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Human C-apolipoproteins promote hydrolysis of dimyristoyl phosphatidylcholine by snake venom phospholipase A2
- Source :
- FEBS Letters. 140:135-138
- Publication Year :
- 1982
- Publisher :
- Wiley, 1982.
-
Abstract
- Introduction Lipoprotein lipase, the enzyme which metabolizes triglyceride-rich plasma lipoproteins, is activated by apolipoprotein CII [ 11. That this activation is impor- tant for the physiological action of the enzyme is demonstrated by the massive hypertriglyceridemia in patients deficient in this apolipoprotein [2]. Whereas the activation of lipoprotein lipase by CII appears to be a specific effect and probably involves direct pro- tein-protein interaction, there are also reports that other apolipoproteins activate or inhibit lipoprotein lipase [3-l l] and/or the related heparin heparin- releasable lipase
- Subjects :
- Time Factors
Apolipoprotein B
Biophysics
Biochemistry
Phospholipases A
chemistry.chemical_compound
Phospholipase A2
Structural Biology
Phosphatidylcholine
Genetics
medicine
Lipase
Apolipoproteins C
Molecular Biology
chemistry.chemical_classification
Lipoprotein lipase
Dose-Response Relationship, Drug
biology
Hydrolysis
Cell Biology
Heparin
Phospholipases A2
Apolipoproteins
Enzyme
chemistry
Phospholipases
Snake venom
Phosphatidylcholines
biology.protein
lipids (amino acids, peptides, and proteins)
Dimyristoylphosphatidylcholine
medicine.drug
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 140
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....75429548dadc5159f9a2b8efbafb5cdf
- Full Text :
- https://doi.org/10.1016/0014-5793(82)80538-3