Lead-induced alteration of heparan sulfate proteoglycans in cultured vascular endothelial cells

We investigated the alterations of heparan sulfate proteoglycans produced by vascular endothelial cells after exposure to lead. Bovine aortic endothelial cells were cultured and metabolically labeled with [ 3H]glucosamine and [ 35S]sulfate in the presence of lead chloride at 10 μM. Radiolabeled HSPG...

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Veröffentlicht in:Toxicology (Amsterdam) 1997-03, Vol.118 (1), p.1-10
Hauptverfasser: Kaji, Toshiyuki, Ohkawara, Susumu, Nakajima, Mie, Yamamoto, Chika, Fujiwara, Yasuyuki, Miyajima, Sawako, Koizumi, Fumitomo
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container_issue 1
container_start_page 1
container_title Toxicology (Amsterdam)
container_volume 118
creator Kaji, Toshiyuki
Ohkawara, Susumu
Nakajima, Mie
Yamamoto, Chika
Fujiwara, Yasuyuki
Miyajima, Sawako
Koizumi, Fumitomo
description We investigated the alterations of heparan sulfate proteoglycans produced by vascular endothelial cells after exposure to lead. Bovine aortic endothelial cells were cultured and metabolically labeled with [ 3H]glucosamine and [ 35S]sulfate in the presence of lead chloride at 10 μM. Radiolabeled HSPGs were separated by ion-exchange chromatography and either their hydrodynamic size or the length of heparan sulfate chains were characterized by gel filtration. It was found that lead markedly suppresses the incorporation of the radioactive precursors into HSPGs in the cell layer; the incorporation into chondroitin/dermatan sulfate proteoglycans was decreased by the metal only slightly. The suppression by lead occurred in the low molecular weight subclass of HSPGs rather than the high molecular weight subclass. However, the length of heparan sulfate chains was not changed by the metal. A sodium dodecyl sulfate-polyacrylamide gel electrophoresis of [ 35S]methionine-labeled proteoglycans after heparitinase digestion showed that there were slightly more HSPG core proteins without a change of the size in lead-treated cell layer. It was, therefore, suggested that vascular endothelial cell layer after exposure to lead has more HSPG core proteins with fewer heparan sulfate chains without a change in length.
doi_str_mv 10.1016/S0300-483X(96)03582-2
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A sodium dodecyl sulfate-polyacrylamide gel electrophoresis of [ 35S]methionine-labeled proteoglycans after heparitinase digestion showed that there were slightly more HSPG core proteins without a change of the size in lead-treated cell layer. It was, therefore, suggested that vascular endothelial cell layer after exposure to lead has more HSPG core proteins with fewer heparan sulfate chains without a change in length.</abstract><cop>Shannon</cop><cop>Amsterdam</cop><pub>Elsevier Ireland Ltd</pub><pmid>9074649</pmid><doi>10.1016/S0300-483X(96)03582-2</doi><tpages>10</tpages></addata></record>
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subjects Animals
Aorta
Biological and medical sciences
Cattle
Cells, Cultured
Chemical and industrial products toxicology. Toxic occupational diseases
Chromatography, DEAE-Cellulose
Chromatography, Gel
Culture Media, Conditioned
Electrophoresis, Polyacrylamide Gel
Endothelial cells
Endothelium, Vascular - chemistry
Endothelium, Vascular - cytology
Endothelium, Vascular - drug effects
Glucosamine - analysis
Glucosamine - metabolism
Glycoproteins - analysis
Glycosaminoglycans - metabolism
Heparan sulfate
Heparan Sulfate Proteoglycans
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Hyaluronic Acid - analysis
Lead
Lead - toxicity
Medical sciences
Metals and various inorganic compounds
Molecular Weight
Papain - metabolism
Polysaccharide-Lyases - metabolism
Proteoglycan
Proteoglycans - chemistry
Proteoglycans - metabolism
Sulfates - analysis
Sulfates - metabolism
Toxicology
Vascular
title Lead-induced alteration of heparan sulfate proteoglycans in cultured vascular endothelial cells
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