Hypertension, Vol 14, 435-444, Copyright © 1989 by American Heart Association
RJ Parmer, AH Koop, MT Handa and DT O'Connor
Chromogranin A (CgA) is the major soluble protein in catecholamine storage
vesicles. To gain insight into its function, we isolated CgA clones from a
size-selected lambda gt10 rat pheochromocytoma complementary DNA (cDNA)
library. The longest cDNA insert identified was 2.2 kb and encoded the
entire 462-amino acid open reading frame of rat CgA including an 18-amino
acid hydrophobic signal peptide. Comparison of rat CgA with the recently
published sequences of bovine CgA and human CgA revealed regions of strong
homology at the N-and COOH- termini as well as variant areas predominantly
in the middle portion of the molecule. Regions highly conserved and
therefore suggestive of functional importance included 1) multiple paired
basic residues, which may serve as proteolytic processing signals; 2) a
region homologous to porcine pancreastatin, a putative modulator of peptide
hormone release; and 3) a short hydrophobic disulfide loop region near the
N-terminus that may have a role in the targeting of CgA to secretory
vesicles. On the other hand, lack of conservation of the membrane
attachment sequence arginine-glycine-aspartic acid argues against its
functional importance in CgA. In addition, the presence of a unique
polyglutamine region in rat CgA points to a possible messenger RNA (mRNA)
splice junction. Northern blot experiments demonstrated the presence of an
approximately 2.2 kb rat CgA mRNA in a neuroendocrine distribution
(adrenal, brain, pheochromocytoma cells, but not skeletal muscle, heart, or
kidney). Southern blot studies were consistent with the presence of a
single CgA gene within the rat pheochromocytoma cell genome. Finally,
comparison of the present rat pheochromocytoma cDNA clones with those
recently obtained from normal rat adrenal gland reveals minor but
apparently real differences that suggest CgA microheterogeneity.
ARTICLES
Molecular cloning of chromogranin A from rat pheochromocytoma cells
Department of Medicine, University of California, San Diego.
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