Modulation of the organization of erythrocyte membrane phospholipids by cytoplasmic ATP. The susceptibility of isoionic human erythrocyte ghosts to attack by detergents and phospholipase C

Research output: Contribution to journalArticlepeer-review

Standard

Modulation of the organization of erythrocyte membrane phospholipids by cytoplasmic ATP. The susceptibility of isoionic human erythrocyte ghosts to attack by detergents and phospholipase C. / Shukla, S. D.; Billah, M. M.; Coleman, R.; Finean, J. B.; Michell, R. H.

In: BBA - Biomembranes, Vol. 509, No. 1, 04.05.1978, p. 48-57.

Research output: Contribution to journalArticlepeer-review

Harvard

APA

Vancouver

Author

Bibtex

@article{d06394215b934bbd9a0d57c6002fc174,
title = "Modulation of the organization of erythrocyte membrane phospholipids by cytoplasmic ATP. The susceptibility of isoionic human erythrocyte ghosts to attack by detergents and phospholipase C",
abstract = "Human erythrocyte ghosts were prepared in media of physiological ionic composition, and these {"}isoionic{"} ghosts were then lysed and resealed in media of varying Ca2+, Mg2+ and ATP concentrations. The susceptibilities of these ghosts to limited attack by various detergents and by phospholipases C were then compared with the susceptibilities of intact cells to similar attack: attack was assessed by measurements of lysis and of phospholipid hydrolysis. Ghosts were more readily attacked than cells by anionic detergents (cholate, glycocholate, dodecyl sulphate) and by phospholipases C, but Triton X-100 and cetyltrimethylammonium attacked cells and ghosts to the same extent. Mg · ATP2- partially protected ghosts from attack by the anionic detergents and by the phospholipases C of Bacillus cereus and of Clostridium perfringens. Protection by Mg · ATP2- occurred only if Mg · ATP2- had access to the cytoplasmic surface of the membrane. Adenylyl(β-γ-methylene)diphosphonate, a non-hydrolysable ATP analogue, protected as effectively as did Mg · ATP2-. Internal Mg · ATP2- caused a marked reduction in the hydrolysis by phospholipases of phosphatidylethanolamine and sphingomyelin, but had no appreciable effect upon the simultaneous hydrolysis of phosphatidylcholine. It therefore seems that interaction of ATP with sites on the cytoplasmic surface of the erythrocyte membrane can, without ATP hydrolysis, cause changes in the organization of the outer surface of the membrane that specifically render phosphatidylethanolamine and sphingomyelin less accessible to attack by extracellular phospholipases.",
author = "Shukla, {S. D.} and Billah, {M. M.} and R. Coleman and Finean, {J. B.} and Michell, {R. H.}",
year = "1978",
month = may,
day = "4",
doi = "10.1016/0005-2736(78)90006-8",
language = "English",
volume = "509",
pages = "48--57",
journal = "Biochimica et Biophysica Acta (BBA) - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Modulation of the organization of erythrocyte membrane phospholipids by cytoplasmic ATP. The susceptibility of isoionic human erythrocyte ghosts to attack by detergents and phospholipase C

AU - Shukla, S. D.

AU - Billah, M. M.

AU - Coleman, R.

AU - Finean, J. B.

AU - Michell, R. H.

PY - 1978/5/4

Y1 - 1978/5/4

N2 - Human erythrocyte ghosts were prepared in media of physiological ionic composition, and these "isoionic" ghosts were then lysed and resealed in media of varying Ca2+, Mg2+ and ATP concentrations. The susceptibilities of these ghosts to limited attack by various detergents and by phospholipases C were then compared with the susceptibilities of intact cells to similar attack: attack was assessed by measurements of lysis and of phospholipid hydrolysis. Ghosts were more readily attacked than cells by anionic detergents (cholate, glycocholate, dodecyl sulphate) and by phospholipases C, but Triton X-100 and cetyltrimethylammonium attacked cells and ghosts to the same extent. Mg · ATP2- partially protected ghosts from attack by the anionic detergents and by the phospholipases C of Bacillus cereus and of Clostridium perfringens. Protection by Mg · ATP2- occurred only if Mg · ATP2- had access to the cytoplasmic surface of the membrane. Adenylyl(β-γ-methylene)diphosphonate, a non-hydrolysable ATP analogue, protected as effectively as did Mg · ATP2-. Internal Mg · ATP2- caused a marked reduction in the hydrolysis by phospholipases of phosphatidylethanolamine and sphingomyelin, but had no appreciable effect upon the simultaneous hydrolysis of phosphatidylcholine. It therefore seems that interaction of ATP with sites on the cytoplasmic surface of the erythrocyte membrane can, without ATP hydrolysis, cause changes in the organization of the outer surface of the membrane that specifically render phosphatidylethanolamine and sphingomyelin less accessible to attack by extracellular phospholipases.

AB - Human erythrocyte ghosts were prepared in media of physiological ionic composition, and these "isoionic" ghosts were then lysed and resealed in media of varying Ca2+, Mg2+ and ATP concentrations. The susceptibilities of these ghosts to limited attack by various detergents and by phospholipases C were then compared with the susceptibilities of intact cells to similar attack: attack was assessed by measurements of lysis and of phospholipid hydrolysis. Ghosts were more readily attacked than cells by anionic detergents (cholate, glycocholate, dodecyl sulphate) and by phospholipases C, but Triton X-100 and cetyltrimethylammonium attacked cells and ghosts to the same extent. Mg · ATP2- partially protected ghosts from attack by the anionic detergents and by the phospholipases C of Bacillus cereus and of Clostridium perfringens. Protection by Mg · ATP2- occurred only if Mg · ATP2- had access to the cytoplasmic surface of the membrane. Adenylyl(β-γ-methylene)diphosphonate, a non-hydrolysable ATP analogue, protected as effectively as did Mg · ATP2-. Internal Mg · ATP2- caused a marked reduction in the hydrolysis by phospholipases of phosphatidylethanolamine and sphingomyelin, but had no appreciable effect upon the simultaneous hydrolysis of phosphatidylcholine. It therefore seems that interaction of ATP with sites on the cytoplasmic surface of the erythrocyte membrane can, without ATP hydrolysis, cause changes in the organization of the outer surface of the membrane that specifically render phosphatidylethanolamine and sphingomyelin less accessible to attack by extracellular phospholipases.

UR - http://www.scopus.com/inward/record.url?scp=0018187564&partnerID=8YFLogxK

U2 - 10.1016/0005-2736(78)90006-8

DO - 10.1016/0005-2736(78)90006-8

M3 - Article

C2 - 647008

AN - SCOPUS:0018187564

VL - 509

SP - 48

EP - 57

JO - Biochimica et Biophysica Acta (BBA) - Biomembranes

JF - Biochimica et Biophysica Acta (BBA) - Biomembranes

SN - 0005-2736

IS - 1

ER -