Growth and Physiological Functions of Vascular Endothelial Cells in a New Serum-Free Medium (SFM)

1993 ◽  
Vol 206 (2) ◽  
pp. 291-301 ◽  
Author(s):  
S. Gorfien ◽  
A. Spector ◽  
D. DeLuca ◽  
S. Weiss
Keyword(s):  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Serum Free Medium ◽  
Free Medium ◽  
Physiological Functions ◽  
Serum Free

High density lipoproteins and the growth of vascular endothelial cells in serum-free medium

In Vitro ◽  
1981 ◽  
Vol 17 (6) ◽  
pp. 519-530 ◽  
Author(s):  
J.-P. -P. Tauber ◽  
J. Cheng ◽  
S. Massoglia ◽  
D. Gospodarowicz
Keyword(s):  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
High Density ◽  
High Density Lipoproteins ◽  
Vascular Endothelial ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free

Human retinal pigment epithelial cells from different donors continuously produce a vascular endothelial cell-stimulating factor into serum-free medium

1993 ◽  
Vol 104 (1) ◽  
pp. 211-218
Author(s):  
Q.R. Yang ◽  
R.M. Smets ◽  
A. Neetens ◽  
D. Vanden Berghe
Keyword(s):  
Endothelial Cells ◽  
Retinal Pigment Epithelial ◽  
Retinal Pigment ◽  
Vascular Endothelial ◽  
Fibroblast Growth ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Pigment Epithelial

Mitogenic activities of human retinal pigment epithelial cell-conditioned medium (HRPE-CM) with different effects, such as inhibition, stimulation or no effect, on the proliferation of vascular endothelial cells (EC) in vitro have been reported. In this study, 14 HRPE cell lines were established from normal human eyes. Human umbilical vein endothelial cells (HUVEC) in the early passages were used as target cells to detect the mitogenic activity of HRPE-CM on the growth of vascular EC. Our results confirm that HRPE cells in culture continuously synthesize and secrete HUVEC growth substance(s) into a serum-free medium. The ability of HRPE cell lines to produce this mitogen seem unrelated either to in vivo donor factors or to in vitro cell life span. Using an enzyme-linked immunosorbance assay, we demonstrated that only HRPE cell extract, not HRPE-CM, can be recognized by basic fibroblast growth factor (bFGF)-specific antibody, though identical bioactivities on the growth of HUVEC were found in both preparations. The active component in HRPE-CM was heat- and trypsin-sensitive, and stable at extremes of pH (2.5 to 10.0). In addition, the bioactive molecule could not pass through a M(r) 30,000 cut-off membrane, suggesting that it is a fairly high molecular mass polypeptide. These observations suggest that the EC growth factor in HRPE-CM is distinct from fibroblast growth factors (FGFs).

Hemoglobin Enhances the Binding of Bacterial Endotoxin to Human Endothelial Cells

1996 ◽  
Vol 76 (02) ◽  
pp. 258-262 ◽  
Author(s):  
Robert I Roth
Keyword(s):  
Endothelial Cells ◽  
Binding Protein ◽  
Bacterial Endotoxin ◽  
Dependent Manner ◽  
Serum Free Medium ◽  
Free Medium ◽  
Human Endothelial Cells ◽  
Serum Factors ◽  
Serum Free ◽  
Lps Binding

SummaryHuman endothelial cells, when incubated with bacterial endotoxin (lipopolysaccharide, LPS), modify their surface in association with prominent production of procoagulant tissue factor (TF) activity. This deleterious biological effect of LPS has been shown previously to be enhanced approximately 10-fold by the presence of hemoglobin (Hb), a recently recognized LPS binding protein that causes disaggregation of LPS and increases the biological activity of LPS in a number of in vitro assays. The present study was performed to test the hypothesis that Hb enhances the LPS-induced procoagulant activity of human umbilical vein endothelial cells (HUVEC) by increasing LPS binding to the cells. The binding of 3H-LPS to HUVEC was determined in the absence or presence of Hb or two other known LPS-binding proteins, human serum albumin (HSA) and IgG. LPS binding was substantially increased in the presence of Hb, in a Hb concentration-dependent manner, but was not increased by HSA or IgG. Hb enhancement of LPS binding was observed in serum-free medium, indicating that there was no additional requirement for any of the serum factors known to participate in the interaction of LPS with cells (e.g., lipopolysaccharide (LPS)-binding protein (LBP) and soluble CD14 (sCD14)). Hb enhancement of LPS binding also was observed in the more physiologic condition of 100% plasma. LPS-induced TF activity was stimulated by Hb, but not by HSA or IgG. In serum-free medium, TF activity was not stimulated under any of the conditions tested. Ultrafiltration of LPS was dramatically increased after incubation with Hb but not with HSA or IgG, suggesting that LPS disaggregation by Hb was responsible for the enhanced binding of LPS to HUVEC and the subsequent stimulation of TF activity.

scholarly journals IGF-I-induced enhancement of contractile response in organ-cultured aortae from diabetic rats is mediated by sustained thromboxane A2 release from endothelial cells

