Creatine kinase muscle type specifically interacts with saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids.
In: Biochemical & Biophysical Research Communications, Jg. 513 (2019-06-11), Heft 4, S. 1035-1040
academicJournal
Zugriff:
Diacylglycerol kinase (DGK) δ, which is a key enzyme in the pathogenesis of type 2 diabetes (T2D), preferentially generates saturated fatty acid (SFA)- and/or monounsaturated fatty acid (MUFA)-containing phosphatidic acids (PAs) such as 16:0/16:0-PA and 16:0/18:1-PA, but not polyunsaturated fatty acid (PUFA)-containing PAs, in glucose-stimulated myoblast cells. Here, we searched for the target proteins of 16:0/16:0-PA in the mouse skeletal muscle and identified an energy metabolizing enzyme, creatine kinase muscle type (CKM), which is correlated with T2D. CKM bound to 16:0/16:0-PA with the highest affinity (dissociation constant: 2.0 μM) among all the PA-binding proteins reported thus far. Intriguingly, CKM preferentially interacted with SFA- and/or MUFA-containing PAs, but not with PUFA-containing PAs. Notably, CKM exclusively interacted with PA, whereas the protein did not bind to other lipids such as diacylglycerol, phosphatidylserine, phosphatidylglycerol, phosphatidylinositol, phosphatidylinositol (3,4,5)-trisphosphate and cardiolipin. Taken together, these results demonstrate that CKM is a very unique PA-binding protein that possesses exceedingly high affinity for PA, exceptional preference for SFA/MUFA-PA and extremely high specificity to PA and suggest that SFA/MUFA-PAs produced by DGKδ are novel regulators of CKM function. • T2D-related DGKδ preferentially generates SFA/MUFA-PAs, including 16:0/16:0-PA. • 16:0/16:0-PA bound to T2D-related creatine kinase muscle type (CKM). • CKM bound to 16:0/16:0-PA with the highest affinity among the PA-binding proteins. • CKM preferentially interacted with SFA/MUFA-PAs but not with PUFA-PAs. • CKM exclusively interacted with PAs but not with other lipids. [ABSTRACT FROM AUTHOR]
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Creatine kinase muscle type specifically interacts with saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids.
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Autor/in / Beteiligte Person: | Hoshino, Fumi ; Murakami, Chiaki ; Sakai, Hiromichi ; Satoh, Mamoru ; Sakane, Fumio |
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Zeitschrift: | Biochemical & Biophysical Research Communications, Jg. 513 (2019-06-11), Heft 4, S. 1035-1040 |
Veröffentlichung: | 2019 |
Medientyp: | academicJournal |
ISSN: | 0006-291X (print) |
DOI: | 10.1016/j.bbrc.2019.04.097 |
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