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Jan F. C. Glatz

Researcher at Maastricht University

Publications -  309
Citations -  20133

Jan F. C. Glatz is an academic researcher from Maastricht University. The author has contributed to research in topics: Fatty acid & CD36. The author has an hindex of 72, co-authored 304 publications receiving 18662 citations. Previous affiliations of Jan F. C. Glatz include Maastricht University Medical Centre & Leiden University Medical Center.

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Differential Translocation of the Fatty Acid Transporter, FAT/CD36, and the Glucose Transporter, GLUT4, Coordinates Changes in Cardiac Substrate Metabolism During Ischemia and Reperfusion

TL;DR: During ischemia, FAT/CD36 moved away from the sarcolemma as GLUT4 moved toward the sarCOlemma, associated with a shift from fatty acid oxidation to glycolysis, while intramyocardial lipid accumulation was prevented.
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Ketone bodies disturb fatty acid handling in isolated cardiomyocytes derived from control and diabetic rats.

TL;DR: The concomitantly increased FA uptake in diabetic cells, mainly due to the elevated extracellular FA levels, may be responsible for the accumulation of FA and triacylglycerol, as observed in the diabetic heart in situ.
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Post-translational modifications of CD36 (SR-B2): Implications for regulation of myocellular fatty acid uptake.

TL;DR: The membrane-associated protein CD36, now officially designated as SR-B2, is present in various tissues and fulfills multiple cellular functions and is subject to a multitude of post-translational modifications of which their functional implications are beginning to be understood.
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The endocannabinoid system: Overview of an emerging multi-faceted therapeutic target.

TL;DR: A conceptual framework linking endocannabinoid signaling to the control of the cellular and molecular hallmarks is provided, and the key components of endoc cannabinoidoid signaling that may serve as targets for novel therapeutics are categorized.
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Signaling role of CD36 in platelet activation and thrombus formation on immobilized thrombospondin or oxidized low-density lipoprotein.

TL;DR: Immobilized TSP1 and oxLDL activate platelets partly via CD36 through a Syk kinase‐dependent Ca2+ signaling mechanism, which enhances collagen‐dependent thrombus formation under flow, providing novel insight into the role of CD36 in hemostasis.