TY - JOUR
T1 - A recognition marker required for uptake of a lysosomal enzyme by cultured fibroblasts
AU - Hickman, Scot
AU - Shapiro, Larry J.
AU - Neufeld, Elizabeth F.
PY - 1974/3/15
Y1 - 1974/3/15
N2 - N-acetyl-β-hexosaminidase secreted by cultured skin fibroblasts from normal individuals, or from patients with mucopolysaccharidoses, is effectively captured by fibroblasts derived from patients with Sandhoff disease. On the other hand, N-acetyl-β-hexosaminidase from several other sources (including placenta, urine, and secretions of fibroblasts from patients with mucolipidosis II or III) is taken up to a much lesser extent. The uptake of the normal fibroblast hydrolase can be abolished by periodate oxidation under conditions that do not affect its catalytic activity, stability, or binding to Concanavalin A - Sepharose. These results suggest that uptake into fibroblasts requires a specific marker on the enzyme.
AB - N-acetyl-β-hexosaminidase secreted by cultured skin fibroblasts from normal individuals, or from patients with mucopolysaccharidoses, is effectively captured by fibroblasts derived from patients with Sandhoff disease. On the other hand, N-acetyl-β-hexosaminidase from several other sources (including placenta, urine, and secretions of fibroblasts from patients with mucolipidosis II or III) is taken up to a much lesser extent. The uptake of the normal fibroblast hydrolase can be abolished by periodate oxidation under conditions that do not affect its catalytic activity, stability, or binding to Concanavalin A - Sepharose. These results suggest that uptake into fibroblasts requires a specific marker on the enzyme.
UR - http://www.scopus.com/inward/record.url?scp=0015970730&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(74)80356-6
DO - 10.1016/S0006-291X(74)80356-6
M3 - Article
C2 - 4364008
AN - SCOPUS:0015970730
VL - 57
SP - 55
EP - 61
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -