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 (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 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 Iida, H.
Right arrow Articles by Shibata, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Iida, H.
Right arrow Articles by Shibata, Y.
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?

Immunocytochemical localization of 67 KD Ca2+ binding protein (p67) in ventricular, skeletal, and smooth muscle cells

H Iida, T Hatae and Y Shibata

Department of Anatomy, Faculty of Medicine, Kyushu University, Fukuoka, Japan.

By using immunocytochemical techniques, we examined the localization of a 67 kDa Ca2+ binding protein (p67) and calpactin I heavy chain (p36) in ventricular myocytes, skeletal myocytes, and intestinal smooth muscle cells. Immunofluorescence microscopy revealed that the p67 was expressed in all these muscle cells, whereas anti-p36 antibody stained cells in connective tissues but failed to stain these muscle cells. Immunogold electron microscopy was carried out to examine the subcellular localization of the p67 in muscle cells. The results showed that the p67 was exclusively confined to the plasma membrane of muscle cells and the presumptive transverse tubules of the striated myocytes. Immunoblot analysis with anti-p67 antibody showed that the p67 was indeed a constitutive protein of the sarcolemma isolated from rat hearts. These results indicate that the p67 is a sarcolemma-associated Ca2+ binding protein expressed in both striated myocytes and intestinal smooth muscle cells.

Volume 40, Issue 12, pp. 1899-1907, 12/01/1992
Copyright © 1992 by The Histochemical Society


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
J. Biol. Chem.Home page
E. B. Babiychuk, R.-J. T. S. Palstra, J. Schaller, U. Kampfer, and A. Draeger
Annexin VI Participates in the Formation of a Reversible, Membrane-Cytoskeleton Complex in Smooth Muscle Cells
J. Biol. Chem., December 3, 1999; 274(49): 35191 - 35195.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
P. Trouve, S. Legot, I. Belikova, F. Marotte, D. Benevolensky, F. Russo-Marie, J.-L. Samuel, and D. Charlemagne
Localization and quantitation of cardiac annexins II, V, and VI in hypertensive guinea pigs
Am J Physiol Heart Circ Physiol, April 1, 1999; 276(4): H1159 - H1166.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
V. Ellis and S. A. Whawell
Vascular Smooth Muscle Cells Potentiate Plasmin Generation by Both Urokinase and Tissue Plasminogen Activator-Dependent Mechanisms: Evidence for a Specific Tissue-Type Plasminogen Activator Receptor on These Cells
Blood, September 15, 1997; 90(6): 2312 - 2322.
[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 © 1992