help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by El Meskini, R.
Right arrow Articles by Ouafik, L'H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by El Meskini, R.
Right arrow Articles by Ouafik, L'H.
Endocrinology Vol. 138, No. 1 379-388
Copyright © 1997 by The Endocrine Society


ARTICLES

Estrogen Regulation of Peptidylglycine {alpha}-Amidating Monooxygenase Expression in Anterior Pituitary Gland

Rajaâ El Meskini, Christine Delfino, Françoise Boudouresque, Micheline Hery, Charles Oliver and L’Houcine Ouafik

INSERM U297, Institut Federatif de Recherche Jean Roche, Faculté de Médecine Nord, 13916 Marseille, Cedex 20, France

Address all correspondence and requests for reprints to: Dr. L’Houcine Ouafik, INSERM U297, IFR Jean Roche, Faculté de Médecine Nord, Bd Pierre Dramard, 13916 Marseille Cedex 20, France.

The pituitary is a rich source of peptidylglycine {alpha}-amidating monooxygenase (PAM). This bifunctional protein contains peptidylglycine {alpha}-hydroxylating monooxygenase (PHM) and peptidyl-{alpha}-hydroxyglycine {alpha}-amidating lyase catalytic domains necessary for the two-step formation of {alpha}-amidated peptides from their COOH-terminal glycine extended precursors. Expression of PAM was evaluated in the anterior pituitary of intact cycling adult female rat and after experimental manipulation of estrogen status. PAM messenger RNA (mRNA) levels showed changes inversely related to the physiological variations of plasma estrogen levels during the estrous cycle. Chronic treatment of ovariectomized (OVX) rats with 17 ß-estradiol decreased PAM mRNA levels to values comparable with those found in intact rats at proestrus. In situ hybridization of anterior pituitary sections using 35S-labeled full length RNA antisense transcripts of rat PAM-1 complementary DNA showed that 17 ß-estradiol treatment induced an overall decrease of the hybridization signal, as compared with OVX rats. Progesterone treatment did not change PAM mRNA levels both in OVX or OVX + E2 rats. Based on Northern blot analysis and amplification of fragments derived from rat PAM-1 by RT-PCR, it was found that estrogen status does not affect the distribution of PAM mRNA among its various alternatively spliced forms. In OVX 17 ß-estradiol treated rats, the specific activity of PAM in the anterior pituitary decreased in both soluble and particulate fractions compared with OVX animals. Western blot analysis demonstrated a 105-kDa PAM protein in particulate fractions prepared from OVX and OVX-17 ß-estradiol treated animals. The soluble fraction from OVX animals contained major PAM proteins of 105, 95, 84, 75, and 45 kDa, and 17 ß-estradiol treatment caused a decrease in the prevalence of these proteins. These results indicate that estrogens are involved, either directly or indirectly, in regulating the expression of PAM in several cell types in the anterior pituitary gland.




This article has been cited by other articles:


Home page
J EndocrinolHome page
A Tury, G Mairet-Coello, F Poncet, C Jacquemard, P Y Risold, D Fellmann, and B Griffond
QSOX sulfhydryl oxidase in rat adenohypophysis: localization and regulation by estrogens
J. Endocrinol., November 1, 2004; 183(2): 353 - 363.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
P. Rocchi, F. Boudouresque, A. J. Zamora, X. Muracciole, E. Lechevallier, P.-M. Martin, and L'H. Ouafik
Expression of Adrenomedullin and Peptide Amidation Activity in Human Prostate Cancer and in Human Prostate Cancer Cell Lines
Cancer Res., February 1, 2001; 61(3): 1196 - 1206.
[Abstract] [Full Text]


Home page
EndocrinologyHome page
R. El Meskini, R. E. Mains, and B. A. Eipper
Cell Type-Specific Metabolism of Peptidylglycine {alpha}-Amidating Monooxygenase in Anterior Pituitary
Endocrinology, August 1, 2000; 141(8): 3020 - 3034.
[Abstract] [Full Text] [PDF]


Home page
J. Pharmacol. Exp. Ther.Home page
G. P. Mueller, W. J. Driscoll, and B. A. Eipper
In Vivo Inhibition of Peptidylglycine-alpha -Hydroxylating Monooxygenase by 4-Phenyl-3-Butenoic Acid
J. Pharmacol. Exp. Ther., September 1, 1999; 290(3): 1331 - 1336.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
R. E. Meskini, C. Delfino, F. Boudouresque, C. Oliver, P.-M. Martin, and L'H. Ouafik
Evidence of high expression of peptidylglycine alpha -amidating monooxygenase in the rat uterus: Estrogen regulation
PNAS, June 9, 1998; 95(12): 7191 - 7196.
[Abstract] [Full Text] [PDF]


Home page
J. Histochem. Cytochem.Home page
M. Grino and A. J. Zamora
An In Situ Hybridization Histochemistry Technique Allowing Simultaneous Visualization by the Use of Confocal Microscopy of Three Cellular mRNA Species in Individual Neurons
J. Histochem. Cytochem., June 1, 1998; 46(6): 753 - 760.
[Abstract] [Full Text]


Home page
EndocrinologyHome page
S. Fraboulet, F. Boudouresque, C. Delfino, and L'H. Ouafik
Identification of a Novel cis-Element in the 3'-Untranslated Region of Mammalian Peptidylglycine {alpha}-Amidating Monooxygenase Messenger Ribonucleic Acid
Endocrinology, March 1, 1998; 139(3): 894 - 904.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
R. El Meskini, F. Boudouresque, and L'H. Ouafik
Estrogen Regulation of Peptidylglycine {alpha}-Amidating Monooxygenase Messenger Ribonucleic Acid Levels by a Nuclear Posttranscriptional Event
Endocrinology, December 1, 1997; 138(12): 5256 - 5265.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. Amir-Ahmady and L. M. Salati
Regulation of the Processing of Glucose-6-phosphate Dehydrogenase mRNA by Nutritional Status
J. Biol. Chem., March 23, 2001; 276(13): 10514 - 10523.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1997 by The Endocrine Society