Identification of a peptide arising from the specific post-translation processing of secretogranin II.
The biological role of secrotogranin II is unknown but it has been suggested that the protein may function as a precursor of one or more biologically active neuroendocrine peptides. We have isolated a 33 amino acid-residue peptide from the brain of the frog Rana ridibunda that shows strong (82%) homology with human presecretogranin II-(182-204)-peptide. This region of secretogranin II has also been very strongly conserved in the rat and bovine proteins. Analysis of the nucleotide sequence of the mammalian secretogranin II cDNAs indicates that the peptide sequence is flanked by two Lys-Arg dibasic residue processing sites. It is proposed, therefore, that this fragment represents a specific product of the post-translational processing of secretogranin II and, by analogy with peptides derived from chromogranin A, may be important in the regulation of neurosecretion.
Vaudry
H
H
European Institute for Peptide Research, Laboratory of Molecular Endocrinology, URA 650, UA INSERM, University of Rouen, Mont-Saint-Aignan, France.
Conlon
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism; D002864:Chromogranins; D006801:Humans; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011895:Rana ridibunda; D016415:Sequence Alignment
D002864:Chromogranins; D011506:Proteins