Membrane‐bound N‐acetyl‐β‐glucosamimdase

FEBS Letters

Kato, Goro¹  Suzuki, Yoshiyuki² 

[1] Division of Chemical Pathology, National Center for Nervous, Mental and Muscular Disorders. Ogawa-Higashimachi, Kodaira, Tokyo 187, Japan;Department of Pediatrics, Faculty of Medicine, The Universty of Tokyo, Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Phosphomannosyl receptor;    Lysosomal enzyme;    Intracellular transport;    Alternate pathway;    I-cell disease;   

DOI  :  10.1016/0014-5793(85)80156-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Several lysosomal enzymes solubilized at pH 4 from saponin-treated membranes showed markedly variable affinities to the bovine liver phosphomannosyl receptor in both bovine and human livers. The enzymes from I-cell disease liver did not bind the receptor in spite of normal intracellular activities. N-Acetyl-β-glucos-aminidase was effectively released from the membrane preparation of a control liver by mannose 6-phosphate, and other sugars showed little effect in this experiment. However, in the I-cell disease liver, dissociation occurred not by mannose 6-phosphate but by other sugars, such as fucose, mannose and N-acetyl-D-glucosamine. These results indicate the presence of an alternate transport system other than the pathway mediated by the mannose 6-phosphate receptor, and the role of other sugar-binding proteins is discussed in intracellular processing and transport of newly synthesized enzymes.

【 授权许可】

Unknown