2005 ◽  
Vol 186 (2) ◽  
pp. 367-376 ◽  
Author(s):  
Tsuneo Kobayashi ◽  
Takayuki Matsumoto ◽  
Katsuo Kamata
Keyword(s):  
Endothelial Cells ◽  
Organ Culture ◽  
Contractile Response ◽  
Diabetic Rats ◽  
Receptor Expression ◽  
Diabetic Rat ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Igf I

We have investigated the mechanisms underlying the changes in vascular contractile responsiveness induced by insulin and IGF-I in established streptozotocin-induced diabetic rats. The contractile response to noradrenaline (NA) in organ-cultured diabetic rat aortae cultured with insulin or IGF-I was significantly greater than the corresponding responses in (a) diabetic rat aortae cultured in serum-free medium and (b) control rat aortae cultured with insulin or IGF-I. In aortae from which the endothelium was removed after organ culture the contractile response to NA was greater in those cultured with insulin or IGF-I than in those cultured in serum-free medium. This was not true of aortae endothelium denuded before organ culture. The IGF-I-induced enhancement was prevented by treatment with indomethacin (cyclo-oxygenase inhibitor), SQ29548 (thromboxane (TX) A2 receptor antagonist) or fregrelate (TXA2 synthase inhibitor). IGF-I-induced production of TXB2, a metabolite of TXA2, was greater in diabetic than in control aortae and was attenuated by endothelium denudation, indomethacin or AG1024 (IGF-I receptor inhibitor). The expression of the protein and mRNA for the IGF-I receptor (as assessed by RT-PCR and immunohistochemistry) was markedly increased within endothelial cells in diabetic aortae but only slightly increased within smooth muscle cells (versus control rat aortae). Thus, the NA-induced contractile response in aortae from diabetic rats was enhanced by both insulin and IGF-I and this enhancement may be mediated by sustained cyclo-oxygenase-dependent TXA2 production from endothelial cells. The observed enhancement of IGF-I receptor expression within endothelial cells may be causally related to the potentiation of vascular contractility and the increase in TXA2 production.

Efficiently differentiating vascular endothelial cells from adipose tissue-derived mesenchymal stem cells in serum-free culture

2010 ◽  
Vol 400 (4) ◽  
pp. 461-465 ◽  
Author(s):  
Masamitsu Konno ◽  
Tatsuo S. Hamazaki ◽  
Satsuki Fukuda ◽  
Makoto Tokuhara ◽  
Hideho Uchiyama ◽  
...  
Keyword(s):  
Stem Cells ◽  
Endothelial Cells ◽  
Mesenchymal Stem Cells ◽  
Adipose Tissue ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Serum Free

scholarly journals Glycoconjugates and Related Molecules in Human Vascular Endothelial Cells

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Norihiko Sasaki ◽  
Masashi Toyoda
Keyword(s):  
Endothelial Cells ◽  
Blood Cell ◽  
Vascular Endothelial Cells ◽  
Vascular Diseases ◽  
Cell Trafficking ◽  
Vascular Endothelial ◽  
Carbohydrate Composition ◽  
Vasomotor Tone ◽  
Physiological Functions ◽  
Functional Roles

Vascular endothelial cells (ECs) form the inner lining of blood vessels. They are critically involved in many physiological functions, including control of vasomotor tone, blood cell trafficking, hemostatic balance, permeability, proliferation, survival, and immunity. It is considered that impairment of EC functions leads to the development of vascular diseases. The carbohydrate antigens carried by glycoconjugates (e.g., glycoproteins, glycosphingolipids, and proteoglycans) mainly present on the cell surface serve not only as marker molecules but also as functional molecules. Recent studies have revealed that the carbohydrate composition of the EC surface is critical for these cells to perform their physiological functions. In this paper, we consider the expression and functional roles of endogenous glycoconjugates and related molecules (galectins and glycan-degrading enzymes) in human ECs.

An endothelial cell growth factor derived from human lung carcinoma cells grown in serum-free medium

1987 ◽  
Vol 87 (5) ◽  
pp. 739-747
Author(s):  
C. Walker ◽  
G. Mates ◽  
D. Pumford ◽  
M. Daniel
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Bronchial Carcinoma ◽  
Serum Free Medium ◽  
Free Medium ◽  
Molecular Weight Range ◽  
Serum Free ◽  
Lung Carcinoma Cells ◽  
Human Lung Carcinoma ◽  
Umbilical Vein Endothelial Cells

A factor that stimulates the proliferation of human umbilical vein endothelial cells has been shown to be present in serum-free medium conditioned by the prior growth of a cell line (1PT) derived from a poorly differentiated bronchial carcinoma. Preliminary characterization of this factor has revealed that it is a heat-labile, acid-stable proteinaceous material, the activity of which is not diminished by treatment with a reducing agent. In its partially purified state it has been shown to be anionic and to be associated with material exhibiting a broad molecular weight range of 35 X 10(3) to 100 X 10(3). It does not bind strongly to heparin-Sepharose and its mitogenic effect on endothelial cells is not potentiated by heparin. These properties suggest that this factor may differ from other previously described tumour-derived endothelial mitogens.

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