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Titolo:
DISTRIBUTION OF HYALURONAN IN ARTICULAR-CARTILAGE AS PROBED BY A BIOTINYLATED BINDING REGION OF AGGRECAN
Autore:
PARKKINEN JJ; HAKKINEN TP; SAVOLAINEN S; WANG C; TAMMI R; AGREN UM; LAMMI MJ; AROKOSKI J; HELMINEN HJ; TAMMI MI;
Indirizzi:
KUOPIO UNIV,DEPT PATHOL KUOPIO FINLAND KUOPIO UNIV,DEPT ANAT SF-70211 KUOPIO FINLAND
Titolo Testata:
HISTOCHEMISTRY AND CELL BIOLOGY
fascicolo: 3, volume: 105, anno: 1996,
pagine: 187 - 194
SICI:
0948-6143(1996)105:3<187:DOHIAA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
AGE-RELATED-CHANGES; KNEE STIFLE JOINT; GLYCOSAMINOGLYCAN CONTENT; PROTEOGLYCAN AGGREGATION; CHONDROITIN SULFATE; LINK PROTEIN; VI COLLAGEN; ACID; LOCALIZATION; IMMOBILIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Parkkinen et al., "DISTRIBUTION OF HYALURONAN IN ARTICULAR-CARTILAGE AS PROBED BY A BIOTINYLATED BINDING REGION OF AGGRECAN", HISTOCHEM C, 105(3), 1996, pp. 187-194

Abstract

The proportion of total tissue hyaluronan involved in interactions with aggrecan and link protein was estimated from extracts of canine knee articular cartilages using a biotinylated hyaluronan binding region-link protein complex (bHABC) of proteoglycan aggregate as a probe in an ELISA-like assay. Microscopic sections were stained with bHABC to reveal free hyaluronan in various sites and zones of the cartilages. Articular cartilage, cut into 20 mu m-thick sections, was extracted with 4 M guanidinium chloride (GuCl). Aliquots of the extract (after removing GuCl) were assayed for hyaluronan, before and after papain digestion. The GuCl extraction residues were analyzed after solubilization by papain. It was found that 47-51% of total hyaluronan remained in the GuCl extraction residue, in contrast to the 8-15% of total proteoglycans. Analysis of the extract revealed that 24-50% of its hyaluronan was directly detectable with the probe, while 50-76% became available onlyafter protease digestion. The extracellular matrix in cartilage sections was stained with the bHABC probe only in the superficial zone and the periphery of the articular surfaces, both sites known to have a relatively low proteoglycan concentration. Trypsin pretreatment of the sections enhanced the staining of the intermediate and deep zones, presumably by removing the steric obstruction caused by the chondroitin sulfate binding region of aggrecans. Enhanced matrix staining in these zones was also obtained by a limited digestion with chondroitinase ABC. The results indicate that a part of cartilage hyaluronan is free fromendogenous binding proteins, such as aggrecan and link protein, but that the chondroitin sulfate-rich region of aggrecan inhibits its probing in intact tissue sections. Therefore, hyaluronan staining was more intense in cartilage areas with lower aggrecan content. A large proportion of hyaluronan resists GuCl extraction, even from 20-mu m-thick tissue sections.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 09:24:25