Heat-labile enzymes in circulating erythrocytes of a progeria family.
Cultured skin fibroblasts from subjects with progeria contain an increased fraction of heat-labile enzymes and other altered proteins. To determine whether freshly obtained cells are similarly affected, erythrocytes from a progeric female and her clinically normal parents were analyzed for heat-lability of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Hemolysates of the child's whole erythrocyte populations and young erythrocytes isolated by equilibrium density centrifugation contained significantly higher heat-labile fractions of both enzymes compared to control hemolysates. Values in both parents were intermediate to those of their daughter and controls, consistent with autosomal recessive inheritance in this family. The primary source of these multiple protein defects is unknown but may reside in a mutant gene producing abnormal protein turnover or defective DNA repair. An increased fraction of thermolabile enzymes in circulating erythrocytes should be useful in identifying persons at risk for progeria and other disorders of premature aging.
D000328:Adult; D002675:Child, Preschool; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008297:Male; D010734:Phosphogluconate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D011371:Progeria / Q000201:enzymology / Q000235:genetics*
D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase