Journal article
Structural modifications of rat serum high density lipoprotein by pancreatic phospholipase A2
Lipids, v 23(3)
Mar 1988
PMID: 3374275
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
An important and unusual aspect of the high density lipoprotein (HDL) in the rat is its tendency to undergo marked alterations in structure in response to physiological perturbations. In this study, the role of the surface lipids for maintenance of HDL integrity were investigated. Hydrolysis by pancreatic phospholipase A2 of the phospholipids of rat HDL in the presence of the d>1.21 g/ml fraction of rat serum results in an increase in the particle diameter and an uptake of apo‐E and apo A‐IV from the lipoprotein‐free fraction; augmentation of the albumin concentration in the incubation mixture intensified the observed changes, probably due to enhancement of the compositional changes brought about by phospholipase treatment. Phospholipase A2 treatment of the d<1.21 g/ml fraction of rat serum produces only minor changes in the properties of the isolated HDL. These data suggest that changes in apoprotein content reflect an uptake of A‐IV and E by the rat HDL, rather than a net loss of apo A‐I. Likewise, titration of the action of pancreatic phospholipase A2 on HDL apoprotein composition showed that initially a modest increase in apo A‐IV content occurred, but with more extensive phospholipolysis there was a considerably greater increase in the apo‐E content of the particle. The data suggest that hydrolysis of phospholipids such as occurs physiologically through the action of lecithin: cholesterol acyl transferase and hepatic lipase may alter the HDL structure independently from changes effected in the neutral lipid core.
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Details
- Title
- Structural modifications of rat serum high density lipoprotein by pancreatic phospholipase A2
- Creators
- John B. Swaney - Hahnemann University HospitalMargaret W. Orishimo - Hahnemann University Hospital
- Publication Details
- Lipids, v 23(3)
- Publisher
- Springer‐Verlag
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Web of Science ID
- WOS:A1988M655800009
- Scopus ID
- 2-s2.0-0023928618
- Other Identifier
- 991019350597904721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Nutrition & Dietetics