Biochemical identification of renin in human pheochromocytoma.
A high activity of renin was demonstrated in human pheochromocytoma tissue. This activity was inhibited by specific antibody raised against human renal renin, indicating that it was not due to the nonspecific actions of proteases such as cathepsin D. The specific renin shared some biochemical features with well-known kidney renin, such as molecular weight (47,000 daltons), optimum pH (6.0), the presence of trypsin-activatable inactive renin, and glycoprotein nature. However, the isoelectrofocusing pattern of renin from the pheochromocytoma differed from that of kidney and plasma renins hitherto reported, a discrepancy which could be interpreted as evidence for endogenous synthesis of the enzyme. Furthermore, angiotensin converting enzyme activity was found in the tissue. Since pheochromocytoma is considered to be of neural crest origin, these results provide biochemical and immunological evidence for the presence of the renin-angiotensin cycle within human neuronal cells.
D000293:Adolescent; D000310:Adrenal Gland Neoplasms / Q000032:analysis*; D000328:Adult; D004789:Enzyme Activation; D005260:Female; D006023:Glycoproteins / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008297:Male; D008970:Molecular Weight; D007703:Peptidyl-Dipeptidase A / Q000032:analysis; D010673:Pheochromocytoma / Q000032:analysis*; D012083:Renin / Q000032:analysis*
D006023:Glycoproteins; D007703:Peptidyl-Dipeptidase A; D012083:Renin