Lymphoblastoid cell lines, transformed by Epstein-Barr virus, in the enzymatic study of hereditary lysosomal storage...

Assay conditions were studied for eight lysosomal enzymes in lymphoblastoid cell lines transformed by Epstein-Barr virus. The transformed lymphoblastoid cells retained all eight enzyme activities, though the levels sometimes differed from those in the peripheral lymphocytes or granulocytes. The levels of these eight lysosomal enzymes were measured in lymphoblastoid cells from 11 patients with hereditary lysosomal storage diseases--GMI-gangliosidosis, a variant of beta-galactosidase deficiency (sialidase deficiency with a partial beta-galactosidase deficiency), Tay-Sachs disease, Gaucher disease, Hurler syndrome, Scheie syndrome and I-cell disease--and from 20 of their obligate heterozygotes. No activity of enzymes that were deficient in the respective disease, except I-cell disease, was detected in the lymphoblastoid cells from the patient. In I-cell disease, the cells showed lower levels of some enzyme activities. beta-D-Galactosidase activity from heterozygotes of the patient with GMI-gangliosidosis and alpha-L-iduronidase activity from heterozygotes of the patient with Hurler syndrome were in carrier range. On sephadex G-150 gel filtration, beta-D-galactosidase in control material gave two peaks (I and II). In GMI-gangliosidosis, peak II was absent and peak I was markedly diminished. Peak II in the heterozygotes was smaller than that of control. On DEAE cellulose column chromatography of hexosaminidase, two major isoenzymes (hexosaminidase A and B) were detected in control. However, hexosaminidase A was not detected in Tay-Sachs disease, and the ratios of hexosaminidase (Hex) A/Hex B in the parents were lower than those in control.