Open AccessUltracytochemistry of calmodulin binding sites in myocardial cells by staining of frozen thin sections with colloidal gold-labeled calmodulin.
Author(s) -
Kazushi Fujimoto,
Nobukazu Araki,
K S Ogawa,
Shinichi Kondo,
Takashi Kitaoka,
Kazuo Ogawa
Publication year - 1989
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/37.2.2911007
Subject(s) - calmodulin , egta , cytoplasm , staining , colloidal gold , chemistry , cytochemistry , negative stain , frozen section procedure , binding site , biophysics , endoplasmic reticulum , biochemistry , biology , calcium , electron microscope , pathology , nanotechnology , enzyme , materials science , nanoparticle , medicine , physics , organic chemistry , optics , genetics
Calmodulin (CaM) has been implicated as a multifunctional regulator of Ca2+ in the cytoplasm of cells. We have recently introduced biologically active colloidal gold-labeled CaM as a marker for identifying potential CaM binding sites (unoccupied by endogenous CaM at the time of fixation) by electron microscopy and have stained frozen thin sections of rat cardiac muscle with this conjugate. In the presence of Ca2+, gold particles indicating CaM binding sites were found localized on the sarcoplasmic reticulum, mitochondria, and gap junctions. Control tissue sections treated with EGTA or exposed to excess amounts of unlabeled native CaM before staining showed no binding. We believe that cytochemistry of potential CaM binding sites revealed by staining with labeled exogenous CaM is useful in correlating known biochemical reactions of CaM with particular cell activities.
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