scholarly journals Immunocytochemical studies of endothelial cells in vivo. II. Chicken aortic and capillary endothelial cells exhibit different cell surface distributions of the integrin complex.

1988 ◽  
Vol 36 (10) ◽  
pp. 1309-1317 ◽  
Author(s):  
T Fujimoto ◽  
S J Singer
Keyword(s):  
Endothelial Cells ◽  
Monoclonal Antibodies ◽  
Cell Types ◽  
Frozen Sections ◽  
Double Labeling ◽  
Adhesion Properties ◽  
Aortic Endothelial Cells ◽  
Capillary Endothelial Cells ◽  
Aortic Endothelial

Frozen sections of chicken tissues containing aortic and capillary endothelial cells were immunolabeled with two mouse monoclonal antibodies directed to different epitopes of the chicken integrin beta-chain. Integrin is an integral membrane protein complex that is believed to mediate a transmembrane linkage between the extracellular matrix and the actin cytoskeleton. In immunofluorescence experiments with semi-thin frozen sections, the aortic endothelial cells were labeled for integrin all around their surfaces, whereas capillary endothelial cells of heart and kidney were labeled only on their basal surfaces. At the immunofluorescence level of resolution, the distribution of integrin appeared to be correlated with that of F-actin in double-labeling experiments with NBD-phallacidin. These different distributions of integrin on the two types of endothelial cells were definitively confirmed by immunoelectron microscopic labeling with the monoclonal antibodies on ultra-thin frozen sections. These results therefore indicate that the luminal surfaces, as well as the underlying cytoskeleton of capillary endothelial cells, are significantly different in structure from those of aortic endothelial cells. These differences may reflect the vastly different hemodynamic stress to which the two types of endothelial cells are subjected, and in addition may mediate different adhesion properties of the luminal surfaces of the two cell types.

scholarly journals Urea transporters are distributed in endothelial cells and mediate inhibition of l-arginine transport

2002 ◽  
Vol 283 (3) ◽  
pp. F578-F582 ◽  
Author(s):  
Laszlo Wagner ◽  
Janet D. Klein ◽  
Jeff M. Sands ◽  
Chris Baylis
Keyword(s):  
Endothelial Cells ◽  
Cell Types ◽  
Inhibitory Effect ◽  
Rat Aorta ◽  
Wide Distribution ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Elevated Blood Urea Nitrogen ◽  
Aortic Endothelial

Our laboratory previously reported that uremic levels of urea inhibitl-arginine (l-Arg) transport into endothelial cells. The present study further investigated this effect. We measuredl-Arg transport in cultured bovine aortic endothelial cells with normal or high urea (25 mM). The urea transport inhibitor phloretin abolished the inhibitory effect of urea on l-Arg transport, suggesting a role for urea transporters (UTs). We screened bovine aortic endothelial cells and several other endothelial cell types for the presence of UTs by using Western blot analysis. UT-B was present in all endothelial cells, irrespective of species or location of derivation, whereas UT-A distribution was variable and sparse. UT-B was also abundant in rat aorta, mesenteric blood vessels, and spinotrapezius muscle, whereas UT-A distribution was, again, variable and sparse. Chronic elevation of urea had variable, inconsistent effects on UT abundance. This study showed that urea must enter endothelial cells, probably by UT-B, to inhibit l-Arg transport. In view of the wide distribution of UT-B in rat vasculature, elevated blood urea nitrogen may lead to endothelial l-Arg deficiency in vivo.

scholarly journals Capillary endothelial cell cultures: phenotypic modulation by matrix components.

