Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
This Article
Right arrow Full Text
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 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 Reiner, M.
Right arrow Articles by Addicks, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reiner, M.
Right arrow Articles by Addicks, K.
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?
Journal of Histochemistry and Cytochemistry, Vol. 49, 1605-1610, December 2001, Copyright © 2001, The Histochemical Society, Inc.


BRIEF REPORT

Functional Interaction of Caveolin-1 and eNOS in Myocardial Capillary Endothelium Revealed by Immunoelectron Microscopy

Michael Reinera, Wilhelm Blocha, and Klaus Addicksa
a Department of Anatomy I, University of Cologne, Cologne, Germany

Correspondence to: Michael Reiner, Dept. of Anatomy I, University of Cologne, Joseph-Stelzmann-Str. 9, 50931 Köln/Cologne, Germany. E-mail: michael.reiner@uni-koeln.de

Immunogold labeling on samples of isolated perfused rat hearts embedded by an innovative low-temperature LR White procedure provided detailed insight into the interaction of caveolin-1 and endothelial NOS in myocardial capillary endothelium at the subcellular level. Separately, the localization of caveolin-1 and eNOS at caveolae under steady state conditions was visualized. A double-labeling experiment supported their close co-localization. Short-term bradykinin stimulation caused a detectable dissociation of eNOS from caveolin and its redistribution to different cell compartments, whereas caveolin itself remained stationary at caveolae. Morphometric analysis revealed that more than 80% of detectable eNOS was co-localized with caveolin-1 at caveolae under control conditions. After brief stimulation for 2 min with 10-7 M bradykinin, only 26% of the eNOS signals were associated with caveolin-1 and randomly distributed over the endothelial cells. After stimulation, eNOS was found at the plasmalemmal and intracellular membranes, freely in the cytoplasm, and at outer mitochondrial membranes. (J Histochem Cytochem 49:1605–1609, 2001)

Key Words: electron microscopy, caveolins, NO synthases, immunogold labeling, biological membranes, signal transduction, isolated perfused rat heart


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
Am. J. Physiol. Cell Physiol.Home page
C. Pott, D. Steinritz, B. Bolck, U. Mehlhorn, K. Brixius, R. H. G. Schwinger, and W. Bloch
eNOS translocation but not eNOS phosphorylation is dependent on intracellular Ca2+ in human atrial myocardium
Am J Physiol Cell Physiol, May 1, 2006; 290(5): C1437 - C1445.
[Abstract] [Full Text] [PDF]


Home page
J. Leukoc. Biol.Home page
R. Saini, S. Patel, R. Saluja, A. A. Sahasrabuddhe, M. P. Singh, S. Habib, V. K. Bajpai, and M. Dikshit
Nitric oxide synthase localization in the rat neutrophils: immunocytochemical, molecular, and biochemical studies
J. Leukoc. Biol., March 1, 2006; 79(3): 519 - 528.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Gao, J. Chen, S. V. Brodsky, H. Huang, S. Adler, J. H. Lee, N. Dhadwal, L. Cohen-Gould, S. S. Gross, and M. S. Goligorsky
Docking of Endothelial Nitric Oxide Synthase (eNOS) to the Mitochondrial Outer Membrane: A PENTABASIC AMINO ACID SEQUENCE IN THE AUTOINHIBITORY DOMAIN OF eNOS TARGETS A PROTEINASE K-CLEAVABLE PEPTIDE ON THE CYTOPLASMIC FACE OF MITOCHONDRIA
J. Biol. Chem., April 16, 2004; 279(16): 15968 - 15974.
[Abstract] [Full Text] [PDF]




Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 2001