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castanospermine/sarkoma
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Inhibition of glycosylation processing alters the growth parameters of cells transformed by the oncogene of simian sarcoma virus.
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Normal rat kidney (NRK) cells transformed by the v-sis oncogene of simian sarcoma virus (SSV) were treated with the glucosidase I inhibitor castanospermine. The inhibitor did not change cell morphology, but specific growth parameters such as serum- and anchorage-independence were lost.
Appropriate glycosylation of the fms gene product is a prerequisite for its transforming potency.
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Processing inhibitors of N-linked glycans were used to determine whether correct glycosylation of the oncogene product gp140v-fms, encoded by the McDonough strain of feline sarcoma virus (SM-FeSV), is required to maintain the oncogenic properties of v-fms. SM-FeSV-transformed cells treated with the
Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression.
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The effect of glycosylational-processing inhibitors on the synthesis, cell surface expression, endocytosis, and transforming function of the v-fms oncogene protein (gp140fms) was examined in McDonough feline sarcoma virus-transformed Fischer rat embryo (SM-FRE) cells. Swainsonine (SW), a mannosidase
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