Erythrocyte spectrofluorometric abnormalities in myotonic dystrophy during "in vitro" aging.
The possibility in Myotonic dystrophy (MyD) that a decreased ATP utilization by the membrane may produce modifications in glycoprotein structure and/or in the supramolecular arrangement of some membrane proteins was investigated in human erythrocytes: a) by determining the membrane sialic acid content and the cellular ATP concentration in eight cases of MyD; b) by evaluating the stability of the membrane glycoprotein structure by in vitro ageing experiments; c) by testing the presence of high molecular weight aggregates of proteins on the membrane; d) by evaluating the physico-chemical properties of the membrane by 1-anilino 8-naftalensulfonate as a fluorescent probe. Our evidence suggests that ATP concentration and membrane sialic acid content are within normal values. Only in two cases did a decreased stability of membrane glycoproteins occur while the supramolecular assembly of membrane proteins could be considered as normal. The fluorescent probe behavior after in vitro aging was indicative of a decreased polarity of its micro-environment.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000293:Adolescent; D000328:Adult; D004905:Erythrocyte Aging; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D008875:Middle Aged; D009223:Myotonic Dystrophy / Q000097:blood*; D013050:Spectrometry, Fluorescence
D006023:Glycoproteins; D008565:Membrane Proteins; D000255:Adenosine Triphosphate