SULEIMAN W. BAHOUTH, Ph.D.

Associate Professor

Department of Pharmacology

The University of Tennessee College of Medicine

Address

The University of Tennessee Health Science Center

874 Union Avenue

Memphis, TN 38163

Tel: (901) 448-6009; Fax: (901) 448-7300;

Lab: 309 Crowe Research Building

Education

Ph.D. Institution: New York University, Department of Pharmacology

Postdoctoral: State University of New York at Stony Brook, Department of Molecular Pharmacology

Research Interests

My research program is focused on analyzing the mechanism(s) by which hormones and neurotransmitters regulate transmembranal signalling. The approach involves determining the regions in G protein coupled receptors and GTP binding regulatory proteins (G proteins) that are involved in regulating the sensitivity of the cell to hormones and neurotransmitters.

The sensitivity of the heart to the neurotransmitter norepinephrine or to its circulating counterpart epinephrine, is profoundly influenced by thyroid hormones (T3). In the heart, it appears that the dominant receptor mediating the functions of catecholamines is the beta-adrenergic receptor. T3 upregulate the number of beta-adrenergic receptors in the heart cell and increase their sensitivity to catecholamines. With respect to the receptor, T3 exert their effects by increasing the transcription of the beta-adrenergic receptor gene. The goal of our ongoing studies is to identify the cis-acting DNA sequences in the beta-adrenergic receptor gene and trans-acting nuclear proteins that are involved in the stimulation of beta-adrenergic receptor gene transcription by T3.

The sensitivity of the receptor to catecholamines is modulated by T3 through a complex mechanism operating at a point distal to the receptor. Activation of the beta-adrenergic receptor results in the initiation of a cascade that results in the generation of the intracellular messenger cyclic AMP. The activity of the effector enzyme that catalyzes the conversion of ATP to cyclic AMP is regulated by G proteins. Our studies are focused on identifying the mechanism by which T3 regulate the abundance and coupling of G proteins to the receptor and effector.

Links

Pharmacology - Suleiman W. Bahouth

Recent Publications

• Fain JN, Buehrer B, Bahouth SW, Tichansky DS, Madan AK. Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue. Metabolism. 2008 Jul;57(7):1005-15. PMID: 18555844
• Fain JN, Sacks HS, Buehrer B, Bahouth SW, Garrett E, Wolf RY, Carter RA, Tichansky DS, Madan AK. Identification of omentin mRNA in human epicardial adipose tissue: comparison to omentin in subcutaneous, internal mammary artery periadventitial and visceral abdominal depots. Int J Obes (Lond). 2008 May;32(5):810-5. Epub 2008 Jan 8. PMID: 18180782
• Gardner LA, Naren AP, Bahouth SW. Assembly of an SAP97-AKAP79-cAMP-dependent protein kinase scaffold at the type 1 PSD-95/DLG/ZO1 motif of the human beta(1)-adrenergic receptor generates a receptosome involved in receptor recycling and networking. J Biol Chem. 2007 Feb 16;282(7):5085-99. Epub 2006 Dec 14. PMID: 17170109
• Gardner LA, Tavalin SJ, Goehring AS, Scott JD, Bahouth SW. AKAP79-mediated targeting of the cyclic AMP-dependent protein kinase to the beta1-adrenergic receptor promotes recycling and functional resensitization of the receptor. J Biol Chem. 2006 Nov 3;281(44):33537-53. Epub 2006 Aug 28. PMID: 16940053
• Zeitoun O, Santos NM, Gardner LA, White SW, Bahouth SW. Mutagenesis within helix 6 of the human beta1-adrenergic receptor identifies Lysine324 as a residue involved in imparting the high-affinity binding state of agonists. Mol Pharmacol. 2006 Sep;70(3):838-50. Epub 2006 Jun 7. PMID: 16760361
• Delos Santos NM, Gardner LA, White SW, Bahouth SW. Characterization of the residues in helix 8 of the human beta1-adrenergic receptor that are involved in coupling the receptor to G proteins. J Biol Chem. 2006 May 5;281(18):12896-907. Epub 2006 Feb 24. PMID: 16500896

view complete list of references (pubmed link)