Vascular Endothelial Surface Proteins in the Perfused Rabbit Lung

1989 ◽  
pp. 43-54 ◽  
Author(s):  
C. Norman Gillis ◽  
Marilyn P. Merker ◽  
William W. Carley
Keyword(s):  
Surface Proteins ◽  
Vascular Endothelial ◽  
Rabbit Lung ◽  
Endothelial Surface

scholarly journals Role of the endothelial glycocalyx in dromotropic, inotropic, and arrythmogenic effects of coronary flow

2000 ◽  
Vol 278 (1) ◽  
pp. H106-H116 ◽  
Author(s):  
Rafael Rubio ◽  
Guillermo Ceballos
Keyword(s):  
Coronary Flow ◽  
Parenchymal Cell ◽  
Cell Types ◽  
Surface Proteins ◽  
Inotropic Effect ◽  
Endothelial Glycocalyx ◽  
Inotropic Effects ◽  
Cardiac Functions ◽  
Endothelial Surface ◽  
Flow Effects

Coronary flow regulates cardiac functions, and it has been suggested that endothelial membrane glycosylated proteins are the primary shear stress mechanosensors. Our hypothesis was that if these proteins are the sensors for flow, then intracoronary perfusion of lectins or specific antibodies should differentially depress coronary flow-enhanced responses of different parenchymal cell types such as auricular-ventricular (A-V) nodal cells (dromotropic effect), contractile myocytes (inotropic effect), and junctional Purkinje-muscle cells (spontaneous ventricular rhythm). The coronary flow stimulatory effects on A-V delay and spontaneous ventricular rhythm were selectively depressed by six of eight lectins. None of the lectins depressed the coronary flow inotropic effect. Antibodies against endothelial surface proteins, αvβ5-integrin and sialyl-Lewisb glycan, depressed the dromotropic but not the inotropic effects of coronary flow, whereas the vascular cell adhesion molecule 1 antibody had no effect on the dromotropic, but enhanced the inotropic, effect. The fact that lectins and antibodies differentially depressed regional coronary flow effects suggests that there is a chemical distinctiveness in their intravascular endothelial cell surfaces. However, nonselective cross-linking of endothelial glycocalyx proteins with 2,000-kDa dextran-aldehyde or vitronectin indistinctively depressed the dromotropic and inotropic effects of coronary flow. These results indicate that coronary flow-induced stress acts on specific structures located in the capillary intravascular membrane glycocalyx.

gp60 is an albumin-binding glycoprotein expressed by continuous endothelium involved in albumin transcytosis

1992 ◽  
Vol 262 (1) ◽  
pp. H246-H254 ◽  
Author(s):  
J. E. Schnitzer
Keyword(s):  
Surface Proteins ◽  
Albumin Binding ◽  
Small Intestinal Mucosa ◽  
Endothelial Surface ◽  
Rat Hearts ◽  
Sinusoidal Endothelium ◽  
Small Intestinal ◽  
Rat Tissue ◽  
Binding Glycoprotein

Albumin reduces capillary permeability and acts as a carrier for various small molecules. Recently, we identified a 60-kDa sialoglycoprotein (gp60) on the surface of cultured rat microvascular endothelial cells (MEC) that binds albumin and antiglycophorin serum (alpha-gp). We verified that alpha-gp recognizes the albumin-binding gp60 by affinity, purifying proteins from MEC extracts using immobilized albumin. gp60 was immunoblotted with alpha-gp only when the MEC extract was reacted with albumin and not in controls. We immunoprecipitated gp60 from biosynthetically radiolabeled MEC lysates and from extracts containing endothelial surface proteins of isolated rat hearts that were radioiodinated in situ. gp60 was immunoblotted selectively in rat tissue microvascular beds lined with continuous endothelium (heart, lung, diaphragm, fat, skeletal muscle, mesentery, and duodenal muscularis but not cortical brain) and not those exclusively lined with fenestrated or sinusoidal endothelium (adrenal, pancreas, liver, and small intestinal mucosa). MEC isolated from rat heart, lung, and epididymal fat pad expressed gp60 and bound albumin, whereas various nonendothelial cells and brain-derived MEC did not. gp60 is an albumin-binding glycoprotein expressed specifically on the surface of continuous endothelium that binds albumin apparently not only to initiate its transcytosis via plasmalemmal vesicles but also to increase capillary permselectivity.

