title: Modification of erythrocyte membrane proteins, enzymes and transport mechanisms in chronic alcoholics: an in vivo and in vitro study.
abstract: OBJECTIVE
  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, Ca(2+),Mg(2+)-ATPase and acetylcholine esterase and membrane transport analysis by in vitro and erythrocyte membrane profile analysis in controls and chronic alcoholic red cells were analyzed.
  
  
  RESULTS
  It was observed that decreased Na(+), K(+)-ATPase enzyme activity and increased activities of Ca(2+),Mg(2+)-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 cells was 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 an increased Na(+) influx in chronic alcoholic cells, the status of Na(+) transport is not altered much. However, ouabain caused slight disturbances 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.
authors: Corresponding author: Department of Biochemistry, Sri Krishnadevaraya University, Anantapur, AP 515055, India. matur_param@yahoo.com.
authors: Paramahamsa
authors: P
authors: Maturu
authors: Damodara Reddy
authors: DR
authors: Vaddi
authors: Padmavathi
authors: P
authors: Pannuru
authors: Varadacharyulu
authors: V
authors: Nallanchakravarthula
mesh_terms: D000110:Acetylcholinesterase / Q000097:blood; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000328:Adult; D057229:Alcoholics; D000437:Alcoholism / Q000097:blood* / Q000201:enzymology; D001786:Blood Glucose / Q000032:analysis / Q000378:metabolism; D001798:Blood Proteins / Q000032:analysis / Q000378:metabolism*; D002352:Carrier Proteins / Q000032:analysis / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000737:chemistry* / Q000187:drug effects* / Q000201:enzymology; D006801:Humans; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D008875:Middle Aged; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000097:blood; D016622:Silver Staining; D012964:Sodium / Q000097:blood
chemical_list: D001786:Blood Glucose; D001798:Blood Proteins; D002352:Carrier Proteins; D004791:Enzyme Inhibitors; D008565:Membrane Proteins; D010042:Ouabain; D012964:Sodium; D000110:Acetylcholinesterase; D000251:Adenosine Triphosphatases; D011188:Potassium