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Molecular characterization of frog chromogranin B reveals conservation of selective sequences encoding potential novel regulatory peptides 1
Author(s) -
Aït-Ali Djida,
Turquier Valérie,
Alexandre David,
Grumolato Luca,
Jégou Sylvie,
Vaudry Hubert,
Anouar Youssef
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03296-3
Subject(s) - chromogranin a , biogenesis , biology , rana ridibunda , peptide sequence , conserved sequence , homology (biology) , cloning (programming) , amino acid , molecular cloning , microbiology and biotechnology , biochemistry , gene , endocrinology , immunohistochemistry , computer science , immunology , programming language
Chromogranin B (CgB) is a member of the granin family of neuroendocrine secretory proteins, which has been proposed to play a role in secretory granule biogenesis and as a precursor to bioactive peptides. The cloning of CgB in a phylogenetically distant vertebrate, the frog Rana ridibunda , reveals a modest overall homology (35–40%) with mammalian CgB. However, the sequences of the N‐ and C‐terminal regions are more highly conserved (57–65% amino acid identity) and may give rise to novel regulatory peptides. In frog, intense expression of CgB mRNA was observed in particular structures of the brain and in the distal lobe of the pituitary.