scholarly journals Transcellular migration of leukocytes is mediated by the endothelial lateral border recycling compartment

2009 ◽  
Vol 206 (12) ◽  
pp. 2795-2808 ◽  
Author(s):  
Zahra Mamdouh ◽  
Alexei Mikhailov ◽  
William A. Muller
Keyword(s):  
Endothelial Cell ◽  
Adhesion Molecule ◽  
Molecular Mechanisms ◽  
Vascular Endothelial Cell ◽  
Dependent Manner ◽  
Vascular Endothelial ◽  
Lateral Border ◽  
Endothelial Surface ◽  
Platelet Endothelial Cell Adhesion ◽  
Intracellular Adhesion Molecule

Leukocyte migration across endothelial cell borders (paracellular) and through endothelial cells (transcellular) appear to be distinct processes. During paracellular migration, membrane from a parajunctional reticulum of interconnected vesicles, the endothelial lateral border recycling compartment (LBRC), moves to surround the leukocyte in a kinesin-mediated, microtubule-dependent manner. We show that transcellular migration likewise requires targeted trafficking of LBRC membrane. We show that in addition to platelet/endothelial cell adhesion molecule (PECAM; CD31), CD99 and junctional adhesion molecule A (JAM-A), but apparently not vascular endothelial cell–specific cadherin (cadherin 5, CD144), are components of the LBRC. During transcellular migration, LBRC membrane invests the transmigrating leukocyte. Intracellular adhesion molecule 1 (ICAM-1) on the apical endothelial surface is enriched around adherent leukocytes. Depolymerization of microtubules has no effect on ICAM-1 enrichment but blocks targeted trafficking of LBRC membrane and transcellular migration by >90%. Similar to their effects on paracellular transmigration, antibodies against PECAM or CD99, but not JAM-A, block transcellular migration. We conclude that similar molecular mechanisms promote both para- and transcellular migration.

MS127 EXPRESSIONS OF MACROPHAGE METALLOELASTASE (MMP-12) IN EXTRACELLULAR MATRIX OF ATHEROSCLEROTIC TISSUES FOLLOWING DISRUPTION OF THE VASCULAR ENDOTHELIAL SURFACE

2010 ◽  
Vol 11 (2) ◽  
pp. 135
Author(s):  
M. Mustakim ◽  
G.A. Froemming ◽  
M.S. Abdul Rahman ◽  
H. Nawawi ◽  
N. Ismail ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Vascular Endothelial ◽  
Endothelial Surface

scholarly journals Shear flow–dependent integration of apical and subendothelial chemokines in T-cell transmigration: implications for locomotion and the multistep paradigm

Blood ◽  
2006 ◽  
Vol 109 (4) ◽  
pp. 1381-1386 ◽  
Author(s):  
Taylor H. Schreiber ◽  
Vera Shinder ◽  
Derek W. Cain ◽  
Ronen Alon ◽  
Robert Sackstein
Keyword(s):  
T Cells ◽  
T Cell ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
T Cell Migration ◽  
Human T Cell ◽  
Endothelial Surface ◽  
Hydrodynamic Shear ◽  
Spatially Distributed ◽  
Static Conditions

Abstract Lymphocyte extravasation requires that emigrating cells process chemoattractant signals, typically mediated by chemokines, encountered on endothelial surface (apical) and subendothelial (basal) compartments. These signals are delivered under conditions of hemodynamic shear, a fundamental feature of all physiologic leukocyte–endothelial interactions. To analyze lymphocyte responsiveness to spatially distributed chemokines and their effects on transendothelial migration (TEM) under hydrodynamic shear, we constructed a transwell-based flow assay. We observed that the inflammatory chemokine CCL5 (RANTES) induces negligible human T-cell migration across inflamed human umbilical vascular endothelial cells (HUVECs) when displayed alone in the subendothelial compartment under static or hemodynamic shear conditions or when combined with apical CXCL12 (SDF-1α) under static conditions. However, under shear stress, T cells encountering apically presented CXCL12 were primed to undergo robust LFA-1–dependent TEM toward subendothelial CCL5. Notably, locomotive T cells arriving at endothelial junctions were retained and extended pseudopodia into and through the junctions, thereby increasing sensitivity to subendothelial CCL5. These findings provide the first evidence that lymphocytes integrate, conditional to shear forces, permissive apical chemokine deposits, and integrin engagement signals, resulting in morphologic changes and amplified chemotaxis to an otherwise weak subendothelial chemokine signal.

