Molecular characterization of frog chromogranin B reveals conservation of selective sequences encoding potential novel regulatory peptides

FEBS Lett. 2002 Jan 30;511(1-3):127-32. doi: 10.1016/s0014-5793(01)03296-3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anura / genetics*
  • Autoradiography
  • Brain / metabolism
  • Chromogranin B
  • Chromogranins / chemistry*
  • Chromogranins / genetics
  • Chromogranins / metabolism*
  • Cloning, Molecular
  • Conserved Sequence / genetics*
  • Humans
  • In Situ Hybridization
  • Molecular Sequence Data
  • Organ Specificity
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / metabolism*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid

Substances

  • CHGB protein, human
  • Chromogranin B
  • Chromogranins
  • Peptides
  • RNA, Messenger

Associated data

  • GENBANK/AA453421