Upregulation of S100 calcium-binding protein A9 is required for induction of smooth muscle cell proliferation by a periodontal pathogen

A heparin-binding protein was isolated from bovine uteri and purified to homogeneity. This protein appears as a double band of approx. 78 kDa in SDS/polyacrylamide-gel electrophoresis and has an isoelectric point of 5.2. The binding of heparin to this protein is saturable. No other glycosaminoglycan from mammalian tissue, such as hyaluronic acid, chondroitin sulphate, dermatan sulphate or keratan sulphate, binds to the 78 kDa protein. Dextran sulphate binds in a non-saturable fashion. Certain heparan sulphate polysaccharide structures are required for binding to the 78 kDa protein. Some proteoheparan sulphates, such as endothelial cell-surface proteoheparan sulphate, show only weak interaction with the 78 kDa protein in contrast with a basement-membrane proteoheparan sulphate from HR-9 cells. Antibodies against the 78 kDa protein inhibit binding of proteoheparan [35S]sulphate from basement membranes to smooth-muscle cells. Conventional antibodies, Fab fragments and some monoclonal antibodies, inhibit smooth-muscle cell proliferation in a similar range as that observed for heparin. The protein was detected in a variety of tissues and cells but not in blood cells. A possible role of this protein as a receptor for heparin or heparan sulphate and its function in the control of the arterial wall structure are discussed.

Download Full-text

GW24-e2996 Involvement of retinol binding protein 4 in insulin-induced vascular smooth muscle cell proliferation

Heart ◽

10.1136/heartjnl-2013-304613.67 ◽

2013 ◽

Vol 99 (Suppl 3) ◽

pp. A26.3-A27

Author(s):

Li Fei ◽

Tianlun Yang

Keyword(s):

Cell Proliferation ◽

Smooth Muscle ◽

Vascular Smooth Muscle ◽

Smooth Muscle Cell ◽

Muscle Cell ◽

Vascular Smooth Muscle Cell ◽

Binding Protein ◽

Smooth Muscle Cell Proliferation ◽

Retinol Binding Protein ◽

Retinol Binding Protein 4

Download Full-text

Novel insight into Y-box binding protein 1 in the regulation of vascular smooth muscle cell proliferation through targeting GC box-dependent genes

FEBS Letters ◽

10.1016/j.febslet.2013.02.047 ◽

2013 ◽

Vol 587 (9) ◽

pp. 1326-1332 ◽

Cited By ~ 13

Author(s):

Jian-hong Shi ◽

Bin Zheng ◽

Yong-hui Li ◽

Yan Sun ◽

Ai-li Han ◽

...

Keyword(s):

Cell Proliferation ◽

Smooth Muscle ◽

Vascular Smooth Muscle ◽

Smooth Muscle Cell ◽

Muscle Cell ◽

Vascular Smooth Muscle Cell ◽

Binding Protein ◽

Smooth Muscle Cell Proliferation ◽

Gc Box ◽

Insight Into

Download Full-text

Involvement of Cyclooxygenase- and Lipoxygenase-Mediated Conversion of Arachidonic Acid in Controlling Human Vascular Smooth Muscle Cell Proliferation

Thrombosis and Haemostasis ◽

10.1055/s-0038-1645212 ◽

1990 ◽

Vol 63 (02) ◽

pp. 291-297 ◽

Cited By ~ 28

Author(s):

Herm-Jan M Brinkman ◽

Marijke F van Buul-Worteiboer ◽

Jan A van Mourik

Keyword(s):

Cell Proliferation ◽

Arachidonic Acid ◽

Smooth Muscle ◽

Vascular Smooth Muscle ◽

Smooth Muscle Cells ◽

Smooth Muscle Cell ◽

Muscle Cell ◽

Vascular Smooth Muscle Cell ◽

Muscle Cells ◽

Smooth Muscle Cell Proliferation

SummaryWe observed that the growth of human umbilical arterysmooth muscle cells was inhibited by the phospholipase A2 inhibitors p-bromophenacylbromide and mepacrine. Thesefindings suggest that fatty acid metabolism might be integrated in the control mechanism of vascular smooth muscle cell proliferation. To identify eicosanoids possibly involved in this process, we studied both the metabolism of arachidonic acid of these cells in more detail and the effect of certain arachidonic acid metabolites on smooth muscle cells growth. We found no evidence for the conversion of arachidonic acid via the lipoxygenase pathway. In contrast, arachidonic acid was rapidly converted via the cyclooxy-genase pathway. The following metabolites were identified: prostaglandin E2 (PGE2), 6-keto-prostaglandin F1α (6-k-PGF1α), prostaglandin F2α (PGF2α), 12-hydroxyheptadecatrienoic acid (12-HHT) and 11-hydroxyeicosatetetraenoic acid (11-HETE). PGE2 was the major metabolite detected. Arachidonic acid metabolites were only found in the culture medium, not in the cell. After synthesis, 11-HETE was cleared from the culture medium. We have previously reported that PGE2 inhibits the serum-induced [3H]-thymidine incorporation of growth-arrested human umbilical artery smooth muscle cells. Here we show that also 11-HETEexerts this inhibitory property. Thus, our data suggeststhat human umbilical artery smooth muscle cells convert arachidonic acid only via the cyclooxygenase pathway. Certain metabolites produced by this pathway, including PGE2 and 11-HETE, may inhibit vascular smooth muscle cell proliferation.

Download Full-text