Internalization and degradation of heparin is not required for stimulus of heparan sulfate proteoglycan synthesis
Identifieur interne : 001990 ( Main/Exploration ); précédent : 001989; suivant : 001991Internalization and degradation of heparin is not required for stimulus of heparan sulfate proteoglycan synthesis
Auteurs : Edvaldo S. Trindade [Brésil] ; Rodrigo I. Bouças [Brésil] ; Hugo A. O. Rocha [Brésil] ; Juliana A. Dominato [Brésil] ; Edgar J. Paredes-Gamero [Brésil] ; Célia Regina C. Franco [Brésil] ; Constance Oliver [Brésil] ; Maria C. Jamur [Brésil] ; Carl P. Dietrich [Brésil] ; Helena B. Nader [Brésil]Source :
- Journal of Cellular Physiology [ 0021-9541 ] ; 2008-11.
English descriptors
- Teeft :
- Alexa fluor, Alexahep, Anticoagulant, Antithrombotic, Assay, Biol, Biothep, Buonassisi, Cacodylate buffer, Cell surface, Chloroquine, Colburn, Contract grant sponsor, Degradation, Endothelial, Endothelial cells, Extracellular matrix, Fresh medium, Glycosaminoglycans, Heparan, Heparan sulfate, Heparan sulfate proteoglycans, Heparin, Heparin degradation, Hiebert, Hspg, Hspg synthesis, Internalization, Lysosomal, Lysosomal markers, Lysosome, Lysotracker, Nader, Online issue, Pinhal, Proteoglycan, Proteoglycans, Rocha, Streptavidin, Sulfate, Sulfated, Sulfated glycosaminoglycans, Thromb, Thrombosis, Transmission electron microscopy, Vesicle.
Abstract
In vitro, heparin and antithrombotic drugs specifically stimulate the synthesis of an antithrombotic heparan sulfate proteoglycan (HSPG) produced by endothelial cells. The putative heparin binding site(s) that may be related to this phenomenon were investigated. In the preceding article, using various heparin probes, it was shown that the heparin does not bind to the endothelial cell surface, but only to the extracellular matrix. The present study demonstrated that, when the cells were exposed to heparin at 37°C, the heparin was internalized and with time was localized in lysosomes. However, endocytosis of heparin was not required for the stimulation of HSPG synthesis. The requirement for heparin degradation in the stimulus of HSPG synthesis was also investigated. When the cells were incubated with chloroquine, a lysosomotropic amine that raises the lysosomal pH thus inhibiting enzymatic degradation of internalized compounds, stimulation of HSPG synthesis was still observed. These combined results indicate that neither internalization nor degradation of heparin is required for stimulation of HSPG synthesis, and suggests that its binding to the extracellular matrix could be responsible for this effect. J. Cell. Physiol. 217: 360–366, 2008. © 2008 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jcp.21510
Affiliations:
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Le document en format XML
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Nader</name><affiliation wicri:level="2"><country xml:lang="fr">Brésil</country><wicri:regionArea>Departamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Brésil</country></affiliation><affiliation wicri:level="2"><country xml:lang="fr">Brésil</country><wicri:regionArea>Correspondence address: Departamento de Bioquímica, Escola Paulista de Medicina, Universidade Federal de São Paulo, Rua 3 de Maio, 100‐CEP 04044‐020, São Paulo, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">217</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="360">360</biblScope><biblScope unit="page" to="366">366</biblScope><biblScope unit="page-count">7</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2008-11">2008-11</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Alexa fluor</term><term>Alexahep</term><term>Anticoagulant</term><term>Antithrombotic</term><term>Assay</term><term>Biol</term><term>Biothep</term><term>Buonassisi</term><term>Cacodylate buffer</term><term>Cell surface</term><term>Chloroquine</term><term>Colburn</term><term>Contract grant sponsor</term><term>Degradation</term><term>Endothelial</term><term>Endothelial cells</term><term>Extracellular matrix</term><term>Fresh medium</term><term>Glycosaminoglycans</term><term>Heparan</term><term>Heparan