scholarly journals The Glycocalyx and Pressure-Dependent Transcellular Albumin Transport

2020 ◽  
Vol 11 (6) ◽  
pp. 655-662 ◽  
Author(s):  
Randal O. Dull ◽  
Andreia Z. Chignalia
Keyword(s):  
Endothelial Cells ◽  
Hydrostatic Pressure ◽  
Solute Flux ◽  
Microvascular Endothelial Cells ◽  
Rat Lung ◽  
Transport Pathway ◽  
Transcellular Transport ◽  
Microvascular Endothelial ◽  
Heparan Sulfates ◽  
Uptake And Transport

Abstract Purpose Acute increases in hydrostatic pressure activate endothelial signaling pathways that modulate barrier function and vascular permeability. We investigated the role the glycocalyx and established mechanotransduction pathways in pressure-induced albumin transport across rat lung microvascular endothelial cells. Methods Rat lung microvascular endothelial cells (RLMEC) were cultured on Costar Snapwell chambers. Cell morphology was assessed using silver nitrate staining. RLMEC were exposed to zero pressure (Control) or 30 cmH2O (Pressure) for 30 or 60 min. Intracellular albumin uptake and transcellular albumin transport was quantified. Transcellular transport was reported as solute flux (Js) and an effective permeability coefficient (Pe). The removal of cell surface heparan sulfates (heparinase), inhibition of NOS (L-NAME) and reactive oxygen species (apocynin, Apo) was investigated. Results Acute increase in hydrostatic pressure augmented albumin uptake by 30–40% at 60 min and Js and Pe both increased significantly. Heparinase increased albumin uptake but attenuated transcellular transport while L-NAME attenuated both pressure-dependent albumin uptake and transport. Apo interrupted albumin uptake under both control and pressure conditions, leading to a near total lack of transcellular transport, suggesting a different mechanism and/or site of action. Conclusion Pressure-dependent albumin uptake and transcellular transport is another component of endothelial mechanotransduction and associated regulation of solute flux. This novel albumin uptake and transport pathway is regulated by heparan sulfates and eNOS. Albumin uptake is sensitive to ROS. The physiological and clinical implications of this albumin transport are discussed.

Hypoxia Modulates the Cellular Signaling in Cultured Rat Lung Microvascular Endothelial Cells

CHEST Journal ◽  
2014 ◽  
Vol 146 (4) ◽  
pp. 857A
Author(s):  
Badri Giri ◽  
Shekhar Ghamande ◽  
David Zawieja ◽  
Mohammad Uddin
Keyword(s):  
Endothelial Cells ◽  
Cellular Signaling ◽  
Microvascular Endothelial Cells ◽  
Rat Lung ◽  
Microvascular Endothelial

Metabolism of nicotine in rat lung microvascular endothelial cells

2006 ◽  
Vol 58 (3) ◽  
pp. 403-407 ◽  
Author(s):  
Yoshinori Ochiai ◽  
Kunio Itoh ◽  
Yorihisa Tanaka ◽  
Eiichi Sakurai ◽  
Akio Nomura
Keyword(s):  
Endothelial Cells ◽  
Microvascular Endothelial Cells ◽  
Rat Lung ◽  
Microvascular Endothelial

Isolation, culture, and characterization of rat lung microvascular endothelial cells

1994 ◽  
Vol 267 (4) ◽  
pp. L433-L441 ◽  
Author(s):  
J. C. Magee ◽  
A. E. Stone ◽  
K. T. Oldham ◽  
K. S. Guice
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Cell Function ◽  
Primary Cultures ◽  
Microvascular Endothelial Cells ◽  
Rat Lung ◽  
Simple Method ◽  
Endothelial Cell Function ◽  
Microvascular Endothelial

Highly pure primary cultures of rat lung microvascular endothelial cells were obtained from peripheral lung tissue using a combination of selective culture strategies. The cells had a characteristic morphology consistent with an endothelial origin and were positive for a number of endothelial cell markers, including uptake of fluorescent acetylated lactate dehydrogenase, binding of the lectin Bandeiraea simplicifolia I, and positive immunofluorescence staining with two endothelial cell monoclonal antibodies. The cells behaved as microvascular endothelial cells using an in vitro angiogenesis assay. This isolation method provides a simple method for culturing the pulmonary microvasculature of the rat and these studies support the idea that endothelial cells from different vessels exhibit phenotypic heterogeneity. This method should prove useful for studying specialized endothelial cell function and differentiation in vitro.

Stereoselective transport of histidine in rat lung microvascular endothelial cells

2002 ◽  
Vol 282 (6) ◽  
pp. L1192-L1197 ◽  
Author(s):  
Eiichi Sakurai ◽  
Tomoya Sakurada ◽  
Yoshinori Ochiai ◽  
Jun Yamakami ◽  
Yorihisa Tanaka
Keyword(s):  
Endothelial Cells ◽  
Glutamic Acid ◽  
Uptake Rate ◽  
Metabolic Inhibitors ◽  
Microvascular Endothelial Cells ◽  
Facilitated Diffusion ◽  
Rat Lung ◽  
Independent System ◽  
System L ◽  
Microvascular Endothelial

