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- Publisher Website: 10.1002/(SICI)1097-4644(19980615)69:4<414::AID-JCB3>3.0.CO;2-Q
- Scopus: eid_2-s2.0-0031750285
- PMID: 9620168
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Article: Purification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytes
Title | Purification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytes |
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Authors | |
Keywords | Biochemical characterization Chondrocytes Guinea pig Insulin-like growth factors Osteoarthritis Purification Regulation YKL40 |
Issue Date | 1998 |
Publisher | John 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/171209 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 0.768 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | De Ceuninck, F | en_US |
dc.contributor.author | Pastoureau, P | en_US |
dc.contributor.author | Bouet, F | en_US |
dc.contributor.author | Bonnet, J | en_US |
dc.contributor.author | Vanhoutte, PM | en_US |
dc.date.accessioned | 2012-10-30T06:12:42Z | - |
dc.date.available | 2012-10-30T06:12:42Z | - |
dc.date.issued | 1998 | en_US |
dc.identifier.citation | Journal Of Cellular Biochemistry, 1998, v. 69 n. 4, p. 414-424 | en_US |
dc.identifier.issn | 0730-2312 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171209 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | John Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503 | en_US |
dc.relation.ispartof | Journal of Cellular Biochemistry | en_US |
dc.subject | Biochemical characterization | - |
dc.subject | Chondrocytes | - |
dc.subject | Guinea pig | - |
dc.subject | Insulin-like growth factors | - |
dc.subject | Osteoarthritis | - |
dc.subject | Purification | - |
dc.subject | Regulation | - |
dc.subject | YKL40 | - |
dc.subject.mesh | Adipokines | en_US |
dc.subject.mesh | Amino Acid Sequence | en_US |
dc.subject.mesh | Amino Acids - Analysis | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cartilage, Articular - Secretion | en_US |
dc.subject.mesh | Cells, Cultured | en_US |
dc.subject.mesh | Chondrocytes - Secretion | en_US |
dc.subject.mesh | Cytokines - Pharmacology | en_US |
dc.subject.mesh | Glycoproteins | en_US |
dc.subject.mesh | Glycosylation | en_US |
dc.subject.mesh | Guinea Pigs | en_US |
dc.subject.mesh | Isoelectric Point | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Lectins | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.subject.mesh | Molecular Weight | en_US |
dc.subject.mesh | Proteins - Chemistry - Isolation & Purification - Secretion | en_US |
dc.subject.mesh | Sequence Analysis | en_US |
dc.title | Purification of guinea pig YKL40 and modulation of its secretion by cultured articular chondrocytes | en_US |
dc.type | Article | en_US |
dc.identifier.email | Vanhoutte, PM:vanhoutt@hku.hk | en_US |
dc.identifier.authority | Vanhoutte, PM=rp00238 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1002/(SICI)1097-4644(19980615)69:4<414::AID-JCB3>3.0.CO;2-Q | en_US |
dc.identifier.pmid | 9620168 | - |
dc.identifier.scopus | eid_2-s2.0-0031750285 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0031750285&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 69 | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.spage | 414 | en_US |
dc.identifier.epage | 424 | en_US |
dc.identifier.isi | WOS:000073757400003 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | De Ceuninck, F=6602162018 | en_US |
dc.identifier.scopusauthorid | Pastoureau, P=6603951885 | en_US |
dc.identifier.scopusauthorid | Bouet, F=7003488135 | en_US |
dc.identifier.scopusauthorid | Bonnet, J=7201770893 | en_US |
dc.identifier.scopusauthorid | Vanhoutte, PM=7202304247 | en_US |
dc.identifier.issnl | 0730-2312 | - |