Expression of vascular endothelial growth factor receptor (VEGF-R) and CD31 receptor (CD31-R) in high-grade neuroendocrine carcinoma of the uterine cervix (cNEC) and its association with prognosis.

2012 ◽  
Vol 30 (15_suppl) ◽  
pp. e15580-e15580
Author(s):  
James A Kuzman ◽  
Boris G. Naraev ◽  
Anna M Button ◽  
Megan I Samuelson ◽  
Michael J Goodheart ◽  
...  
Keyword(s):  
Growth Factor Receptor ◽  
Surface Proteins ◽  
Vascular Endothelial ◽  
High Grade ◽  
Proportional Hazard ◽  
Risk Of Death ◽  
Cox Proportional Hazard ◽  
Unit Increase ◽  
Endothelial Growth Factor

e15580 Background: High-grade cNEC is uncommon cancer, and the optimal treatment is unclear. It is not known if cNEC expresses surface proteins related to angiogenesis. The aim of this study is to evaluate the expression of proteins involved in angiogenesis, as well as their possible association with clinical outcomes. Methods: Expression of VEGF-R and CD31-R was analyzed with standard immunohistochemical methods in tumor specimens from 16 patients with cNEC seen at our institution from 1977 to 2010. CD31-R expression was estimated by analyzing microvessel density using a CD31 specific antibody. Intensity and percentage of cells expressing VEGF-R was determined. Univariate survival analysis was performed using a Cox Proportional Hazard Model. Results: VEGF-R was expressed in 15 out of 16 specimens whereas CD31-R was expressed in all specimens. Increased VEGF-R expression correlated with shortened survival but the association was not statistically significant (p=0.0544, hazard ratio=1.514, CI=0.992-2.309). A one unit increase in VEGF-R expression correlated with increase in the risk of death by 51.4%. CD31-R expression showed no significant association with survival (p=0.9638,CI=0.865-1.165). Conclusions: VEGF-R and CD31-R are expressed by most cNECs. Increased VEGF-R, but not CD31-R, expression may be associated with worse survival. Further exploration of the role of angiogenesis in cervical NETs is warranted.

scholarly journals Human vascular endothelial cells transport foreign exosomes from cow's milk by endocytosis

2016 ◽  
Vol 310 (10) ◽  
pp. C800-C807 ◽  
Author(s):  
Rio Jati Kusuma ◽  
Sonia Manca ◽  
Taylor Friemel ◽  
Sonal Sukreet ◽  
Christopher Nguyen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Incubation Temperature ◽  
Vascular Endothelial Cells ◽  
Umbilical Vein ◽  
Surface Proteins ◽  
Proteinase K ◽  
Cow’S Milk ◽  
Vascular Endothelial ◽  
Peripheral Tissues ◽  
Cow's Milk

Encapsulation of microRNAs in exosomes confers protection against degradation and a vehicle for shuttling of microRNAs between cells and tissues, and cellular uptake by endocytosis. Exosomes can be found in foods including milk. Humans absorb cow's milk exosomes and deliver the microRNA cargo to peripheral tissues, consistent with gene regulation by dietary nucleic acids across species boundaries. Here, we tested the hypothesis that human vascular endothelial cells transport milk exosomes by endocytosis, constituting a step crucial for the delivery of dietary exosomes and their cargo to peripheral tissues. We tested this hypothesis by using human umbilical vein endothelial cells and fluorophore-labeled exosomes isolated from cow's milk. Exosome uptake followed Michaelis-Menten kinetics ( Vmax = 0.057 ± 0.004 ng exosome protein × 40,000 cells/h; Km = 17.97 ± 3.84 μg exosomal protein/200 μl media) and decreased by 80% when the incubation temperature was lowered from 37°C to 4°C. When exosome surface proteins were removed by treatment with proteinase K, or transport was measured in the presence of the carbohydrate competitor d-galactose or measured in the presence of excess unlabeled exosomes, transport rates decreased by 45% to 80% compared with controls. Treatment with an inhibitor of endocytosis, cytochalasin D, caused a 50% decrease in transport. When fluorophore-labeled exosomes were administered retro-orbitally, exosomes accumulated in liver, spleen, and lungs in mice. We conclude that human vascular endothelial cells transport bovine exosomes by endocytosis and propose that this is an important step in the delivery of dietary exosomes and their cargo to peripheral tissues.

