Cytocheltnical Examination of the Compartments Involved in the Transcellular Transport of Horseradish Peroxidase in Rat Hepatocytes

Cell Structure and Function

Jun Yamaguchi¹  Akio Kaneko¹  Michio Mori¹  Masahito Oyamada¹  Katsuhiko Enomoto¹ 

[1] Deparment of Pathology, Sapporo Medical College

关键词: transcellular transport;    biliary protein;    vesicular transport;    double cytochemistry;    electron microscopy;   

DOI  :  10.1247/csf.15.263

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(44)Cited-By(3)Horseradish peroxidase (HRP, 10 mg/100 g body weight) was intravenously injected into rats in order to investigate the nature of the compartmens involved in the transcellular transport of the protein through hepatocytes into bile. Double cytochemistry for HRP and the marker enzymesfor cytoplasmic orgattelles was used. HRP was shown to be taken up by hepatocytes via vesicles at the sinusoidal surface, some of which were positive for 5'-nucleotiddse activity. HRP was then found in the smooth-surfaced vesicles and tubules which were negative in 5'-nucleotidase, glucose 6-phosphatase, thiamine pyrophosphatase and acid phosphatase activity, suggesting that the tubular structures are neither the endoplasmic reticulum, the Golgi apparatus nor lysosomes. Biochemical studies revealed that the lead procedures used for the double cytochemistry did not inhibit the peroxidatic activity of HRP, and conversely that HRP did not interfere with the marker enzyme activity. Such cytochemical observations seemed to be supported by the observation that administration of monensin (3.5 mg/100 g) and chloroquine (5 mg/100 g), which markedly aletered the structure of the Golgi apparatus and lysosomes, respectively, slightly altered the biliary excretion of HRP but not to a significant extent.

【 授权许可】

Unknown