, Sanborn BM. 2003. ERK1/2 activation by oxytocin receptor in myometrium involves GaGbg and EGF tyrosine kinase activation. Mol Endocrinol144:2947-2956.
Yang M, Wang W, Zhong M, Philippi A, Lichtarge O, Sanborn BM. 2002. Lysine 270 in the third intracellular domain of the oxytocin receptor is an important determinant for Gaq coupling specificity. Molec Endocrinol 16:814-823.
Ku C-Y, Sanborn BM. 2002. Progesterone prevents the pregnancy-related decline in protein kinase A association with rat myometrial plasma membrane and A-kinase anchoring protein. Biol Reprod 67:605-609.
Yang M, Gupta A, Shlykov SG, Corrigan R, Tsujimoto S, Sanborn BM. 2002. Multiple Trp isoforms implicated in capacitative calcium entry are expressed in human pregnant myometrium and myometrial cells. Biol Reprod 67:988-994.
Sanborn BM. 2001. Hormones and calcium: Mechanisms controlling uterine smooth muscle contractile activity. Exp Physiol 86:223-237. (review)
Yue C, Ku C-Y, Liu M, Simon MI, Sanborn BM. 2000. Molecular mechanism of the inhibition of phospholipase Cb3 by protein kinase C. J Biol Chem 275:30220-30225.
