Genetics of type II glycogenosis: Assignment of the human gene for acid α-glucosidase to chromosome 17

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Abstract
Somatic cell hybrids between thymidine kinase (EC 2.71.75) deficient mouse cells and human diploid fibroblasts were studied for the expression of human acid .alpha.-glucosidase (EC 3.2.1.20). A deficiency in this enzyme is associated with the type II glycogenosis or Pompe disease. All 30 somatic cell hybrids selected in hypoxanthine/aminopterin/thymidine medium expressed human acid .alpha.-glucosidase and galactokinase (EC 2.7.1.6) and retained human chromosome 17; counterselection of the same hybrids in medium containing 5-bromodeoxyuridine resulted in the growth of hybrids that concordantly lost the expression of human acid .alpha.-glucosidase and galactokinase and human chromosome 17. Hybrids between thymidine kinase-deficient mouse cells and fibroblasts from a patient with Pompe disease that contained human chromosome 17 did not express human acid .alpha.-glucosidase. Since hybrids between mouse peritoneal macrophages and GM54VA simian virus 40-transformed human cells selectively retain human chromosome 17 and lose all other human chromosomes, 13 independent mouse macrophage .times. GM54VA hybrid clones were tested, (including 2 that retained human chromosome 17 and no other human chromosomes) for the expression of human acid .alpha.-glucosidase and galactokinase. All 13 hybrid clones expressed these human enzymes. The gene coding for human acid .alpha.-glucosidase evidently is located on human chromosome 17.