+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region

Embo Journal 6(5): 1203-1211
The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region
We have determined and analyzed the primary structure of human secretogranin I (chromogranin B), a tyrosine-sulfated secretory protein found in a wide variety of peptidergic endocrine cells. A 2.5-kb cDNA clone, hybridizing to an mRNA of similar length, was isolated from a cDNA library of human pheochromocytoma. The identity of the clone was established by comparison of its deduced amino acid sequence with N-terminal and several internal secretogranin I sequences as well as by immunoprecipitation of the protein produced by in vitro transcription-translation of the cloned cDNA. Secretogranin I is a 657 amino acid long polypeptide of 76 kd and is preceded by a cleaved N-terminal signal peptide of 20 residues. Comparison of the predicted amino acid sequence of human secretogranin I with that of bovine chromogranin A reveals significant homologies near the N termini and at the C termini. The N-terminal homologous domains contain the only two cysteine residues of both proteins and form disulfide-stabilized loop structures. The sequences between the homologous terminal domains in both proteins differ but are characterized by a remarkable hydrophilicity, an abundance of acidic amino acids and potential dibasic cleavage sites for the generation of smaller, perhaps hormone-like, peptides.

Accession: 006740925

PMID: 3608978

Related references

Chromogranin A, chromogranin B and secretogranin II mRNAs in the pituitary and adrenal glands of various mammals. Regulation of chromogranin A, chromogranin B and secretogranin II mRNA levels by estrogen. Laboratory Investigation; A Journal of Technical Methods and Pathology 67(3): 394-404, 1992

Identification of gastroenteropancreatic neuroendocrine cells in normal and neoplastic human tissue with antibodies against synaptophysin, chromogranin A, secretogranin I (chromogranin B), and secretogranin II. Gastroenterology 95(5): 1364-1374, 1988

Measurements of chromogranin A, chromogranin B (secretogranin I), chromogranin C (secretogranin II) and pancreastatin in plasma and urine from patients with carcinoid tumours and endocrine pancreatic tumours. Journal of Endocrinology 144(1): 49-59, 1995

Identification of normal and neoplastic gastroenteropancreatic neuroendocrine cells with antibodies against synaptophysin chromogranin a secretogranin i chromogranin b and secretogranin ii. Gastroenterology 94(5 PART 2): A496, 1988

Preparation and characterization of anti-human chromogranin A and chromogranin B (secretogranin I) monoclonal antibodies. Molecular and Cellular Probes 3(1): 87-101, 1989

Immunolocalization of secretogranin II, chromogranin A, and chromogranin B in differentiating human neuroblastoma cells. European Journal of Cell Biology 58(2): 383-389, 1992

Interaction of calcium with porcine adrenal chromogranin A (secretory protein-I) and chromogranin B (secretogranin I). American Journal of Physiology 257(2 Pt 1): E247-E254, 1989

Regulation of chromogranin a and chromogranin B (secretogranin I) synthesis in bovine cultured chromaffin cells. Journal of Neuroendocrinology 3(6): 669-677, 1991

Immunohistochemical demonstration of chromogranin A, chromogranin B, and secretogranin II in extra-adrenal paragangliomas. Modern Pathology 7(3): 347-353, 1994

Differential regulation of chromogranin A, chromogranin B and secretogranin II in rat brain by phencyclidine treatment. Neuroscience 104(2): 325-333, 10 May, 2001