Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 17 August 1984:
Vol. 225. no. 4663, pp. 734 - 737
DOI: 10.1126/science.6547780
Prev | Table of Contents | Next

Articles

Science, Vol 225, Issue 4663, 734-737
Copyright © 1984 by American Association for the Advancement of Science

articles

Processing of proenkephalin is tissue-specific

D Liston, G Patey, J Rossier, P Verbanck, and JJ Vanderhaeghen

Most neuropeptides are synthesized as large precursor proteins. These precursors undergo a maturation process involving several proteolytic events that generate the biologically active peptides. The enzymatic mechanisms underlying this processing are still largely unknown. The processing of the precursor protein proenkephalin was studied in two different bovine tissues, the hypothalamus and adrenal medulla. The high molecular weight enkephalin-containing peptides that accumulate in these two tissues were found to be different, indicating the existence of two processing pathways for this neuropeptide precursor.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Cloning of Endopin 1, a Novel Serpin Localized to Neurosecretory Vesicles of Chromaffin Cells. INHIBITION OF BASIC RESIDUE-CLEAVING PROTEASES BY ENDOPIN 1.
S.-R. Hwang, B. Steineckert, S. Yasothornsrikul, C. A. Sei, T. Toneff, J. Rattan, and V. Y. H. Hook (1999)
J. Biol. Chem. 274, 34164-34173
   Abstract »    Full Text »    PDF »
The Biology of pro-Thyrotropin-Releasing Hormone-Derived Peptides.
E. A. Nillni and K. A. Sevarino (1999)
Endocr. Rev. 20, 599-648
   Abstract »    Full Text »
The Kunitz Protease Inhibitor Form of the Amyloid Precursor Protein (KPI/APP) Inhibits the Proneuropeptide Processing Enzyme Prohormone Thiol Protease (PTP). COLOCALIZATION OF KPI/APP AND PTP IN SECRETORY VESICLES.
V. Y. H. Hook, C. Sei, S. Yasothornsrikul, T. Toneff, Y.-H. Kang, S. Efthimiopoulos, N. K. Robakis, and W. Van Nostrand (1999)
J. Biol. Chem. 274, 3165-3172
   Abstract »    Full Text »    PDF »
Intracellular Sites of Prothyrotropin-releasing Hormone Processing.
I. P. d. l. Cruz and E. A. Nillni (1996)
J. Biol. Chem. 271, 22736-22745
   Abstract »    Full Text »    PDF »
Purification and Characteristics of the Candidate Prohormone Processing Proteases PC2 and PC1/3 from Bovine Adrenal Medulla Chromaffin Granules.
A. V. Azaryan, T. J. Krieger, and V. Y. H. Hook (1995)
J. Biol. Chem. 270, 8201-8208
   Abstract »    Full Text »    PDF »
Expression and cell type--specific processing of human preproenkephalin with a vaccinia recombinant.
G Thomas, E Herbert, and D. Hruby (1986)
Science 232, 1641-1643
   Abstract »    PDF »
Processing of Proenkephalin-A in Bovine Chromaffin Cells. IDENTIFICATION OF NATURAL DERIVED FRAGMENTS BY N-TERMINAL SEQUENCING AND MATRIX-ASSISTED LASER DESORPTION IONIZATION-TIME OF FLIGHT MASS SPECTROMETRY.
Y. Goumon, K. Lugardon, P. Gadroy, J.-M. Strub, I. D. Welters, G. B. Stefano, D. Aunis, and M.-H. Metz-Boutigue (2000)
J. Biol. Chem. 275, 38355-38362
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)