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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Somatostatin receptors in pituitary and development of somatostatin receptor subtype-selective analogs.

Somatostatin receptor (SSTR) subtypes 1, 2, and 5 are expressed in the normal human pituitary. SSTR2 and SSTR5 are expressed in almost all growth hormone (GH) cell adenomas, and prolactin (PRL)- secreting tumors express SSTR5 more than SSTR2. SSTR4 is not detected in all pituitary adenoma subtypes, and SSTR1 and SSTR3 are expressed in about 50% of tumors. Human GH is regulated through ligand binding to both SSTR2 and SSTR5, but octreotide and lanreotide, the two clinically available somatostatin analogs, bind to human SSTR2 much better than to SSTR5. Novel SSTR2- and SSTR5- selective analogs with improved binding affinity for these receptor subtypes are highly potent in suppressing GH release from cultures of human fetal pituitaries or GH-cell adenomas. Only SSTR5-selective analogs suppress in vitro PRL secretion from cultured prolactinomas. A new SSTR2+5 bispecific analog with high affinity and selectivity for both SSTR2 and SSTR5, and a somatostatin analog with a unique broad receptor (SSTR1, 2, 3, and 5) binding profile, are both able to inhibit in vitro GH release in GH cell adenomas partially sensitive to octreotide. Recently, a somatostatindopamine hybrid molecule was introduced with potentially functional synergy on GH and PRL release. Using the expanding knowledge on SSTRs and their ligand activation, the development of novel pharmacologic concepts may open new opportunities for effective manipulation of this complex intracellular signaling system. These concepts may achieve better control of pituitary hormone hypersecretion, pituitary size, as well as antitumor effects in patients with SSTR-expressing tumors.[1]


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