sulfate</term><term>Heparan sulfate proteoglycans</term><term>Heparin</term><term>Heparin degradation</term><term>Hiebert</term><term>Hspg</term><term>Hspg synthesis</term><term>Internalization</term><term>Lysosomal</term><term>Lysosomal markers</term><term>Lysosome</term><term>Lysotracker</term><term>Nader</term><term>Online issue</term><term>Pinhal</term><term>Proteoglycan</term><term>Proteoglycans</term><term>Rocha</term><term>Streptavidin</term><term>Sulfate</term><term>Sulfated</term><term>Sulfated glycosaminoglycans</term><term>Thromb</term><term>Thrombosis</term><term>Transmission electron microscopy</term><term>Vesicle</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In vitro, heparin and antithrombotic drugs specifically stimulate the synthesis of an antithrombotic heparan sulfate proteoglycan (HSPG) produced by endothelial cells. The putative heparin binding site(s) that may be related to this phenomenon were investigated. In the preceding article, using various heparin probes, it was shown that the heparin does not bind to the endothelial cell surface, but only to the extracellular matrix. The present study demonstrated that, when the cells were exposed to heparin at 37°C, the heparin was internalized and with time was localized in lysosomes. However, endocytosis of heparin was not required for the stimulation of HSPG synthesis. The requirement for heparin degradation in the stimulus of HSPG synthesis was also investigated. When the cells were incubated with chloroquine, a lysosomotropic amine that raises the lysosomal pH thus inhibiting enzymatic degradation of internalized compounds, stimulation of HSPG synthesis was still observed. These combined results indicate that neither internalization nor degradation of heparin is required for stimulation of HSPG synthesis, and suggests that its binding to the extracellular matrix could be responsible for this effect. J. Cell. Physiol. 217: 360–366, 2008. © 2008 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>Brésil</li></country><region><li>Paraná (État)</li><li>Rio Grande do Norte</li><li>État de São Paulo</li></region></list><tree><country name="Brésil"><region name="État de São Paulo"><name sortKey="Trindade, Edvaldo S" sort="Trindade, Edvaldo S" uniqKey="Trindade E" first="Edvaldo S." last="Trindade">Edvaldo S. Trindade</name></region><name sortKey="Boucas, Rodrigo I" sort="Boucas, Rodrigo I" uniqKey="Boucas R" first="Rodrigo I." last="Bouças">Rodrigo I. Bouças</name><name sortKey="Dietrich, Carl P" sort="Dietrich, Carl P" uniqKey="Dietrich C" first="Carl P." last="Dietrich">Carl P. Dietrich</name><name sortKey="Dominato, Juliana A" sort="Dominato, Juliana A" uniqKey="Dominato J" first="Juliana A." last="Dominato">Juliana A. Dominato</name><name sortKey="Franco, Celia Regina C" sort="Franco, Celia Regina C" uniqKey="Franco C" first="Célia Regina C." last="Franco">Célia Regina C. Franco</name><name sortKey="Jamur, Maria C" sort="Jamur, Maria C" uniqKey="Jamur M" first="Maria C." last="Jamur">Maria C. Jamur</name><name sortKey="Nader, Helena B" sort="Nader, Helena B" uniqKey="Nader H" first="Helena B." last="Nader">Helena B. Nader</name><name sortKey="Nader, Helena B" sort="Nader, Helena B" uniqKey="Nader H" first="Helena B." last="Nader">Helena B. Nader</name><name sortKey="Nader, Helena B" sort="Nader, Helena B" uniqKey="Nader H" first="Helena B." last="Nader">Helena B. Nader</name><name sortKey="Oliver, Constance" sort="Oliver, Constance" uniqKey="Oliver C" first="Constance" last="Oliver">Constance Oliver</name><name sortKey="Paredes Amero, Edgar J" sort="Paredes Amero, Edgar J" uniqKey="Paredes Amero E" first="Edgar J." last="Paredes-Gamero">Edgar J. Paredes-Gamero</name><name sortKey="Rocha, Hugo A O" sort="Rocha, Hugo A O" uniqKey="Rocha H" first="Hugo A. O." last="Rocha">Hugo A. O. Rocha</name><name sortKey="Trindade, Edvaldo S" sort="Trindade, Edvaldo S" uniqKey="Trindade E" first="Edvaldo S." last="Trindade">Edvaldo S. Trindade</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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