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 23 March 1990:
Vol. 247. no. 4949, pp. 1477 - 1479
DOI: 10.1126/science.2181662
Prev | Table of Contents | Next

Articles

Science, Vol 247, Issue 4949, 1477-1479
Copyright © 1990 by American Association for the Advancement of Science

articles

HIP-70: a protein induced by estrogen in the brain and LH-RH in the pituitary

CV Mobbs, G Fink, and DW Pfaff

Department of Neurobiology and Behavior, Rockefeller University, New York, NY 10021.

Estrogen and luteinizing hormone-releasing hormone (LH-RH) interact to influence both behavior and gonadotropin release. However, little is known about the biochemical mechanisms that mediate the effects of these hormones or their interactions. The most prominent protein induced by estrogen in the ventromedial hypothalamus has the same amino-terminal sequence as the most prominent protein induced by LH-RH in the pituitary in vitro and in vivo; these proteins comigrate on two-dimensional gels. Furthermore, the hormonal induction may be caused by modification of a constitutive protein with the same molecular weight (70,000) but a slightly more acidic isoelectric point, whose level is inversely related to the level of the induced form after estrogen treatment. Thus estrogen and LH-RH may interact by additively or synergistically inducing this protein, which is called HIP-70.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A paradoxical inhibitory effect of oestradiol-17{beta} on GnRH self-priming in pituitaries from tamoxifen-treated rats.
J. E Sanchez-Criado, C. Bellido, R. Aguilar, and J. C Garrido-Gracia (2005)
J. Endocrinol. 186, 43-49
   Abstract »    Full Text »    PDF »
ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and Calnexin.
J. D. Oliver, H. L. Roderick, D. H. Llewellyn, and S. High (1999)
Mol. Biol. Cell 10, 2573-2582
   Abstract »    Full Text »
The Thiol-dependent Reductase ERp57 Interacts Specifically with N-Glycosylated Integral Membrane Proteins.
J. G. Elliott, J. D. Oliver, and S. High (1997)
J. Biol. Chem. 272, 13849-13855
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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