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Article: Purification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytes

TitlePurification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytes
Authors
Issue Date1998
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
Citation
Journal Of Cellular Biochemistry, 1998, v. 69 n. 4, p. 414-424 How to Cite?
AbstractThe aim of this study was to purify, characterize, and study the regulation at the chondrocyte level of the guinea pig (gp) homologue of human (R) YKL40, a putative marker of arthritic disorders. Studying YKL40 in guinea pigs is of particular interest, as age-related osteoarthritis develops in this species spontaneously. Both N-terminal sequencing and total amino acid composition of gpYKL40 purified from the secretion medium of cultured articular chondrocytes indicate a high degree of identity with hYKL40. gpYKL40 was found to contain complex N-linked carbohydrate, as demonstrated by N-glycosidase F and endoglycosidase F digestion. Isoelectric focusing demonstrated the presence of a major band at pI 6.7. The secretion of gpYKL40 by confluent articular chondrocytes in the extracellular medium was studied by immunoblotting. gpYKL40 was released by chondrocytes continuously over a 7 day period and did not appear to be degraded by proteinases, as its signal intensity in cell-free medium at 37°C did not decrease with time. Thus, gpYKL40 displays high stability and accumulates in extracellular medium without reaching a steady-state level. Among the main factors known to regulate cartilage metabolism, IL-1β, TNF-α, bFGF, or 1,25(OH)2D3 did not alter the basal level of gpYKL40, and retinoic acid had a slight inhibitory effect; TGF-β and IGF-I and -II dose-dependently and inversely modulated this basal level. TGF-β at 5 ng/ml decreased extracellular gpYKL40 2.9- fold, whereas IGF-I and IGF-II at 50 ng/ml increased extracellular gpYKL40 3.6- and 3.4-fold, respectively. The present biochemical and biological findings give new insights for studying the function of YKL40 in cartilage.
Persistent Identifierhttp://hdl.handle.net/10722/171209
ISSN
2015 Impact Factor: 3.446
2015 SCImago Journal Rankings: 1.520
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDe Ceuninck, Fen_US
dc.contributor.authorPastoureau, Pen_US
dc.contributor.authorBouet, Fen_US
dc.contributor.authorBonnet, Jen_US
dc.contributor.authorVanhoutte, PMen_US
dc.date.accessioned2012-10-30T06:12:42Z-
dc.date.available2012-10-30T06:12:42Z-
dc.date.issued1998en_US
dc.identifier.citationJournal Of Cellular Biochemistry, 1998, v. 69 n. 4, p. 414-424en_US
dc.identifier.issn0730-2312en_US
dc.identifier.urihttp://hdl.handle.net/10722/171209-
dc.description.abstractThe aim of this study was to purify, characterize, and study the regulation at the chondrocyte level of the guinea pig (gp) homologue of human (R) YKL40, a putative marker of arthritic disorders. Studying YKL40 in guinea pigs is of particular interest, as age-related osteoarthritis develops in this species spontaneously. Both N-terminal sequencing and total amino acid composition of gpYKL40 purified from the secretion medium of cultured articular chondrocytes indicate a high degree of identity with hYKL40. gpYKL40 was found to contain complex N-linked carbohydrate, as demonstrated by N-glycosidase F and endoglycosidase F digestion. Isoelectric focusing demonstrated the presence of a major band at pI 6.7. The secretion of gpYKL40 by confluent articular chondrocytes in the extracellular medium was studied by immunoblotting. gpYKL40 was released by chondrocytes continuously over a 7 day period and did not appear to be degraded by proteinases, as its signal intensity in cell-free medium at 37°C did not decrease with time. Thus, gpYKL40 displays high stability and accumulates in extracellular medium without reaching a steady-state level. Among the main factors known to regulate cartilage metabolism, IL-1β, TNF-α, bFGF, or 1,25(OH)2D3 did not alter the basal level of gpYKL40, and retinoic acid had a slight inhibitory effect; TGF-β and IGF-I and -II dose-dependently and inversely modulated this basal level. TGF-β at 5 ng/ml decreased extracellular gpYKL40 2.9- fold, whereas IGF-I and IGF-II at 50 ng/ml increased extracellular gpYKL40 3.6- and 3.4-fold, respectively. The present biochemical and biological findings give new insights for studying the function of YKL40 in cartilage.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503en_US
dc.relation.ispartofJournal of Cellular Biochemistryen_US
dc.subject.meshAdipokinesen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAmino Acids - Analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCartilage, Articular - Secretionen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshChondrocytes - Secretionen_US
dc.subject.meshCytokines - Pharmacologyen_US
dc.subject.meshGlycoproteinsen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshIsoelectric Pointen_US
dc.subject.meshKineticsen_US
dc.subject.meshLectinsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshProteins - Chemistry - Isolation & Purification - Secretionen_US
dc.subject.meshSequence Analysisen_US
dc.titlePurification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytesen_US
dc.typeArticleen_US
dc.identifier.emailVanhoutte, PM:vanhoutt@hku.hken_US
dc.identifier.authorityVanhoutte, PM=rp00238en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/(SICI)1097-4644(19980615)69:4<414::AID-JCB3>3.0.CO;2-Qen_US
dc.identifier.pmid9620168-
dc.identifier.scopuseid_2-s2.0-0031750285en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031750285&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume69en_US
dc.identifier.issue4en_US
dc.identifier.spage414en_US
dc.identifier.epage424en_US
dc.identifier.isiWOS:000073757400003-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDe Ceuninck, F=6602162018en_US
dc.identifier.scopusauthoridPastoureau, P=6603951885en_US
dc.identifier.scopusauthoridBouet, F=7003488135en_US
dc.identifier.scopusauthoridBonnet, J=7201770893en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US

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