Abstract
A solubilized sialidase is partially deficient in cultured fibroblasts derived from skin biopsies of four mucolipidosis IV patients. Fibroblasts from two obligate heterozygotes also have sialidase activity lower than normal controls. Membrane-bound sialidase activity is not affected in this disease. Based on previous and present findings, we propose that this solubilized activity is probably lysosomal origin. Sialidase activity in mucolipidosis IV cells is normal when neuraminlactose is used as substrate. Mixing cell homogenates from mucolipidosis IV patients and from controls results in the expected combined sialidase activity, indicating the absence of an internal inhibitor in the deficient cells. It is therefore suggested that the mutation in mucolipidosis IV specifically affects a lysosomal ganglioside sialidase, while the remaining non-lysosomal sialidases partially mask this deficiency.
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