Compounds > valyl-prolyl-glycyl-valyl-glycine

valyl-prolyl-glycyl-valyl-glycine and valyl-glycyl-valyl-alanyl-prolyl-glycine

valyl-prolyl-glycyl-valyl-glycine has been researched along with valyl-glycyl-valyl-alanyl-prolyl-glycine* in 1 studies

Other Studies

1 other study(ies) available for valyl-prolyl-glycyl-valyl-glycine and valyl-glycyl-valyl-alanyl-prolyl-glycine

Article	Year
Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VPGVG in cultured chick vascular smooth muscle cells. FEBS letters, 1995, Jul-17, Volume: 368, Issue:2 Synthetic elastin peptides, VPGVG or its polymer (VPGVG)n, enhanced the proliferation of smooth muscle cells 1.5-fold during 48 h treatment at the concentrations over 10(-6) M or 1.0 microgram/ml, respectively. Monomeric and polymeric VPGVG sequences reduced elastin synthesis and its mRNA level to one-third and one-half of control respectively under the conditions in which the proliferation of cells were enhanced, but did not change collagen synthesis as measured by bacterial collagenase digestion. The elastin-specific autoregulation by elastin fragments may reflect the feedback regulation of elastin expression which may play an essential role in elastin metabolism under the normal and diseased conditions. Topics: Amino Acid Sequence; Animals; Cell Division; Cells, Cultured; Chickens; Collagen; Elastin; Homeostasis; Molecular Sequence Data; Muscle, Smooth, Vascular; Oligopeptides; RNA, Messenger	1995

Article

Year

Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VPGVG in cultured chick vascular smooth muscle cells.

FEBS letters, 1995, Jul-17, Volume: 368, Issue:2

Synthetic elastin peptides, VPGVG or its polymer (VPGVG)n, enhanced the proliferation of smooth muscle cells 1.5-fold during 48 h treatment at the concentrations over 10(-6) M or 1.0 microgram/ml, respectively. Monomeric and polymeric VPGVG sequences reduced elastin synthesis and its mRNA level to one-third and one-half of control respectively under the conditions in which the proliferation of cells were enhanced, but did not change collagen synthesis as measured by bacterial collagenase digestion. The elastin-specific autoregulation by elastin fragments may reflect the feedback regulation of elastin expression which may play an essential role in elastin metabolism under the normal and diseased conditions.

Topics: Amino Acid Sequence; Animals; Cell Division; Cells, Cultured; Chickens; Collagen; Elastin; Homeostasis; Molecular Sequence Data; Muscle, Smooth, Vascular; Oligopeptides; RNA, Messenger

1995