Modification of erythrocyte membrane proteins, enzymes and transport mechanisms in chronic alcoholics: An in vivo and in vitro study

Paramahamsa Maturu, Damodara Reddy Vaddi, Padmavathi Pannuru, Varadacharyulu Nallanchakravarthula

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Aim: The aim of the study was to elucidate the molecular mechanisms underlying the alcohol perturbation leading to deleterious effects on erythrocyte membrane transport in chronic alcoholics. Methods: Membrane bound enzyme activities such as Na+, K+-ATPase, Ca2+,Mg2+-ATPase and acetylcholine esterase and membrane transport analysis by in vitro and erythrocyte membraneprofile analysis in controls and chronic alcoholic red cells were analyzed.Results: It was observed that decreased Na+, K+-ATPase enzyme activity and increasedactivities of Ca2+,Mg2+-ATPase and acetylcholine esterase in chronic alcoholics compared to controls. The in vitro studies of erythrocytes suggested that there is an increased uptake of glucose through chronic alcoholic red cells. However, glucose utilization by chronic alcoholic red cellswas decreased. An increased sensitivity of ouabain for its binding site on Na+, K+- ATPase in chronic alcoholic erythrocyte membrane was evident from this study. Though there appears to be anincreased Na+ influx in chronic alcoholic cells, the status of Na+ transport is not altered much. However, ouabain caused slightdisturbances in the transport of sodium, similar disturbances in the potassium transport resulting in much accumulation of potassium in red cells. Conclusions: It was concluded that chronic alcohol consumption modified certain membrane bound proteins, enzymes and transport mechanisms in chronic alcoholics.

Original languageEnglish (US)
Article numberagt071
Pages (from-to)679-686
Number of pages8
JournalAlcohol and Alcoholism
Volume48
Issue number6
DOIs
StatePublished - Nov 2013

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Toxicology
  • Psychiatry and Mental health

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