Differential secretion of proLHRH fragments in response to [K+], prostaglandin E2 and C kinase activation.

Journal Article (Journal Article)

ProLHRH contains the luteinizing hormone-releasing hormone (LHRH) decapeptide and a 56 amino acid peptide designated gonadotropin-releasing hormone-associated peptide (GAP). We studied the effects of various known secretagogues of LHRH on the in vitro release of proLHRH fragments from the median eminence (ME) and subsequently characterized these immunoreactive products according to molecular weight (MW). GAP- and LHRH-like immunoreactive (LI) materials were secreted simultaneously into the media under basal conditions. Prostaglandin E2 stimulated release of both peptides by approximately 2-fold. Both phorbol ester and [K+] stimulated release of GAP-LI by 4-fold and LHRH-LI by 9-fold over baseline levels. When materials from [K+]-stimulated media were separated according to MW by high performance size-exclusion chromatography, a single peak eluted at 1300 MW in the same position as synthetic LHRH. Two GAP-LI peaks were observed. One eluted in the void volume, while the predominant peak co-eluted with synthetic rat GAP1-56 at approximately 6500 MW. These results indicate that GAP and LHRH are co-secreted, that they are released as intact peptides, and that activation of different intracellular pathways may cause their differential secretion. These results emphasize the importance of using both in vitro and chromatographic methodologies to evaluate the changes which may occur in LHRH prohormone processing and secretion.

Full Text

Duke Authors

Cited Authors

  • Valenca, MM; Wetsel, WC; Culler, MD; Negro-Vilar, A

Published Date

  • January 1988

Published In

Volume / Issue

  • 55 / 1

Start / End Page

  • 95 - 100

PubMed ID

  • 3282935

International Standard Serial Number (ISSN)

  • 0303-7207

Digital Object Identifier (DOI)

  • 10.1016/0303-7207(88)90095-0


  • eng

Conference Location

  • Ireland