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Activation In Vitro of Somatostatin Receptor Subtypes 2, 3, or 4 Stimulates Protein Tyrosine Phosphatase Activity in Membranes from Transfected Ras-Transformed NIH 3T3 Cells: Coexpression with Catalytically Inactive SHP-2 Blocks Responsiveness

Howard Hughes Medical Institute and the Center for Cell Signaling Departments of Internal Medicine and Pharmacology University of Virginia Charlottesville, Virginia 22908

Somatostatin receptors (sstr) subtypes 1–5 were transiently expressed in NIH 3T3 cells stably transformed with Ha-Ras^G12V to assess the ability of each receptor to stimulate protein tyrosine phosphatase (PTPase) activity in vitro. Treatment of membranes from sstr₂-, sstr₃-, or sstr₄-expressing cells with somatostatin-14 plus guanyl-5'-yl imidodiphosphate (GMPPNP) increased PTPase activity, and this stimulation was pertussis toxin-sensitive. Somatostatin alone, GMPPNP alone, or somatostatin plus GDP were ineffective under these conditions. sstr₁ and sstr₅ failed to increase PTPase activity although both receptors were expressed, as assessed by appearance of high-affinity binding sites for [¹²⁵I-Tyr¹¹]somatostatin-14. Somatostatin plus GMPPNP stimulated PTPase activity in vitro when sstr₂ was coexpressed with wild type PTP1B or a Cys to Ser (C/S), catalytically inactive PTP1B or with wild type SH2-domain containing PTPase SHP-2. However, coexpression with catalytically inactive C/S SHP-2 abrogated this response. Thus, three of the five cloned sstr’s can couple to activate PTPase in this cellular background. Abrogation of the response by C/S SHP-2 strongly suggests, but does not prove, a role for SHP-2 in the mechanism.

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