catecholamine 英 /ˌkætəˈkɒləˌmiːn/ 美 /ˌkætəˈtʃoʊləˌmɪn; ˌkætəˈkoʊləˌmin/
释 义 n. 儿茶酚胺
例 句 Primary culture of human embryonic hepatocytes was employed to study the effects of catecholamine and thrombin on the secretion of histidine rich glycoprotein(HRG). 采用人胎肝细胞原代培养方法，观察儿茶酚胺和凝血酶对肝细胞富组氨酸糖蛋白（HRG）分泌的影响。
作者： Chin-Chyuan Chang
期刊：Dev Com Immunol
Through specific signal transduction pathways, multiple cellular processes including differentiation, cell growth, secretion and muscle contraction were regulated by varied isotypes of protein kinase C (PKC) following the difference of their tissue distributions and localization within the cells. Cells response to signals through phosphorylation of critical targeted proteins following triggering the turnover of inositol phospholipids (IPs), which generates diacylglycerol (DG) and mobilizes Ca2+, are activated to result in the cell activation. Upon elucidating the primary structure and biochemical properties, and the difference of demand on DGs, phorbol esters, acidic phospholipids such as phosphatidylserine (PS), and the presence of Ca2+, there were three classes including classical or conventional (c)PKC, novel (n)PKC, and atypical (a)PKC isotypes reviewed by Ohno and Nishizuka. Base on the well preserved catalytic and regulatory domains peptidic sequences of the different vertebrate PKC families, the use of antibodies could be the strategy for detecting specific protein with antibodies obtained against mammalian molecules in invertebrates. In mollusks, different isotypes of cPKC (DG- and Ca2+-dependent) and nPKC (DGdependent and Ca2+-independent) were detected in the cytosolic fraction in the adductor and retractor muscles of Mytilus galloprovincialis by immunoblot analysis. In crustaceans, PKCα (a cPKC isotype) in regulating vitellogenin uptake in the ovary of Cherax quadricarinatus was identified by rabbit polyclonal anti-PKC isoenzyme antibodies. In Penaeus monodon, using mammalian PKC antibodies, PKCδ (an nPKC isotype) was purified from the hepatopancreas. In addition, the preserved domains sequences of aPKC in Macrobrachium rosenbergii and nPKC in Litopenaeus vannamei were isolated using designed degenerate primers and the rapid amplification of cDNA ends. Using staurosporine (a PKC inhibitor) and phorbol 12- myristate 13-acetate (PMA, a PKC activator), Johansson and Söderhäll reported that the degranulation of crayfish granular blood cells and the release of the proPO activating system can be mediated by two endogenous ligands, a 76-kDa cell adhesion protein (peroxinectin) or a β-l,3-glucan binding protein through PKC signaling transduction. Moreover, Ng et al. indicated that extracellular traps for phagocytosis were revealed in L. vannamei responding to PMA stimulation. These revealed that not only the structural domains of PKC isotypes but also the pharmaceuticals for PKC might be similar in either vertebrates or invertebrates.