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Berry Fruits Modulated Endothelial Cell Migration and Angiogenesis via Phosphoinositide-3 Kinase/Protein Kinase B Pathway In Vitro in Endothelial Cells.

07:23 EDT 21st May 2013 | BioPortfolio

Summary of "Berry Fruits Modulated Endothelial Cell Migration and Angiogenesis via Phosphoinositide-3 Kinase/Protein Kinase B Pathway In Vitro in Endothelial Cells."

Polyphenolic-rich berry fruits are known to activate redox sensitive cellular signaling molecules such as phosphatidylinositol-3-kinase (PI-3-kinase)/kinase B (Akt) resulting in a cascade of downstream signaling pathways. We investigated the ability of strawberry (SB), wild blueberry (WBB), and cranberry (CB) extracts to induce the activation of PI3-kinase/Akt signaling in vitro in human umbilical endothelial cells (HUVECs) and whether this activation would enhance cell migration and angiogenesis. Anthocyanin profiles of the extracts were characterized and quantified using HPLC-ESI/MS. Antioxidant capacity and ascorbic acid content were determined using oxygen radical absorbance capacity assay and HPLC, respectively. Akt activation, cell migration, and angiogenesis were investigated using Alpha Screen SureFire, scratch, and capillary-like tube formation assays, respectively. The total anthocyanin contents of SB, WBB, and CB extracts were 81.7, 82.5, and 83.0 mg/100 g fresh weight, respectively. SB, WBB, and CB extracts activated Akt in a dose-dependent manner via PI-3 kinase, and enhanced cell migration and angiogenesis at physiologically relevance concentrations in vitro in HUVECs. The results from this study suggest that polyphenolics in berry fruits may play a role in promoting vascular health.

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Journal Details

This article was published in the following journal.

Name: Journal of agricultural and food chemistry
ISSN: 1520-5118
Pages:

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Medical and Biotech [MESH] Definitions

Integrin Alphavbeta3

An integrin that binds to a variety of plasma and extracellular matrix proteins containing the conserved RGD amino acid sequence and modulates cell adhesion. Integrin alphavbeta3 is highly expressed in OSTEOCLASTS where it may play role in BONE RESORPTION. It is also abundant in vascular smooth muscle and endothelial cells, and in some tumor cells, where it is involved in angiogenesis and cell migration. Although often referred to as the vitronectin receptor there is more than one receptor for vitronectin (RECEPTORS, VITRONECTIN).

Vascular Endothelial Growth Factor A

The original member of the family of endothelial cell growth factors referred to as VASCULAR ENDOTHELIAL GROWTH FACTORS. Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as "tumor angiogenesis factor" and "vascular permeability factor". Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth and vascular permeability it may play a role in stimulating VASODILATION via NITRIC OXIDE-dependent pathways. Alternative splicing of the mRNA for vascular endothelial growth factor A results in several isoforms of the protein being produced.

Cell Migration Inhibition

Phenomenon of cell-mediated immunity measured by in vitro inhibition of the migration or phagocytosis of antigen-stimulated LEUKOCYTES or MACROPHAGES. Specific CELL MIGRATION ASSAYS have been developed to estimate levels of migration inhibitory factors, immune reactivity against tumor-associated antigens, and immunosuppressive effects of infectious microorganisms.

Tumor Necrosis Factor Ligand Superfamily Member 15

A member of tumor necrosis factor superfamily found on ENDOTHELIAL CELLS that plays a role in the inhibition of endothelial cell growth and PHYSIOLOGIC ANGIOGENESIS.

Integrin Alpha1beta1

Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.

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