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Am J Physiol Gastrointest Liver Physiol 255: G113-G120, 1988;
0193-1857/88 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 255, Issue 1 113-G120, Copyright © 1988 by American Physiological Society

ARTICLES

Functional somatostatin receptors on a rat pancreatic acinar cell line

N. Viguerie, N. Tahiri-Jouti, J. P. Esteve, P. Clerc, C. Logsdon, M. Svoboda, C. Susini, N. Vaysse and A. Ribet
Institut National de la Sante et de la Recherche Medicale U. 151, CHU Rangueil, Toulouse, France.

Somatostatin receptors from a rat pancreatic acinar cell line, AR4-2J, were characterized biochemically, structurally, and functionally. Binding of 125I-[Tyr11]somatostatin to AR4-2J cells was saturable, exhibiting a single class of high-affinity binding sites (Kd = 0.55 +/- 0.06 nM) with a maximal binding capacity of 258 +/- 20 fmol/10(6) cells. Somatostatin receptor structure was analyzed by covalently cross-linking 125I-[Tyr11]somatostatin to its plasma membrane receptors. Gel electrophoresis and autoradiography of cross-linked proteins revealed a peptide (Mr 80,000) containing the somatostatin receptor. Somatostatin inhibited vasoactive intestinal peptide (VIP)-stimulated adenosine 3',5'-cyclic monophosphate (cAMP) formation in a dose-dependent manner. The concentration of somatostatin that caused half-maximal inhibition of cAMP formation (IC50 = 0.4 nM) was close to the receptor affinity for somatostatin. Pertussis toxin pretreatment of AR4-2J cells prevented somatostatin inhibition of VIP-stimulated cAMP formation as well as somatostatin binding. We conclude that AR4-2J cells exhibit functional somatostatin receptors that retain both specificity and affinity of the pancreatic acinar cell somatostatin receptors and act via the pertussis toxin-sensitive guanine nucleotide-binding protein Ni to inhibit adenylate cyclase.


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