JBC

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


     


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
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 reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Toyofuku, T.
Right arrow Articles by Zak, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Toyofuku, T.
Right arrow Articles by Zak, R.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 266, Issue 9, 5375-5383, 03, 1991

Characterization of cDNA and genomic sequences encoding a chicken phospholamban

T Toyofuku and R Zak
Department of Medicine, University of Chicago, Illinois 60637.

We report on the isolation and characterization of cDNA and genomic sequences encoding a chicken cardiac phospholamban. Three mRNAs, 0.6, 1.1, and 3.3 kilobase pairs in size, were detected in cardiac and slow- tonic muscle RNAs on Northern blots. We determined that these mRNAs differ in the length of their 3'-untranslated regions, perhaps because they utilize alternative polyadenylation signals. We studied the developmental and tissue-specific expression of phospholamban mRNA using nuclease mapping analysis. There appeared to be considerable homology between coding and 3'-untranslated regions of phospholamban mRNAs from cardiac and slow-tonic muscles during development, strongly suggesting that these mRNAs are encoded by the same gene. The phospholamban gene, which is present as a single copy in the chicken genome, is about 10 kilobase pairs long, with approximately 6.5 kilobase pairs representing the intron sequences. Primer extension and nuclease mapping analyses of the 5' end of the phospholamban mRNA showed that the three transcripts are initiated from the same initiation site. Analysis of the putative promoter region revealed "TATA box" and "CAAT box" sequences, putative muscle-specific elements, and a cyclic AMP-responsive element.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Poult. Sci.Home page
K.-C. Lin, K. Gyenai, R. L. Pyle, T. Geng, J. Xu, and E. J. Smith
Candidate Gene Expression Analysis of Toxin-Induced Dilated Cardiomyopathy in the Turkey (Meleagris gallopavo)
Poult. Sci., December 1, 2006; 85(12): 2216 - 2221.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. H. Gao, T. Tang, T. Guo, S. Q. Sun, J. R. Feramisco, and H. K. Hammond
Adenylyl Cyclase Type VI Gene Transfer Reduces Phospholamban Expression in Cardiac Myocytes via Activating Transcription Factor 3
J. Biol. Chem., September 10, 2004; 279(37): 38797 - 38802.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
K. W. Patberg, A. N. Plotnikov, A. Quamina, R. Z. Gainullin, A. Rybin, P. Danilo Jr, L. S. Sun, and M. R. Rosen
Cardiac Memory Is Associated With Decreased Levels of the Transcriptional Factor CREB Modulated by Angiotensin II and Calcium
Circ. Res., September 5, 2003; 93(5): 472 - 478.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
F. U Muller, P. Boknik, J. Knapp, B. Linck, H. Luss, J. Neumann, and W. Schmitz
Activation and inactivation of cAMP-response element-mediated gene transcription in cardiac myocytes
Cardiovasc Res, October 1, 2001; 52(1): 95 - 102.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
H. K. B. SIMMERMAN and L. R. JONES
Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function
Physiol Rev, October 1, 1998; 78(4): 921 - 947.
[Abstract] [Full Text] [PDF]


Home page
J. Pharmacol. Exp. Ther.Home page
B. Linck, P. Bokník, H. A. Baba, T. Eschenhagen, U. Haverkamp, E. Jäckel, L. R. Jones, U. Kirchhefer, J. Knapp, S. Läer, et al.
Long-term Beta Adrenoceptor-Mediated Alteration in Contractility and Expression of Phospholamban and Sarcoplasmic Reticulum Ca++-ATPase in Mammalian Ventricle
J. Pharmacol. Exp. Ther., July 1, 1998; 286(1): 531 - 538.
[Abstract] [Full Text]


Home page
Circ. Res.Home page
K. L. Koss, S. Ponniah, W. K. Jones, I. L. Grupp, and E. G. Kranias
Differential Phospholamban Gene Expression in Murine Cardiac Compartments : Molecular and Physiological Analyses
Circ. Res., August 1, 1995; 77(2): 342 - 353.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1991 by the American Society for Biochemistry and Molecular Biology.