Skip Navigation

This Article
Right arrow Print PDF (2483K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (53)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Thekkumkara, T. J.
Right arrow Articles by Sen, G. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Thekkumkara, T. J.
Right arrow Articles by Sen, G. C.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 4 683-687
© 1992


Articles

Use of alternative polyadenylation sites for tissue-specific transcription of two angiotensin-converting enzyme mRNAs

Thomas J. Thekkumkara, William Livingston, III, Ravi S. Kumar and Ganes C. Sen*

Department of Molecular Biology, The Cleveland Clinic Foundation 9500 Euclid Avenue, Cleveland, OH 44195, USA

*To whom correspondence should be addressed

Received December 12, 1991. Revised January 16, 1992. Accepted January 16, 1992.

The pulmonary isozyme of rabbit angiotensin-converting enzyme (ACE) is encoded by an mRNA of about 5 kb. cDNA clones corresponding to different parts of this mRNA have been isolated and the complete nucleotide sequences of both the coding and non-coding regions of the mRNA have been determined. The encoded protein has 1309 residues with a 33 amino acids-long signal peptide at the amino terminus and a potential membrane-anchoring domain near the carboxyl terminus. There is a strong sequence homology between two regions of the rabbit cDNA and between the rabbit, human, and mouse cDNAs. Comparison of the nucleotide sequences of the 3' untranslated regions of rabbit pulmonary and testicular ACE cDNAs revealed that the testicular cDNA Is nested within the pulmonary cDNA at the 3' end. A rabbit genomlc clone encompassing this region was isolated and partially sequenced. It was shown that the gene contains two potential polyadenylation sites 628 bp apart within one exon. Northern analyses with an appropriate oligonucleotide probe confirmed that the proximal polyadenylation site is used exclusively for terminating the testicular mRNA whereas the distal one is used exclusively for the pulmonary mRNA. These results demonstrated that the transcription of the two mRNAs encoding the two ACE Isozymes not only Initiates at two alternative tissue-specific sites which are 5.7 kb apart but the mRNAs also get polyadenylated at two alternative sites which are 628 bp apart.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Physiol. Rev.Home page
M. Paul, A. Poyan Mehr, and R. Kreutz
Physiology of local Renin-Angiotensin systems.
Physiol Rev, July 1, 2006; 86(3): 747 - 803.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. P. Kessler, P. deS. Senanayake, T. S. Scheidemantel, J. B. Gomos, T. M. Rowe, and G. C. Sen
Maintenance of Normal Blood Pressure and Renal Functions Are Independent Effects of Angiotensin-converting Enzyme
J. Biol. Chem., May 30, 2003; 278(23): 21105 - 21112.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. P. Kessler, J. B. Gomos, T. S. Scheidemantel, T. M. Rowe, H. L. Smith, and G. C. Sen
The Germinal Isozyme of Angiotensin-converting Enzyme Can Substitute for the Somatic Isozyme in Maintaining Normal Renal Structure and Functions
J. Biol. Chem., February 1, 2002; 277(6): 4271 - 4276.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
A. Miano, A. Gobbetti, M. Zerani, L. Quassinti, E. Maccari, O. Murri, D. Amici, and M. Bramucci
Different modulation of aromatase activity in frog testis in vitro by ACE and ANG II
Am J Physiol Regulatory Integrative Comp Physiol, November 1, 1999; 277(5): R1261 - R1267.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. P. Kessler, T. M. Rowe, J. A. Blendy, R. P. Erickson, and G. C. Sen
A Cyclic AMP Response Element in the Angiotensin-converting Enzyme Gene and the Transcription Factor CREM Are Required for Transcription of the mRNA for the Testicular Isozyme
J. Biol. Chem., April 17, 1998; 273(16): 9971 - 9975.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
R. Sadhukhan, G. C. Sen, R. Ramchandran, and I. Sen
The distal ectodomain of angiotensin-converting enzyme regulates its cleavage-secretion from the cell surface
PNAS, January 6, 1998; 95(1): 138 - 143.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Sadhukhan and I. Sen
Different Glycosylation Requirements for the Synthesis of Enzymatically Active Angiotensin-converting Enzyme in Mammalian Cells and Yeast
J. Biol. Chem., March 15, 1996; 271(11): 6429 - 6434.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. J. Cornell, T. A.Williams, N. S. Lamango, D. Coates, P. Corvol, F. Soubrier, J. Hoheisel, H. Lehrach, and R. E. Isaac
Cloning and Expression of an Evolutionary Conserved Single-domain Angiotensin Converting Enzyme from Drosophila melanogaster
J. Biol. Chem., June 9, 1995; 270(23): 13613 - 13619.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. G. Thomas, T. J. Thekkumkara, T. J. Motel, and K. M. Baker
Stable Expression of a Truncated AT[IMAGE] Receptor in CHO-K1 Cells
J. Biol. Chem., January 6, 1995; 270(1): 207 - 213.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. R. Santhamma and I. Sen
Specific Cellular Proteins Associate with Angiotensin-converting Enzyme and Regulate Its Intracellular Transport and Cleavage-Secretion
J. Biol. Chem., July 21, 2000; 275(30): 23253 - 23258.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. P. Kessler, T. M. Rowe, J. B. Gomos, P. M. Kessler, and G. C. Sen
Physiological Non-equivalence of the Two Isoforms of Angiotensin-converting Enzyme
J. Biol. Chem., August 18, 2000; 275(34): 26259 - 26264.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.