Bilirubin Binding Activity of Cytokeratin 18 Isolated from the Porcine Liver

Cell Structure and Function

Toru Takahashi²  Kentaro Ohishi³  Mamoru Isemura³  Hiroshi Munakata⁵  Kohtaro Tada⁶  Shoji Odani⁷  Takashi Mita³  Cheng-Chin Hsu¹  Satoko Isemura⁴  Yutaka Aoyagi² 

[1] Department of Nutrition, Chung Shan Medical and Dental College;Third Department of Internal Medicine, Niigata University School of Medicine;Laboratory of Biochemistry, School of Food and Nutritional Sciences, University of Shizuoka;Nippon Dental University Junior College at Niigata;Department of Biochemistry, Kinki University School of Medicine;Department of Bacteriology, Tohoku University School of Medicine;Department of Biology, Niigata University College of Science

关键词: cytokeratin 18;    bilirubin;    liver;    hepatocyte;   

DOI  :  10.1247/csf.23.325

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(24)Cited-By(1)A porcine liver 40 kDa protein designated SBP40 isolated by affinity chromatography with agarose-linked spermine was identified as a porcine cytokeratin 18 on the basis of partial amino acid sequences of peptides derived by lysylendopeptidase digestion and by its reactivity with two commercially available preparations of monoclonal antibody. Immunohistochemistry revealed that SBP40 is localized at the hepatocyte membranes, preferentially in the bile canalicular area in accordance with the previously reported localization of cytokertain 18 in the murine liver. Affinity chromatography with agarose-linked bilirubin, a solubilization experiment of bilirubin from bilirubin-Sephadex G-10 complex, and gel-filtration of a mixture with bilirubin demonstrated that SBP40 or porcine cytokeratin 18 has binding affinity for bilirubin. These results suggest that cytokeratin 18 may play a role as a membrane reservoir in the event of transport and secretion of bile pigments in the liver.

【 授权许可】

Unknown