The transport characteristics of l- and d-histidine through the blood-lung barrier were studied in cultured rat lung microvascular endothelial cells (LMECs). l-Histidine uptake was a saturable process. The addition of metabolic inhibitors [2,4-dinitrophenol (DNP) and rotenone] reduced the uptake rate ofl-histidine. Ouabain, an inhibitor of Na+-K+-ATPase, also reduced uptake ofl-histidine. Moreover, the initial l-histidine uptake rate was reduced by the substitution of Na+ with choline chloride and choline bicarbonate in the incubation buffer. The system N substrate, l-glutamic acid γ-monohydroxamate, also inhibited uptake of l-histidine. However, system N-mediated transport was not pH sensitive. These results demonstrated that l-histidine is actively taken up by a system N transport mechanism into rat LMECs, with energy supplied by Na+. Moreover, the Na+-independent system L substrate, 2-amino-2-norbornanecarboxylic acid (BCH), had an inhibitory effect on l-histidine uptake in Na+ removal, indicating facilitated diffusion by a Na+-independent system L transport into the rat LMECs. These results provide evidence for there being at least two pathways for l-histidine uptake into rat LMECs, a Na+-dependent system N and Na+-independent system L process. On the other hand, the uptake of d-histidine into rat LMECs was not reduced by the addition of DNP, rotenone, or ouabain, or by Na+replacement. Although the uptake of d-histidine was reduced in the presence of BCH, the addition of l-glutamic acid γ-monohydroxamate did not significantly decrease uptake ofd-histidine. These results suggest that the uptake ofd-histidine by rat LMECs has different characteristics compared with its isomer, l-histidine, indicating that system N transport did not involve d-histidine uptake.

scholarly journals Transcellular transport of CCL2 across brain microvascular endothelial cells

2008 ◽  
Vol 104 (5) ◽  
pp. 1219-1232 ◽  
Author(s):  
Shujun Ge ◽  
Li Song ◽  
David R. Serwanski ◽  
William A. Kuziel ◽  
Joel S. Pachter
Keyword(s):  
Endothelial Cells ◽  
Microvascular Endothelial Cells ◽  
Brain Microvascular Endothelial Cells ◽  
Transcellular Transport ◽  
Microvascular Endothelial

Ca(2+)-inhibitable adenylyl cyclase and pulmonary microvascular permeability

1997 ◽  
Vol 273 (1) ◽  
pp. L22-L30 ◽  
Author(s):  
P. M. Chetham ◽  
H. A. Guldemeester ◽  
N. Mons ◽  
G. H. Brough ◽  
J. P. Bridges ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adenylyl Cyclase ◽  
Microvascular Permeability ◽  
Microvascular Endothelial Cells ◽  
Rat Lung ◽  
Microvascular Endothelium ◽  
Camp Content ◽  
Microvascular Endothelial ◽  
Vitro Model

Intracellular mechanisms responsible for endothelial cell disruption are unknown, although either elevated cytosolic Ca2+ ([Ca2+]i) or decreased adenosine 3',5'-cyclic monophosphate (cAMP) promotes permeability. Recent identification that Ca(2+)-inhibitable adenylyl cyclase establishes an inverse relationship between [Ca2+]i and cAMP in macrovascular endothelial cells provided a possible mechanism of development of permeability. However, these data utilized an in vitro model; lacking was evidence supporting 1) expression of Ca(2+)-inhibitable adenylyl cyclase in pulmonary microvascular endothelium and 2) Ca2+ inhibition of adenylyl cyclase and cAMP content as a paradigm for inflammatory mediator-induced permeability in the intact circulation. We therefore addressed these issues in microvascular endothelial cells derived from rat lung and in an isolated perfused rat lung preparation. Results demonstrate expression of a Ca(2+)-inhibitable adenylyl cyclase in microvascular endothelial cells. Furthermore, data suggest that Ca2+ inhibition of adenylyl cyclase is necessary for development of microvascular permeability in the intact circulation. We conclude Ca2+ inhibition of cAMP represents a critical step in genesis of microvascular permeability in the intact pulmonary circulation.

Resveratrol Reduces Matrix Metalloproteinase-2 Activity Induced by Oxygen-Glucose Deprivation and Reoxygenation in Human Cerebral Microvascular Endothelial Cells

2012 ◽  
Vol 82 (4) ◽  
pp. 267-274 ◽  
Author(s):  
Zahide Cavdar ◽  
Mehtap Y. Egrilmez ◽  
Zekiye S. Altun ◽  
Nur Arslan ◽  
Nilgun Yener ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Neuroprotective Effect ◽  
Ischemia Reperfusion ◽  
Neurovascular Unit ◽  
Glucose Deprivation ◽  
Matrix Metalloproteinase 2 ◽  
Microvascular Endothelial Cells ◽  
Oxygen Glucose Deprivation ◽  
Microvascular Endothelial

The main pathophysiology in cerebral ischemia is the structural alteration in the neurovascular unit, coinciding with neurovascular matrix degradation. Among the human matrix metalloproteinases (MMPs), MMP-2 and -9, known as gelatinases, are the key enzymes for degrading type IV collagen, which is the major component of the basal membrane that surrounds the cerebral blood vessel. In the present study, we investigated the effects of resveratrol on cytotoxicity, reactive oxygen species (ROS), and gelatinases (MMP-2 and -9) in human cerebral microvascular endothelial cells exposed to 6 hours of oxygen-glucose deprivation and a subsequent 24 hours of reoxygenation with glucose (OGD/R), to mimic ischemia/reperfusion in vivo. Lactate dehydrogenase increased significantly, in comparison to that in the normoxia group. ROS was markedly increased in the OGD/R group, compared to normoxia. Correspondingly, ROS was significantly reduced with 50 μM of resveratrol. The proMMP-2 activity in the OGD/R group showed a statistically significant increase from the control cells. Resveratrol preconditioning decreased significantly the proMMP-2 in the cells exposed to OGD/R in comparison to that in the OGD/R group. Our results indicate that resveratrol regulates MMP-2 activity induced by OGD/R via its antioxidant effect, implying a possible mechanism related to the neuroprotective effect of resveratrol.

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