Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
IMMORTALIZED, CLONED MOUSE CHONDROCYTIC CELLS (MC615) PRODUCE 3 DIFFERENT MATRIX PROTEOGLYCANS WITH CORE-PROTEIN-SPECIFIC CHONDROITIN DERMATAN SULFATE STRUCTURES/
Autore:
KOKENYESI R; SILBERT JE;
Indirizzi:
EDITH NOURSE ROGERS MEM VET ADM HOSP,CONNECT TISSUE RES LAB,200 SPRINGS RD BEDFORD MA 01730 HARVARD UNIV,BRIGHAM & WOMENS HOSP,SCH MED,DIV RHEUMATOL ALLERGY & IMMUNOL,DEPT MED BOSTON MA 02115
Titolo Testata:
Biochemical journal
, volume: 327, anno: 1997,
parte:, 3
pagine: 831 - 839
SICI:
0264-6021(1997)327:<831:ICMCC(>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
DERMATAN SULFATE PROTEOGLYCAN; HUMAN ARTICULAR-CARTILAGE; EMBRYO EPIPHYSEAL CARTILAGE; COMPLETE CDNA CLONING; CHICK-EMBRYO; BREFELDIN-A; GENOMIC ORGANIZATION; PG-M; LOCALIZATION; BIOSYNTHESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
R. Kokenyesi e J.E. Silbert, "IMMORTALIZED, CLONED MOUSE CHONDROCYTIC CELLS (MC615) PRODUCE 3 DIFFERENT MATRIX PROTEOGLYCANS WITH CORE-PROTEIN-SPECIFIC CHONDROITIN DERMATAN SULFATE STRUCTURES/", Biochemical journal, 327, 1997, pp. 831-839

Abstract

Cloned immortalized MC615 mouse chondrocytic cells were used to examine their capability to produce multiple types of matrix proteoglycans. Immunofluorescence staining indicated a uniform expression of aggrecan, biglycan and decorin by all cells. After culture with [S-35]sulphate, proteo[S-35]glycans secreted by the cells were found to elute in two peaks from a Sepharose CL-4B column. The first peak, at the void volume of the column, contained a large proteoglycan with an estimated average hydrodynamic mass of 10(3) kDa. The glycosaminoglycan chains of this proteoglycan had an average hydrodynamic size of 17 kDa, estimated by Sepharose CL-6B chromatography, indicating the presence of 30-70 glycosaminoglycan chains per core protein, which was consistent with the characteristics of aggrecan. Biglycan and decorin were immunoisolated from the second Sepharose CL-4B peak, and had average glycosaminoglycan hydrodynamic sizes of approx, 25 kDa and 32 kDa respectively. Glycosaminoglycan chains of the aggrecan, biglycan and decorin were treated with chondroitin ABC lyase, chondroitin AC lyase and chondroitin B lyase to determine the positions of sulphation and the degree of uronic acid epimerization. The aggrecan glycosaminoglycan chains were foundto contain a 4-sulphate/6-sulphate ratio of 7:3, with no epimerization of glucuronic acid to iduronic acid. The biglycan glycosaminoglycan chains were found to contain a similar ratio of 4-sulphate/6-sulphate,but with approx. 40-45 % of the glucuronic acid epimerized to iduronic acid. The decorin glycosaminoglycan chains were found to contain 4-sulphate but no detectable 6-sulphate, and approx. 30-35 % epimerization of the glucuronic acid to iduronic acid. The results, using these cloned cells, indicated that a single MC615 cell is able to make all three proteoglycans with distinctive differences between the glycosaminoglycans of aggrecan, biglycan and decorin. These data indicate that a mechanism must exist for a single MC615 cell to regulate the sizes and fine structures of glycosaminoglycans on simultaneously produced, different proteoglycans in a core-protein-specific manner.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 20:56:15