Sodium chondroitin sulfate-protein complexes of cartilage. I. Molecular weight and shape

Mathews, Martin B.; Lozaityte, Irene

doi:10.1016/0003-9861(58)90210-8

Cited by 200 publications

(75 citation statements)

References 38 publications

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“…The predominate glycosaminoglycan present in cartilage has long been known to be chondroitin sulfate. 2 However, extraction of the chondroitin sulfate in a more native form, as a proteoglycan, proved to be a daunting task. The revolution in the field came about through the work of Hascall and Sajdera.…”

Section: Introductionmentioning

confidence: 99%

Cartilage proteoglycans

Knudson

2001

Seminars in Cell & Developmental Biology

546

412

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Section: Introductionmentioning

confidence: 99%

Cartilage proteoglycans

Knudson

2001

Seminars in Cell & Developmental Biology

546

412

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“…Most glycosaminoglycans in normal cartilage do not exist free as such but are covalently linked to protein in complex molecules, i.e.. proteoglycans (5). The majority of the proteoglycans in normal cartilage are organized into macromolecular aggregates with sedimentation coeffi-cients (Szoow) o f 60-70s (6), i n which many proteoglycan molecules are noncovalently linked to hyaluronic acid (7).…”

Section: Effects Of Diphosphonates On Glycosaminoglycan Synthesis Andmentioning

confidence: 99%

Effects of diphosphonates on glycosaminoglycan synthesis and proteoglycan aggregation in normal adult articular cartilage

Palmoski

Brandt

1978

Arthritis & Rheumatism

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The effects of disodium ethane-1-hydroxy-1,ldiphosphonate (EHDP) and disodium dichloromethylene diphosphonate (CI,MDP) on glycosaminoglycan synthesis and macromolecular organization of proteoglycans have been examined in normal adult canine cartilage. One to 500 p M of either compound produced reversible inhibition of glycosaminoglycan synthesis to about 70% of control levels, whereas lower concentrations had no effect. Based on Sephadex (3-200 chromatography, the average hydrodynamic size of glycosaminoglycans in diphosphonatetreated cartilage was similar to that of those in control cartilage. In most cases proteoglycan aggregates from diphosphonate-treated cartilage were smaller in hydrodynamic size than those from control cartilage, as judged by Sepharose 2B elution profiles. The size of purified proteoglycan subunits, obtained after dissociation of the aggregates with 4 M guanidinium chloride or after incubation of the aggregates with hyaluronic acid PI 4 3 hydrolase, was not affected by the diphosphonates. Fur-

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“…30), in 12 Organen wurde die Aktivität der "sauren" Carboxypeptidase (EC3.4.2.) 2 ) und in 9 dieser Organe die bei pH 3,2 optimal Hämoglobin-spaltende Kathepsin (EC 3.4A23) 2 und äquilibriertem Sephadex-G-150. Auf eine Säule von 150 X 1,5cm (Volumen: 265m/) wurden 45mg einer 11-30 Gew.% Ammoniumsulfatfraktion (gelöst in 2-3 ml 0,2M NaCl-Lösung) aufgetragen und mit 0,2M NaCl-Lösung eluiert.…”

Section: Methodikunclassified

Untersuchungen zum katabolen Mucopolysaccharid-Protein-Stoffwechsel in menschlichen Organen

Platt¹,

Stein²

1969

Clinical Chemistry and Laboratory Medicine

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In der vorliegenden Arbeit wurden in epithelialen und mesenchymalen Geweben vom Menschen die Aktivitäten der Glycosaminoglycano-Hydrolasen: Hyaluronidase, ß-Glucuronidase und ß-Acetylglucosaminidase und die der Peptidhydrolasen: Kathepsin D und saure Carboxypeptidase gemessen. Die höchsten Aktivitäten fanden sich in Thymus, Leber, Milz und Nebenniere. Geringe Aktivitäten wurden im subkutanen Bindegewebe und im Herzen gemessen. Die synergistische Wirkung der 5 lysosomalen Enzyme am MucopolysaccharidProteinkomplex wurde diskutiert. Studies on the Catabolic Mucopolysaccbaride-Protein Metabolism in Human OrgansIn this investigation the activity of the glycosaminoglycan hydrolases: hyaluronidase, /5-gliicuronidase, /?-acetylglucosaminidase and the activity of the peptide hydrolases: cathepsin D and "acid" carboxypeptidase, were measured in human organs. The highest activities were found in the thymus, liver, spleen and suprarenal organ. Low activities were found in the connective tissue of the skin and in the heart. The synergistic mechanism of the five lysosomal enzymes on the mucopolysaccharidprotein complex was discussed.

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Sodium chondroitin sulfate-protein complexes of cartilage. I. Molecular weight and shape

Cited by 200 publications

References 38 publications

Cartilage proteoglycans

Cartilage proteoglycans

Effects of diphosphonates on glycosaminoglycan synthesis and proteoglycan aggregation in normal adult articular cartilage

Untersuchungen zum katabolen Mucopolysaccharid-Protein-Stoffwechsel in menschlichen Organen

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