Characterization of mammalian heart annexins with special reference to CaBP33 (annexin V).
FEBS Lett
; 277(1-2): 53-8, 1990 Dec 17.
Article
in En
| MEDLINE
| ID: mdl-2148529
ABSTRACT
Porcine heart was observed to express annexins V (CaBP33) and VI in large amounts, and annexins III and IV in much smaller amounts. Annexin V (CaBP33) in porcine heart was examined in detail by immunochemistry. Homogenization and further processing of heart in the presence of EGTA resulted in the recovery of annexin V (CaBP33) in the cytosolic fraction and in an EGTA-resistant, Triton X-100-soluble fraction from cardiac membranes. Including Ca2+ in the homogenization medium resulted in a significant decrease in the annexin V (CaBP33) content of the cytosolic fraction with concomitant increase in the content of this protein in myofibrils, mitochrondria, the sarcoplasmic reticulum and the sarcolemma. The amount of annexin V (CaBP33) in each of these subfractions depended on the free Ca2+ concentration in the homogenizing medium. At the lowest free Ca2+ concentration tested, 0.8 microM, only the sarcolemma appeared to contain bound annexin V (CaBP33). Membrane-bound annexins V (CaBP33) and VI partitioned in two fractions, one EGTA-resistant and Triton X-100-extractable, and one Triton X-100-resistant and EGTA-extractable. Altogether, these data suggest that annexins V and VI are involved in the regulation of membrane-related processes.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Pregnancy Proteins
/
Calcium-Binding Proteins
/
Myocardium
Limits:
Animals
Language:
En
Journal:
FEBS Lett
Year:
1990
Document type:
Article
Affiliation country:
Italia