Ultracytochemistry of calmodulin binding sites in myocardial cells by staining of frozen thin sections with colloidal gold-labeled calmodulin.
J Histochem Cytochem
; 37(2): 249-56, 1989 Feb.
Article
en En
| MEDLINE
| ID: mdl-2911007
ABSTRACT
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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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Calmodulina
/
Oro
/
Miocardio
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
J Histochem Cytochem
Asunto de la revista:
HISTOCITOQUIMICA
Año:
1989
Tipo del documento:
Article
País de afiliación:
Japón