Role of glycosaminoglycan and fibronectin in endothelial cell growth

Sato, Tadahiro; Arai, Katsuyuki; Ishiharajima, Shigehiko; Asano, Gorō

doi:10.1016/0014-4800(87)90075-x

Cited by 8 publications

(2 citation statements)

References 15 publications

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“…The cell function of endothelium is complex and includes secretion of vasorelaxing and constricting factors, such as prostacyclin, endothelial-derived relaxing factor (EDRF), endothelial-derived hyperpolarizing factor (EDHF), endothelial-derived contracting factor (EDCF), or endothelin (8,9), coagulation factors such as factor VIII antigen, von Willebrand's factor, and plasminogen activator, matrix factors including collagen, glycosaminoglycans, fibronectin (10), and metalloproteinases, as well as secretion of heparane and growth factors that regulate smooth muscle cell proliferation (11). Endothelial cells are also well characterized for their production of NO, which is the predominant form of EDRF (8), and are well known for their ability to metabolize plasma lipids, nucleotides, serotonine, catecholamines, bradykinin, and angiotensin-1 (12).…”

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confidence: 99%

Cellular dedifferentiation of endothelium is linked to activation and silencing of certain nuclear transcription factors: implications for endothelial dysfunction and vascular biology

2000

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We investigated the gene expression of the nuclear transcription factors c/EBPalpha, GATA-2, and the silencer Oct-1 in conjunction with the gene expression of all major cytochrome P450 genes and of eNOS in cultures of endothelial cells of the rat. The purity of cultured endothelial cells was also confirmed by flow cytometry measurements of PECAM-1, a surface antigen of endothelial cells. Taken collectively, the gene expression and flow cytometry studies provide strong evidence for c/EBPalpha, GATA-2, and Oct-1 to play a key role in the cellular dedifferentiation of endothelial cells; gene expression of eight individual CYP genes in conjunction with protein activity could be significantly increased upon treatment with Aroclor 1254, a well-documented chemical inducer of a battery of genes. Nevertheless, the gene expression of c/EBPalpha, GATA-2, and most of the CYP genes was dramatically reduced (up to 90%) in cell cultures lacking PECAM-1 expression; in strong contrast, expression of the silencer Oct-1 was massively increased (approximately 14-fold). We thus conclude activation of the silencer Oct-1 to be strongly correlated with loss of PECAM-1 and eNOS gene expression, e.g., loss of cellular differentiation and endothelial function; in conjunction, gene expression of all major P450 isoforms was dramatically reduced in cultures of dedifferentiated endothelial cells. This process of cellular dedifferentiation and endothelial dysfunction was accompanied by down-regulation of endothelial specific transcription factors.

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confidence: 99%

Cellular dedifferentiation of endothelium is linked to activation and silencing of certain nuclear transcription factors: implications for endothelial dysfunction and vascular biology

2000

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“…In spite of the high adsorption of these proteins, endothelial cells adhere and spread well on TCPS [3,10]. Moreover, endothelial celt-derived fibronectin is deposited in relatively large amounts on to TCPS during adhesion and spreading [11,12]. Proteins generally adsorb to surfaces as a monolayer of molecules, but do not adsorb to already adsorbed protein molecules [13,14].…”

confidence: 99%

Deposition of cellular fibronectin and desorption of human serum albumin during adhesion and spreading of human endothelial cells on polymers

Dekker

Beugeling

Wind

et al. 1991

J Mater Sci: Mater Med

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More insight into the mechanism of adhesion of human endothelial cells (HEC) on to polymeric surfaces may lead to the development of improved small-diameter vascular grafts. H EC suspended in 20% human serum-containing culture medium adhere and spread well on moderately water-wettable polymers such as tissue culture polystyrene (TCPS). Earlier it was demonstrated that during adhesion and spreading of HEC on TCPS, cellular fibronectin is deposited on to this surface. It was postulated that fibronectin deposition is accompanied by desorption of adsorbed serum proteins, e.g. human serum albumin (HSA). The amounts of adsorbed (cellular) fibronectin and HSA on TCPS surfaces pretreated for 1 h with solutions of human serum (ranging from 0.01%-20%), were determined after incubation of these surfaces for 6 h with HEC in culture medium and after incubation with culture medium without cells. Protein adsorption was determined by means of a two-step enzyme-immunoassay (EIA). HEC adhesion and spreading on TCPS resulted in a significant deposition of fibronectin irrespective of the serum concentration in the solution used for the pretreatment of TCPS. The deposition of cellular fibronectin on to TCPS, pretreated with human serum, was accompanied by displacement of adsorbed HSA. Desorption of HSA from TCPS was only detectable with the EIA at serum concentrations ranging from 0.01%-1%. Using l~l-I-labelled HSA as tracer protein; it could, however, be demonstrated that HSA was also displaced from TCPS, pretreated with solutions of higher serum concentrations. Pretreatment of the hydrophobic vascular graft material PET (poly(ethylene terephthalate); Dacron) and of FEP (fluoroethylenepropylene copotymer; a Teflon-like polymer) with a solution containing 20% human serum resulted in a reduced adhesion of HEC compared to uncoated surfaces. We suggest that this may be caused by a poor displacement of adsorbed serum proteins from these hydrophobic surfaces by cellular fibronectin. This may explain why HEC normally fail to adhere on to prosthetic surfaces.

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