JME
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

DOI: 10.1677/jme.0.0270031
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (28)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Martinez, A
Right arrow Articles by Cuttitta, F
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martinez, A
Right arrow Articles by Cuttitta, F
Journal of Molecular Endocrinology, Vol 27, Issue 1, 31-41
Copyright © 2001 by Society for Endocrinology

Articles

Alternative splicing of the proadrenomedullin gene results in differential expression of gene products

A Martinez, DL Hodge, M Garayoa, HA Young, and F Cuttitta


The adrenomedullin (AM) gene codifies for two bioactive peptides, AM and proAM N-terminal 20 peptide (PAMP). We have found two forms of the AM mRNA. Form A is devoid of introns and results in a prohormone containing both peptides. Form B retains the third intron, which introduces a premature stop codon, producing a shorter prohormone with only PAMP. Tissues with a higher B/A ratio were more immunoreactive for PAMP than for AM. The form B message was found in the cytoplasmic compartment, thus excluding that the longer message was a result of contaminating nuclear mRNA. Form B was found in cells that express PAMP but not AM. mRNA expression in a variety of cell lines was investigated by ribonuclease protection assay and form B was found in significant amounts in two of them. Treatments that modify AM expression, such as exposure to hypoxia, were shown to change the B/A ratio and the relative secretion of AM and PAMP, indicating that the splicing mechanism for AM can be modulated and is physiologically relevant. Analysis of the sequence of the third intron and the fourth exon of the AM gene found motifs compatible with a highly regulated alternative splicing mechanism.


This article has been cited by other articles:


Home page
 EndocrinologyHome page
D. L. Sackett, L. Ozbun, E. Zudaire, L. Wessner, J. M. Chirgwin, F. Cuttitta, and A. Martinez
Intracellular Proadrenomedullin-Derived Peptides Decorate the Microtubules and Contribute to Cytoskeleton Function
Endocrinology, June 1, 2008; 149(6): 2888 - 2898.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
S. Nobata, M. Ogoshi, and Y. Takei
Potent cardiovascular actions of homologous adrenomedullins in eels
Am J Physiol Regulatory Integrative Comp Physiol, May 1, 2008; 294(5): R1544 - R1553.
[Abstract] [Full Text] [PDF]

Home page
 J. Leukoc. Biol.Home page
E. Zudaire, S. Portal-Nunez, and F. Cuttitta
The central role of adrenomedullin in host defense
J. Leukoc. Biol., August 1, 2006; 80(2): 237 - 244.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
A. Martinez, E. Zudaire, S. Portal-Nunez, L. Guedez, S. K. Libutti, W. G. Stetler-Stevenson, and F. Cuttitta
Proadrenomedullin NH2-Terminal 20 Peptide Is a Potent Angiogenic Factor, and Its Inhibition Results in Reduction of Tumor Growth
Cancer Res., September 15, 2004; 64(18): 6489 - 6494.
[Abstract] [Full Text] [PDF]

Home page
 JNCI J Natl Cancer InstHome page
A. Martinez, M. Vos, L. Guedez, G. Kaur, Z. Chen, M. Garayoa, R. Pio, T. Moody, W. G. Stetler-Stevenson, H. K. Kleinman, et al.
The Effects of Adrenomedullin Overexpression in Breast Tumor Cells
J Natl Cancer Inst, August 21, 2002; 94(16): 1226 - 1237.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2001 by the Society for Endocrinology.