Catecholamine synthesizing enzymes in rat pheochromocytoma PC-12 cells
The purification of catecholamine synthesizing enzymes from rat adrenal glands or brain requires a large number of animals and elaborate procedures are yielding small amounts of purified enzyme preparations. Furthermore, rat adrenal tyrosine hydroxylase (TH) tends to aggregate and this hampers its extensive purification. The availability of transplantable rat pheochromocytoma tumors (Warren and Chute, 1972), and of cultured rat pheochromocytoma cells (Tischler and Greene, 1975), provides an excellent source for purification of rat catecholamine synthesizing enzyme. Indeed, we have recently purified TH from a clonal pheochromocytoma PC-12 cell line (Markey et al., 1979) and dopaminebeta-hydroxylae (DβH) from rat pheochromocytoma tumors (Fong et al., 1980). In this presentation, we will review the characteristics of rat pheochromocytoma TH and DβH and we will describe some of our recent studies with DβH in cultured PC-12 cells.
KeywordsNerve Growth Factor Tyrosine Hydroxy Purify Enzyme Preparation Protein Kinase Phosphorylation Tyrosine Hydroxy
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- This study is supported by NINDS grant #06801 and NIMH grant #02717.Google Scholar