1983 ◽  
Vol 97 (1) ◽  
pp. 153-165 ◽  
Author(s):  
J A Madri ◽  
S K Williams
Keyword(s):  
Endothelial Cells ◽  
Basement Membrane ◽  
Membrane Surface ◽  
Phenotypic Expression ◽  
Aortic Endothelial Cells ◽  
Capillary Endothelial Cells ◽  
Endothelial Cell Cultures ◽  
Cell Densities

Capillary endothelial cells of rat epididymal fat pad were isolated and cultured in media conditioned by bovine aortic endothelial cells and substrata consisting of interstitial or basement membrane collagens. When these cells were grown on interstitial collagens they underwent proliferation, formed a continuous cell layer and, if cultured for long periods of time, formed occasional tubelike structures. In contrast, when these cells were grown on basement membrane collagens, they did not proliferate but did aggregate and form tubelike structures at early culture times. In addition, cells grown on basement membrane substrata expressed more basement membrane constituents as compared with cells grown on interstitial matrices when assayed by immunoperoxidase methods and quantitated by enzyme-linked immunosorbent inhibition assays. Furthermore, when cells were grown on either side of washed, acellular amnionic membranes their phenotypes were markedly different. On the basement membrane surface they adhered, spread, and formed tubelike structures but did not migrate through the basement membrane. In contrast, when seeded on the stromal surface, these cells were observed to proliferate and migrate into the stromal aspect of the amnion and ultimately formed tubelike structures at high cell densities at longer culture periods (21 d). Thus, connective tissue components play important roles in regulating the phenotypic expression of capillary endothelial cells in vitro, and similar roles of the collagenous components of the extracellular matrix may exist in vivo following injury and during angiogenesis. Furthermore, the culture systems outlined here may be of use in the further study of differentiated, organized capillary endothelial cells in culture.

Stimulation Of Prostacyclin Production In Aortic Endothelial Cells By A Non-Dialysable Serum Factor

1981 ◽  
Author(s):  
E R Hall ◽  
M Rafelson ◽  
K Wu
Keyword(s):  
Endothelial Cells ◽  
Arachidonic Acid ◽  
Calf Serum ◽  
Dependent Manner ◽  
Freezing And Thawing ◽  
Concentration Dependent Manner ◽  
Aortic Endothelial Cells ◽  
Prostacyclin Production ◽  
Aortic Endothelial

The production of prostacyclin (PGI2) by vascular endothelial cells is thought to be of primary importance in maintaining normal hemostasis. We have investigated the production of prostacyclin in bovine arterial endothelial cells maintained in Dulbecco’s modified Eagle’s medium (DMEM) containing 30% fetal calf serum. Intact, confluent monolayers of endothelial cells (3x106 cells) in passages 2 through 6 were used. The growth medium was removed and the cells were washed in DMEM that did not contain serum. 3 mls of medium alone or containing normal plasma or serum was then added and incubated at 37°C for 15 min. Then, 1 mg of arachidonic acid was added and the cells incubated for an additional hour. The test medium was removed, centrifuged to remove any loose cells and stored at -70°C. To determine the production of PGI2 by the endothelial cells, the medium was assayed for 6-keto-PGF1α, the stable metabolite of PGI2, by radioimmunoassay. The synthesis of prostacyclin by bovine aortic endothelial cells was significantly increased in a concentration dependent manner by both normal platelet poor plasma and normal serum. This increase in prostacyclin production was inhibited by both aspirin and indomethacin, indicating an increase in synthesis rather than the release of PGI2. Furthermore, this increase could be demonstrated in the presence or absence of added arachidonic acid. The active component in plasma and serum was non-dialysable, eliminating the possibility of a small compound such as bradykinin or angiotensin II. This active factor was present after freezing and thawing the plasma and serum and was heat stable (60°C, 5 min). The presence of an endogenous prostacyclin stimulating factor may be significant in the in vivo regulation of prostacyclin production.

