Clinical Chemistry Link to Randox Laboratories Web Site
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Clinical Chemistry 46: 234-241, 2000;
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via ISI Web of Science (4)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rose, A. M.
Right arrow Articles by Valdes, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rose, A. M.
Right arrow Articles by Valdes, R., Jr
Related Collections
Right arrow Molecular Diagnostics and Genetics
Right arrow Proteomics and Protein Markers
Right arrow Drug Monitoring and Toxicology
Right arrow Endocrinology and Metabolism
(Clinical Chemistry. 2000;46:234-241.)
© 2000 American Association for Clinical Chemistry, Inc.


Articles

Sodium Pump Isoforms in Xenotransplantation: Importance of Biochemical Compatibility

Andrea M. Rose1,1, Hassan M. Qazzaz1, Nina Zolotarjova1, Brenda J. Mellett1, Alvin W. Martin1 and Roland Valdes Jr1,2,a

Departments of
1 Pathology and Laboratory Medicine and
2 Biochemistry and Molecular Biology, University of Louisville, School of Medicine, Louisville, KY 40292.
a Address correspondence to this author at: Department of Pathology and Laboratory Medicine, University of Louisville, Louisville, KY 40292. Fax 502-852-1177; e-mail rvaldes{at}louisville.edu

Background: Xenotransplantation of pig hearts to humans could be hampered by the reportedly reduced affinity for digoxin of pig heart. We examined the hypothesis that expression of the individual {alpha}-subunit isoforms of the sodium pump [Na+,K+-ATPase (NKA)], the receptor for the plant-derived cardiac glycosides, may be responsible for this difference.

Methods: We used a NKA-inhibition assay in combination with Western analysis, immunohistochemistry, and phosphorylation of the NKA {alpha} subunit to identify the distribution and expression of {alpha} isoforms in four chambers of porcine and human hearts.

Results: We confirmed that tissue from porcine heart is less sensitive to digitalis (IC50 = 1740 nmol/L) when compared with human heart (IC50 = 840 nmol/L), whereas porcine cerebral cortex-mix had an affinity comparable to that of human heart (IC50 = 910 nmol/L). Our data show that porcine cerebral cortex-mix and human heart contain all three {alpha} isoforms, whereas porcine heart expresses only the {alpha}1 isoform.

Conclusions: The different expressions of sodium pump isoforms in human vs porcine cardiac tissues suggests that porcine hearts may not be pharmacologically or endocrinologically compatible when used in humans. Studies of both pharmacologic and endocrinologic tissue compatibility are needed prior to selection of organs for xenotransplantation.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the American Association for Clinical Chemistry.