| Autor: |
Babiychuk EB; Department of Cell Biology, Institute of Anatomy, University of Bern, Bühlstrasse 26, 3012, Bern, Switzerland., Babiychuk VS, Danilova VM, Tregubov VS, Sagach VF, Draeger A |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 2002 Nov 04; Vol. 1600 (1-2), pp. 154-61. |
| DOI: |
10.1016/s1570-9639(02)00456-9 |
| Abstrakt: |
Annexins belong to a family of lipid-binding proteins that are implicated in membrane organization. Several members are capable of binding to actin and, in smooth muscle cells, annexin 6 is known to form a Ca(2+)-dependent, plasmalemmal complex with actin filaments. Annexins can also associate with F-actin containing stress fibres within cultured smooth muscle cells or fibroblasts in a Ca(2+)-independent manner. Depolymerization of stress-fibre systems with cytochalasin D leads to the translocation of actin-bound annexin 2 from the cytoplasm to the plasma membrane at high intracellular levels of Ca(2+). This type of Ca(2+)-dependent annexin mobility is observed only in cells of mesenchymal phenotype, which have a well-developed stress-fibre system; not in epithelial cells. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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