Transport of acid phosphatase to lysosomes does not involve passage through the cell surface

Yoshitaka Tanaka, Shinji Yano, Koji Furuno, Toyoko Ishikawa, Masaru Himeno, Keitaro Kato

研究成果: Contribution to journalArticle査読

11 被引用数 (Scopus)


In foregoing studies, we reported that LGP107, a major lysosomal membrane glycoprotein in the rat liver, distributes in and circulates continuously throughout the endocytic membrane system (endosomes, lysosomes and plasma membrane), in hepatocytes (1,2). In the present study we examined whether acid phosphatase (APase), an enzyme that is transported to lysosomes as a transmembrane protein, passes through the cell surface during intracellular transport, because transport of newly synthesized APase to lysosomes involves the passage of endosomes containing a ligand which is internalized via receptors on the cell surface and is finally dispatched to lysosomes for degradation (3). When localization of APase in rat hepatocytes was investigated by immunoelectron microscopy, APase was found to be localized in lysosomes and endosomes, but not in coated pits on the cell surface, which are positive for LGP107, and from which antibodies for LGP107 are internalized. Further, unlike LGP107, newly synthesized APase was not detected in plasma membranes isolated from livers of rats given [35S]methionine, and when cultured hepatocytes were exposed to 125I-labeled anti APase IgG at 37°C, there was no transfer of the antibody to lysosomes even after 24 h incubation. Therefore, these results indicate that intracellular movement of APase does not involve cell surface passage in rat hepatocytes, and clearly differs from the recent report that human APase is transported to lysosomes via the cell surface in BHK cells transfected with its cDNA (4).

ジャーナルBiochemical and Biophysical Research Communications
出版ステータス出版済み - 8 16 1990

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学


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