Studies on rat c-reactive protein : binding to isolated rat hepatocytes and clearance from circulation

Yang, Cheng Yong (1991) Studies on rat c-reactive protein : binding to isolated rat hepatocytes and clearance from circulation. Masters thesis, Memorial University of Newfoundland.

[img] [English] PDF (Migrated (PDF/A Conversion) from original format: (application/pdf)) - Accepted Version
Available under License - The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission.

Download (14Mb)
  • [img] [English] PDF - Accepted Version
    Available under License - The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission.
    (Original Version)

Abstract

The clearance mechanism of C-reactive proteins (CRP) was examined in this study. In vitro binding assays using isolated rat hepatocytes were followed by clearance studies in vivo and using perfused rat liver. -- It was shown that rat asialo CRP was rapidly cleared from the circulation (half-life about 4 min), whereas rat and rabbit CRP remained in the circulation for much longer periods of time (half-life 7.8 h for rat CRP). The clearance of rat asialo CRP was shown to be mediated through the hepatic asialoglycoprotein receptor, and this clearance was not affected by the phosphorylcholine binding domain of rat asialo CRP. Results of the clearance studies also suggested that, in addition to liver, lungs might also be involved in the clearance of CRP. -- It was observed that large amounts of rat asialo CRP, rat CRP and rabbit CRP bound to isolated rat hepatocytes, and the binding was shown to be mediated predominantly through the phosphorylcholine binding domain of these proteins. In addition, rat asialo CRP was shown to bind to the hepatic asialoglycoprotein receptor on the hepatocytes, despite the avid phosphorylcholine binding domain-mediated binding of this protein. It was demonstrated that the binding of large amounts of rat asialo CRP, rat CRP and rabbit CRP to the hepatocytes through the phosphorylcholine binding domain resulted from a disruption of the hepatocyte surface.

Item Type: Thesis (Masters)
URI: http://research.library.mun.ca/id/eprint/4071
Item ID: 4071
Additional Information: Bibliography: leaves 109-120.
Department(s): Science, Faculty of > Biochemistry
Date: 1991
Date Type: Submission
Library of Congress Subject Heading: C-reactive protein

Actions (login required)

View Item View Item

Downloads

Downloads per month over the past year

View more statistics