Literature DB >> 11427712

A unique phospholipid organization in bovine erythrocyte membranes.

J Florin-Christensen1, C E Suarez, M Florin-Christensen, M Wainszelbaum, W C Brown, T F McElwain, G H Palmer.   

Abstract

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 A(2), 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 A(2) 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.

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Year:  2001        PMID: 11427712      PMCID: PMC35411          DOI: 10.1073/pnas.131580998

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  31 in total

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4.  Lysosomal phospholipase A1 in Trypanosoma cruzi: an enzyme with a possible role in the pathogenesis of Chagas' disease.

Authors:  M Wainszelbaum; E Isola; S Wilkowsky; J J Cannata; J Florin-Christensen; M Florin-Christensen
Journal:  Biochem J       Date:  2001-05-01       Impact factor: 3.857

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Authors:  J Florin-Christensen; C E Suarez; M Florin-Christensen; S A Hines; T F McElwain; G H Palmer
Journal:  Mol Biochem Parasitol       Date:  2000-02-25       Impact factor: 1.759

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