Brain and atrial natriuretic peptides bind to common receptors in brain capillary endothelial cells

1991 ◽  
Vol 261 (2) ◽  
pp. E183-E189 ◽  
Author(s):  
R. A. Gelfand ◽  
H. J. Frank ◽  
E. Levin ◽  
A. Pedram
Keyword(s):  
Endothelial Cells ◽  
Guanylate Cyclase ◽  
Natriuretic Peptides ◽  
Common Mechanism ◽  
Brain Capillary ◽  
Aortic Endothelial Cells ◽  
Brain Capillary Endothelial Cells ◽  
Capillary Endothelial Cells ◽  
Atrial Natriuretic ◽  
Aortic Endothelial

The recent discovery of brain natriuretic peptides (BNP) that stimulates natriuresis, diuresis, and vascular smooth muscle relaxation in a manner similar to that of atrial natriuretic peptide (ANP) suggests the possibility that these endocrine hormones function via some common mechanism. Indirect evidence from several laboratories suggests that BNP and ANP may bind to the same receptors. We examined whether ANP and BNP bind to a common set of receptors in cultured bovine brain capillary endothelial cells and in bovine aortic endothelial cells. Scatchard plot analysis of binding data shows a similar dissociation constant (KD) of approximately 0.3 nM and a maximal binding capacity (Bmax) of 50 fmol/mg protein for both natriuretic peptides in brain capillary cells and 0.6 nM and 80 fmol/mg protein, respectively, in the aortic endothelial cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the affinity cross-linked receptor-ligand complex shows a strongly labeled 65-kDa receptor and a 125-kDa band that is likely to be a receptor of the guanylate cyclase type. ANP and BNP cross compete equally for binding to the two receptors identified on the gels. ANP and BNP also stimulate guanosine 3', 5'-cyclic monophosphate production in these cells, consistent with the presence of a functional guanylate cyclase-linked B receptor. We conclude that ANP and BNP share common receptors in brain capillary and aortic endothelial cells.

scholarly journals Scavenger Receptors are Present on Rabbit Aortic Endothelial Cells In Vivo

1997 ◽  
Vol 17 (11) ◽  
pp. 2369-2375 ◽  
Author(s):  
Alan Daugherty ◽  
Joseph A. Cornicelli ◽  
Kathryn Welch ◽  
Sandra M. Sendobry ◽  
Debra L. Rateri
Keyword(s):  
Endothelial Cells ◽  
Scavenger Receptors ◽  
Aortic Endothelial Cells ◽  
Aortic Endothelial

scholarly journals Novel Vascular Molecule Involved in Monocyte Adhesion to Aortic Endothelium in Models of Atherogenesis

1997 ◽  
Vol 185 (12) ◽  
pp. 2069-2077 ◽  
Author(s):  
Leslie M. McEvoy ◽  
Hailing Sun ◽  
Philip S. Tsao ◽  
John P. Cooke ◽  
Judith A. Berliner ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Ex Vivo ◽  
Critical Role ◽  
Constitutive Expression ◽  
Monocyte Adhesion ◽  
Aortic Endothelial Cells ◽  
Aortic Endothelium ◽  
Aortic Endothelial

Adhesion of monocytes to the endothelium in lesion-prone areas is one of the earliest events in fatty streak formation leading to atherogenesis. The molecular basis of increased monocyte adhesion is not fully characterized. We have identified a novel vascular monocyte adhesion-associated protein, VMAP-1, that plays a role in adhesion of monocytes to activated endothelium. Originally selected for its ability to block binding of a mouse monocyte-like cell line (WEHI78/24) to cytokine- or LPS-stimulated cultured mouse endothelial cells in vitro, antiVMAP-1 mAb LM151 cross-reacts with rabbit endothelium and blocks binding of human monocytes to cultured rabbit aortic endothelial cells stimulated with minimally modified low density lipoprotein, thought to be a physiologically relevant atherogenic stimulus. Most importantly, LM151 prevents adhesion of normal monocytes and monocytoid cells to intact aortic endothelium from cholesterol-fed rabbits in an ex vivo assay. VMAP-1 is a 50-kD protein. Immunohistology of vessels reveals focal constitutive expression in aorta and other large vessels. VMAP-1 is thus a novel vascular adhesion-associated protein that appears to play a critical role in monocyte adhesion to aortic endothelial cells in atherogenesis in vivo.

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