Measurement of outward translocation of phospholipids across human erythrocyte membrane.
AUTOR(ES)
Bitbol, M
RESUMO
Spin-labeled phospholipids have been used to study the outside----inside and inside----outside transport of phospholipids across the human erythrocyte membrane at 37 degrees C. As already shown, inward transport is much faster for aminophospholipids than for phosphatidylcholine. In addition, we show here that outward transport of the phosphatidylserine and phosphatidylethanolamine analogues is three to four times faster than that of phosphatidylcholine. Magnesium depletion of the erythrocytes considerably decreases the outward rate of both aminophospholipids to values close to that of phosphatidylcholine. These results suggest that the outward aminophospholipid translocation is, at least partly, protein mediated. The protein involved could be identical to the inward Mg-ATP-dependent aminophospholipid carrier.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=282062Documentos Relacionados
- Asymmetric lateral mobility of phospholipids in the human erythrocyte membrane.
- Translocation of N-terminal tails across the plasma membrane.
- Regulation of the interaction of purified human erythrocyte AMP deaminase and the human erythrocyte membrane.
- An ATP-binding membrane protein is required for protein translocation across the endoplasmic reticulum membrane.
- Electrospray ionization mass spectroscopic analysis of human erythrocyte plasma membrane phospholipids.