Processing of chromogranin A within chromaffin granules starts at C- and N-terminal cleavage sites

Thomas Wohlfarter, Reiner Fischer-Colbrie, Ruth Hogue-Angeletti, Lee E. Eiden, Hans Winkler

Research output: Contribution to journalArticle

74 Scopus citations

Abstract

Specific antisera were raised against synthetic peptide fragments of bovine chromogranin A. The soluble proteins of bovine chromaffin granules were subjected to two-dimensional immunoblotting with these antisera. The endogenous breakdown products of chromogranin A gave distinct patterns of immunostaining which enabled us to correlate these peptides with defined regions of the chromogranin A molecule. The results establish that within chromaffin granules degradation of chromogranin A by the endogenous proteases can start either at the C- or the N-terminal site.

Original languageEnglish (US)
Pages (from-to)67-70
Number of pages4
JournalFEBS Letters
Volume231
Issue number1
DOIs
StatePublished - Apr 11 1988

Keywords

  • Chromaffin granule
  • Chromogranin A
  • Proteolytic processing

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Wohlfarter, T., Fischer-Colbrie, R., Hogue-Angeletti, R., Eiden, L. E., & Winkler, H. (1988). Processing of chromogranin A within chromaffin granules starts at C- and N-terminal cleavage sites. FEBS Letters, 231(1), 67-70. https://doi.org/10.1016/0014-5793(88)80704-X