A unique phospholipid organization in bovine erythrocyte membranes


Autoria(s): Florin-Christensen, J.; Suarez, C. E.; Florin-Christensen, M.; Wainszelbaum, M.; Brown, W. C.; McElwain, T. F.; Palmer, G. H.
Data(s)

03/07/2001

26/06/2001

Resumo

Ruminant erythrocytes are remarkable for their choline-phospholipid anomalies; namely, low or absent phosphatidylcholine (PC) along with high sphingomyelin levels. Here, we report another anomaly in bovine erythrocytes that affects aminophospholipids: phosphatidylethanolamine (PE) shows an extreme asymmetry, with only 2% of the total present in the outer leaflet. Furthermore, we found that phospholipase A2, an enzyme located on the external surface of the erythrocytes, shows higher activity against PC than against PE. In addition, we observed that acylation of PE is by far the most important biosynthetic event in this system. We propose that deacylation of PE and PC by phospholipase A2 to generate lysocompounds, followed by selective reacylation of lyso-PE in the inner leaflet, can account for the compositional and architectural peculiarities of bovine erythrocyte membranes.

Identificador

/pmc/articles/PMC35411/

/pubmed/11427712

http://dx.doi.org/10.1073/pnas.131580998

Idioma(s)

en

Publicador

The National Academy of Sciences

Direitos

Copyright © 2001, The National Academy of Sciences

Palavras-Chave #Biological Sciences
Tipo

Text