No abstract

src homology 2 (SH2)-containing protein-tyrosine phosphatase SHP2 is known to transduce positive signals from activated receptor protein-tyrosine kinases such as platelet-derived growth factor receptor (PDGFR) beta and insulin receptor. Here, we demonstrate the physiological expression of SHP2 in rats. In northern and western blot analyses, SHP2 expressions were recognized in all tissues, but their expression levels varied significantly among tissues: it is lowest in the liver and kidney. Immunohistochemical staining and in situ hybridization showed SHP2 was expressed ubiquitously but predominantly in vascular smooth muscle cells (SMC). During the development of granulations. SHP2 was expressed predominantly in vascular SMC and also highly expressed in capillary cells. The functional associations of SHP2 with PDGFR beta, which transduces major growth signals in vascular SMC, identify a crucial function of SHP2 in blood vessels in consert with PDGFR beta.

Abstract.The localization of cyclooxygenase and prostaglandin 12 synthase in human female reproductive organs was examined by immunohistochemistry. Cyclooxygenase was localized in the cytoplasm of various cell types. The extent of cyclooxygenase expression in endometrial epithelial cells varied with the menstrual cycle, showing a peak at the secretory phase. Cyclooxygenase was also detected in the secretory cells, but not in the ciliated cells, of the fallopian tubes. Prostaglandin I2 synthase was detected in the cytoplasm of myometrial cells throughout the menstrual cycle and during pregnancy. The results suggest that cyclooxygenase expression in endometrial epithelial cells may be regulated by ovarian hormones, and that the localization of cyclooxygenase in secretory cells--but not ciliated cells--in the fallopian tube may reflect the different functions of these two cell types.