Abstract
Somatostatin (somatotropin release inhibitory factor, SRIF) is widely expressed in the body, where it controls cell proliferation and secretion via a family of highly homologous G protein-coupled receptors (GPCRs). SRIF analogs have demonstrated clinical utility in a range of endocrine, neuroendocrine and inflammatory disorders. We have investigated the role of SRIF in modulating the inflammatory response of the human synoviocyte, a critical cell in rheumatoid arthritis (RA). We utilized SRIF receptor-specific oligonucleotide primers to perform reverse transcriptase-polymerase chain reaction (RT-PCR) on synovial mRNA, thus identifying a molecular target for synovial SRIF action. Immunoblotting experiments with phospho-specific antiserum showed that SRIF controlled the ERK1/2 extracellular regulated kinases in rheumatoid synoviocytes. In addition, SRIF suppresses sodium vanadate sensitive protein tyrosine phosphatase activity as measured with the fluorescent substrate, 6,8 difluor-4-methylumbelliferryll phosphate (DiF MUP; Invitrogen, Carlsbad, CA). Taken together our results demonstrate that SRIF regulates intracellular signaling in rheumatoid synoviocytes.
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