Glucosylceramide, a Neutral Glycosphingolipid Anticoagulant Cofactor, Enhances the Interaction of Human- and Bovine-activated Protein C with Negatively Charged Phospholipid Vesicles *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 278, Issue: 17, Page: 14614-14621
2003
- 20Citations
- 14Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations20
- Citation Indexes20
- 20
- CrossRef18
- Captures14
- Readers14
- 14
Article Description
The effect of glucosylceramide (GlcCer) on activated protein C (APC)-phospholipid interactions was examined using fluorescence resonance energy transfer. Human APC, labeled with either fluorescein (Fl-APC) or dansyl (DEGR-APC) donor, bound to phosphatidylcholine/phosphatidylserine (PC/PS, 9:1 w/w) vesicles containing octadecylrhodamine (OR) acceptor with a K d app = 16 μg/ml, whereas Fl-APC (or DEGR-APC) bound to PC/PS/GlcCer(OR) (8:1:1) vesicles with a K d app = 3 μg/ml. This 5-fold increase in apparent affinity was not species-specific since bovine DEGR-APC also showed a similar GlcCer-dependent enhancement of binding of APC to PC/PS vesicles. From the efficiency of fluorescence resonance energy transfer, distances of closest approach of ∼63 and ∼64 Å were estimated between the dansyl on DEGR-APC and rhodamine in PC/PS/GlcCer(OR) and PC/PS(OR), respectively, assuming κ 2 = 2/3. DEGR-APC bound to short chain C8-GlcCer with an apparent K d of 460 n m. The presence of C8-GlcCer selectively enhanced the binding of C16,6-NBD-phosphatidylserine but not C16,6–7-nitrobenz-2-oxa-1,3-diazole (NBD)-phosphatidylcholine to coumarin-labeled APC. These data suggest that APC binds to GlcCer, that PC/PS/GlcCer vesicles like PC/PS vesicles bind to the N-terminal γ-carboxyglutamic acid domain of APC, and that one mechanism by which GlcCer enhances the activity of APC is by increasing its affinity for membrane surfaces containing negatively charged phospholipids.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819302522; http://dx.doi.org/10.1074/jbc.m206746200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037677084&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12560338; http://www.jbc.org/lookup/doi/10.1074/jbc.M206746200; https://syndication.highwire.org/content/doi/10.1074/jbc.M206746200; https://linkinghub.elsevier.com/retrieve/pii/S0021925819302522; https://dx.doi.org/10.1074/jbc.m206746200
American Society for Biochemistry & Molecular Biology (ASBMB)
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