Skip to main content
eScholarship
Open Access Publications from the University of California

UC San Diego

UC San Diego Electronic Theses and Dissertations bannerUC San Diego

Molecular Characterization of Heparin Binding Proteins in Triglyceride-rich Lipoprotein Catabolism

  • Author(s): Gonzales, Jon Christopher
  • et al.
Abstract

Heparan sulfate proteoglycans mediate multiple aspects of triglyceride-rich lipoprotein metabolism through non- covalent interactions with several lipases and apolipoproteins. In the circulation, lipoprotein lipase bound to the luminal side of the microvascular endothelium catalyzes the lipolysis of triglyceride-rich lipoproteins, resulting in lipoprotein remnants. In the liver, remnant lipoproteins are cleared from the circulation by three major endocytic clearance receptors, including the heparan sulfate proteoglycan syndecan-1. This dissertation describes the identification of the lipoprotein ligands responsible for heparan sulfate mediated clearance and studies suggesting a role for endothelial heparan sulfate proteoglycans in lipolysis. Chapter 1 provides background information on the structure and function of heparan sulfate, its putative role in lipolysis, and its participation in the clearance of triglyceride-rich lipoprotein remnants. The protein components of triglyceride-rich lipoproteins that bind to heparan sulfate are described. Chapter 2 provides evidence that led to the identification of the physiologic proteins responsible for lipoprotein binding to hepatic heparan sulfate proteoglycans. Chapter 3 describes studies of several mutant cell lines and mice that suggest a role for endothelial heparan sulfate proteoglycans in lipolysis. Chapter 4 presents on-going and future studies and the relevance of these findings to human disease

Main Content
Current View