Localization of endothelin-converting enzyme-1 in human kidney

1997 ◽  
Vol 273 (5) ◽  
pp. F749-F756 ◽  
Author(s):  
C. Pupilli ◽  
P. Romagnani ◽  
L. Lasagni ◽  
F. Bellini ◽  
N. Misciglia ◽  
...  
Keyword(s):  
Human Kidney ◽  
Distribution Patterns ◽  
Renal Tumors ◽  
Mrna Levels ◽  
Vascular Endothelial ◽  
Converting Enzyme ◽  
Vasa Recta ◽  
Endothelial Surface ◽  
Endothelin Converting Enzyme ◽  
Von Willebrand

The distribution of endothelin-converting enzyme-1 (ECE-1) mRNA and protein was investigated in human kidney excised because of renal tumors. ECE-1 immunoreactivity was detected by immunohistochemistry throughout the different areas of the kidney in the vascular and tubular structures. In the cortex, ECE-1 immunostaining was present in the endothelial surface of arcuate and interlobular arteries and in arterioles. Weak specific immunoreactivity was present over some proximal and distal tubules. Few endothelial glomerular cells contained ECE-1 protein. In the medulla, ECE-1 immunoreactivity was observed in the vasa recta bundles and capillaries. ECE-1 immunostaining was also detected in the outer and inner medullary collecting ducts and thin limbs of Henle’s loops. Immunohistochemical detection of the von Willebrand factor on adjacent sections confirmed the endothelial nature of the vascular cells that exhibited ECE-1 immunostaining. The distribution patterns of ECE-1 mRNA, investigated by in situ hybridization, appeared similar to that obtained by immunohistochemistry in the cortical and medullary vasculature and in different portions of the nephron. Northern blot and densitometric analyses demonstrated that ECE-1 mRNA levels were quantitatively similar in both the renal cortex and medulla. These results demonstrate that vascular endothelial and tubular epithelial cells in the cortex and medulla of the human kidney synthesize ECE-1, which, in turn, may play an important role in regulating endothelin production in physiological and pathological conditions.

Antiphospholipid Antibodies Activate Vascular Endothelial Cells

Lupus ◽  
1996 ◽  
Vol 5 (5) ◽  
pp. 440-441 ◽  
Author(s):  
R Simantov ◽  
SK Lo ◽  
A Gharavi ◽  
LR Sammaritano ◽  
JE Salmon ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Antiphospholipid Antibodies ◽  
Vascular Endothelial Cells ◽  
Leukocyte Adhesion ◽  
Fetal Loss ◽  
Endothelial Activation ◽  
Vascular Endothelial ◽  
Endothelial Surface ◽  
Endotoxin Contamination ◽  
Leukocyte Adhesion Molecules

Antiphospholipid antibodies (aPL) are associated with a syndrome of arterial and venous thrombosis and recurrent fetal loss. We have shown that IgG purified from patients with aPL activate vascular endothelial cells (EC), converting the steady-state, non-thrombotic endothelial surface to a pro-thrombotic state. The aPL-activated EC are characterized by the expression of leukocyte adhesion molecules, including ICAM-1, VCAM, and E-selectin. EC activation is dependent upon the presence of β2-GP-I, a cofactor necessary for anticardiolipin reactivity. In addition, EC activation is not attributable to endotoxin contamination, Fc receptor interactions, or immune complexes, but rather is the result of the specific anticardiolipin reactivity of the IgG. Endothelial activation by aPL may be an important mechanism by which these antibodies cause a hypercoagulable state.

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