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John M. Tarbell

Researcher at City College of New York

Publications -  262
Citations -  14058

John M. Tarbell is an academic researcher from City College of New York. The author has contributed to research in topics: Shear stress & Glycocalyx. The author has an hindex of 61, co-authored 257 publications receiving 12650 citations. Previous affiliations of John M. Tarbell include Pennsylvania State University & University of Utah.

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The Structure and Function of the Endothelial Glycocalyx Layer

TL;DR: The mechanical and biochemical properties of the EGL and the latest studies on the interactions of this layer with red and white blood cells are examined, including its deformation owing to fluid shear stress, its penetration by leukocyte microvilli, and its restorative response after the passage of a white cell in a tightly fitting capillary.
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Vascular permeability in experimental diabetes is associated with reduced endothelial occludin content: vascular endothelial growth factor decreases occludin in retinal endothelial cells. Penn State Retina Research Group.

TL;DR: These data show that diabetes selectively reduces retinal occludin protein expression and increases BRB permeability, and suggest that the elevated VEGF in the vitreous of patients with diabetic retinopathy increases vascular permeability by downregulating occlUDin content.
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Heparan sulfate proteoglycan is a mechanosensor on endothelial cells.

TL;DR: These experiments demonstrate that a heparan sulfate component of the EC glycocalyx participates in mechanosensing that mediates NO production in response to shear stress.
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Mechanotransduction and the glycocalyx.

TL;DR: The evidence in support of the surface glycocalyx acting as a mechanotransducer of shear stress by ECs is considered and the mechanisms by which these forces are transduced into biomolecular responses of the cells are considered.
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The role of endothelial glycocalyx components in mechanotransduction of fluid shear stress.

TL;DR: The results may be interpreted in terms of a glypican-caveolae-eNOS mechanism for shear-induced NO transduction, with PGI(2) being transduced in basal adhesion plaques that sense the same reaction stress whether the glycocalyx is intact or not.