Cowpea (Vigna unguiculata) Extract Reduce Malondialdehyde Levels and Prevent Aortic Endothelial Cell Decline in Ovariectomized Rats

Estrogen has anti-oxidative and anti-inflammatory properties, but its levels decrease in postmenopausal women who can trigger oxidative stress. One of the most damaging effects of ROS is lipid peroxidation, and the end product is Malondialdehyde (MDA). Similarly, aging endothelium has increased oxidative stress and endothelial cell sensitivity to apoptosis. This study aimed to determine the effect of cowpea extract on serum MDA levels, aortic endothelial cell counts, and brain MDA levels in the ovariectomy model. Cowpea extract can be used as an alternative to prevent and overcome the effects that occur during menopause, such as cardiovascular problems, decreased bone mineral density, and dementia. The study used 15-month-old female Rattus norvegicus, divided into six groups (OVX, SHAM, OVX+estradiol, OVX+Vu 1.25; 2.5; and 5 mg/kg BW/day). Serum and brain MDA levels were examined by ELISA method, while the number of aortic endothelial cells were examined on histopathological preparations with Hematoxylin & Eosin (HE) staining. The mean value of serum and brain MDA levels decreased with an increase in the dose given (p-value 0.016). The mean value of aortic endothelial cells between the dose groups did not significantly differ. However, the mean value showed an increasing trend as the dose of cowpea extract was given. The results of this study indicate that the extract of cowpea has the potential as an antioxidant to reduce serum and brain MDA levels, prevent a decrease in the number of aortic endothelial cells. As prevention, cowpea extract can be used as an antioxidant and consumed since premenopause to minimize problems that occur during postmenopause.

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Differential effects of laminin, intact type IV collagen, and specific domains of type IV collagen on endothelial cell adhesion and migration.

The Journal of Cell Biology ◽

10.1083/jcb.106.4.1365 ◽

1988 ◽

Vol 106 (4) ◽

pp. 1365-1373 ◽

Cited By ~ 143

Author(s):

T J Herbst ◽

J B McCarthy ◽

E C Tsilibary ◽

L T Furcht

Keyword(s):

Endothelial Cells ◽

Cell Adhesion ◽

Endothelial Cell ◽

Type Iv Collagen ◽

Aortic Endothelial Cells ◽

Aortic Endothelial Cell ◽

Type Iv ◽

And Migration ◽

Endothelial Cell Adhesion ◽

Aortic Endothelial

Laminin and type IV collagen were compared for the ability to promote aortic endothelial cell adhesion and directed migration in vitro. Substratum-adsorbed IV promoted aortic endothelial cell adhesion in a concentration dependent fashion attaining a maximum level 141-fold greater than controls within 30 min. Aortic endothelial cell adhesion to type IV collagen was not inhibited by high levels (10(-3) M) of arginyl-glycyl-aspartyl-serine. In contrast, adhesion of aortic endothelial cells on laminin was slower, attaining only 53% of the adhesion observed on type IV collagen by 90 min. Type IV collagen when added to the lower well of a Boyden chamber stimulated the directional migration of aortic endothelial cells in a concentration dependent manner with a maximal response 6.9-fold over control levels, whereas aortic endothelial cells did not migrate in response to laminin at any concentration (.01-2.0 X 10(-7) M). Triple helix-rich fragments of type IV collagen were nearly as active as intact type IV collagen in stimulating both adhesion and migration whereas the carboxy terminal globular domain was less active at promoting adhesion (36% of the adhesion promoted by intact type IV collagen) or migration. Importantly, aortic endothelial cells also migrate to substratum adsorbed gradients of type IV collagen suggesting that the mechanism of migration is haptotactic in nature. These results demonstrate that the aortic endothelial cell adhesion and migration is preferentially promoted by type IV collagen compared with laminin, and has a complex molecular basis which may be important in angiogenesis and large vessel repair.

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Effects of indomethacin on the oxidative stress induced by 1-chloro-2,4-dinitrobenzene in cultured bovine aortic endothelial cells.

The Japanese Journal of Pharmacology ◽

10.1016/s0021-5198(19)36765-4 ◽

1996 ◽

Vol 71 ◽

pp. 131

Author(s):

Masakazu Ishii ◽

Masako Yasuda ◽

Toshinori Yamamoto ◽

Yukio Kuroiwa

Keyword(s):

Oxidative Stress ◽

Endothelial Cells ◽

Aortic Endothelial Cells ◽

Bovine Aortic Endothelial Cells ◽

Aortic Endothelial

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Molecular characterization of the Na-K-Cl cotransporter of bovine aortic endothelial cells

AJP Cell Physiology ◽

10.1152/ajpcell.1997.273.1.c188 ◽

1997 ◽

Vol 273 (1) ◽

pp. C188-C197 ◽

Cited By ~ 43

Author(s):

T. R. Yerby ◽

C. R. Vibat ◽

D. Sun ◽

J. A. Payne ◽

M. E. O'Donnell

Keyword(s):

Endothelial Cells ◽

Endothelial Cell ◽

Amino Acid ◽

Blot Analysis ◽

Cdna Probe ◽

Bovine Aortic Endothelial Cell ◽

Coding Region ◽

Cerebral Microvessels ◽

Aortic Endothelial Cells ◽

Aortic Endothelial

The Na-K-Cl cotransporter is an important regulator of endothelial cell volume and may also contribute to flux of Na and Cl across the endothelium of the blood-brain barrier. To date, two Na-K-Cl cotransport isoforms have been identified, the cotransporter in secretory epithelia, NKCC1, and that in absorptive renal epithelia, NKCC2. Our previous studies showed that a monoclonal antibody to the cotransporter of human colonic T84 epithelial cells, an NKCC1 isoform, recognizes a 170-kDa glycoprotein from endothelial cells. The molecular identity of the Na-K-Cl cotransporter present in endothelial cells, however, has been unknown. In addition, although evidence has been provided that phosphorylation of the endothelial cotransporter plays a role in regulating its activity, little is known about potential sites for protein kinase interaction with the cotransporter. The present study was conducted to determine the molecular structure of the endothelial Na-K-Cl cotransporter. Using a 1.0-kilobase (kb) cDNA fragment from a conserved region of the T84 cell cotransporter, we screened a bovine aortic endothelial cell cDNA library and subsequently identified and sequenced two overlapping clones that together spanned the entire coding region. The endothelial cotransporter is a 1,201-amino acid protein with 12 putative transmembrane segments and large amino and carboxy termini, each containing several consensus sites for phosphorylation by protein kinases. Comparison of the endothelial cotransporter amino acid sequence with known NKCC1 and NKCC2 sequences revealed a 96% identity with NKCC1. Northern blot analysis using a cDNA probe from the endothelial cotransporter revealed high expression of approximately 7.5-kb transcripts in a number of bovine tissues. Finally, a prominent expression of Na-K-Cl cotransporter was found by Western blot analysis in both cultured and freshly isolated endothelial cells of bovine aorta and cerebral microvessels.

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