- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Faculty Research and Publications /
- Lipoprotein Lipase and Its Delivery of Fatty Acids...
Open Collections
UBC Faculty Research and Publications
Lipoprotein Lipase and Its Delivery of Fatty Acids to the Heart Shang, Rui; Rodrigues, Brian
Abstract
Ninety percent of plasma fatty acids (FAs) are contained within lipoprotein-triglyceride, and lipoprotein lipase (LPL) is robustly expressed in the heart. Hence, LPL-mediated lipolysis of lipoproteins is suggested to be a key source of FAs for cardiac use. Lipoprotein clearance by LPL occurs at the apical surface of the endothelial cell lining of the coronary lumen. In the heart, the majority of LPL is produced in cardiomyocytes and subsequently is translocated to the apical luminal surface. Here, vascular LPL hydrolyzes lipoprotein-triglyceride to provide the heart with FAs for ATP generation. This article presents an overview of cardiac LPL, explains how the enzyme works, describes key molecules that regulate its activity and outlines how changes in LPL are brought about by physiological and pathological states such as fasting and diabetes, respectively.
Item Metadata
Title |
Lipoprotein Lipase and Its Delivery of Fatty Acids to the Heart
|
Creator | |
Publisher |
Multidisciplinary Digital Publishing Institute
|
Date Issued |
2021-07-12
|
Description |
Ninety percent of plasma fatty acids (FAs) are contained within lipoprotein-triglyceride, and lipoprotein lipase (LPL) is robustly expressed in the heart. Hence, LPL-mediated lipolysis of lipoproteins is suggested to be a key source of FAs for cardiac use. Lipoprotein clearance by LPL occurs at the apical surface of the endothelial cell lining of the coronary lumen. In the heart, the majority of LPL is produced in cardiomyocytes and subsequently is translocated to the apical luminal surface. Here, vascular LPL hydrolyzes lipoprotein-triglyceride to provide the heart with FAs for ATP generation. This article presents an overview of cardiac LPL, explains how the enzyme works, describes key molecules that regulate its activity and outlines how changes in LPL are brought about by physiological and pathological states such as fasting and diabetes, respectively.
|
Subject | |
Genre | |
Type | |
Language |
eng
|
Date Available |
2021-07-26
|
Provider |
Vancouver : University of British Columbia Library
|
Rights |
CC BY 4.0
|
DOI |
10.14288/1.0400908
|
URI | |
Affiliation | |
Citation |
Biomolecules 11 (7): 1016 (2021)
|
Publisher DOI |
10.3390/biom11071016
|
Peer Review Status |
Reviewed
|
Scholarly Level |
Faculty
|
Rights URI | |
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
Rights
CC BY 4.0