Age-Related Changes of the Dermatan Sulfate Containing Small Proteoglycans in Bovine Tendon

Honda, Tomohito; Katagiri, Kazumoto; Kuroda, Atsuomi; Matsunaga, Etsuji; Shinkai, Hiroshi

doi:10.1016/s0174-173x(87)80008-0

Cited by 11 publications

(4 citation statements)

References 22 publications

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“…Rosenberg et al [20] have isolated two species of dermatan sulphate proteoglycans from articular cartilages and have shown that these proteoglycans were composed of core proteins of the same molecular size, but of genetically different species. Recently, we found that dermatan sulphate containing small proteoglycans in tendon, skin and cartilage were composed of the same molecular size core proteins, but that those from skin were genetically different from those of tendon and cartilage [21]. No hypermobility of joints was observed in our case, but we were not able to analyse dermatan sulphate in the tendon, which is mainly composed of type I collagen.…”

Section: Discussionmentioning

confidence: 54%

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

Fushimi

Kameyama

Shinkai

1989

Journal of Internal Medicine

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A variant form of Ehlers-Danlos syndrome with single adrenocorticotrophic hormone (ACTH) deficiency and mild diabetes mellitus was studied by immunohistochemical and biochemical analyses of the connective tissue. The patient exhibited features characteristic of the Ehlers-Danlos syndrome, such as fragility, hyperextensibility, and bruisability of the skin and large veins were readily seen, but no hypermobility of any joint was detectable. Biochemical studies of the connective tissue confirmed that the apparent synthesis of collagens was within normal limits, but the deposition of the major proteoglycan in the skin of this patient was markedly reduced, mainly because the synthesis of core protein of dermatan sulphate proteoglycan was defective.

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Section: Discussionmentioning

confidence: 54%

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

Fushimi

Kameyama

Shinkai

1989

Journal of Internal Medicine

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“…The larger ofthese proteoglycans (DS-PGI) predominates over the smaller (DS-PGII) in about a 3:2 molar ratio. The dermatan sulphate chains contain no more than 20-25 % of the uronic acid as iduronate, which is lower than that previously reported for DS-PGs from human fetal membranes (Brennan et al, 1984), bovine fetal tendon (Vogel & Evanko, 1987;Honda et al, 1987) and bovine fetal cartilage (Rosenberg et al, 1982), where iduronate contents greater than 40 % were observed. The core protein of the DS-PGI appeared to be a single species of Mr 44000, whereas DS-PGII had two core proteins of Mr 43000 and 47000.…”

Section: Discussionmentioning

confidence: 56%

Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II

Roughley

White

1989

Biochemical Journal

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Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt. of cartilage. Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance. The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively. After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII. Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.

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“…This is even true in a tissue such as adult human articular cartilage, where the aggregating proteoglycans , presumably produced by the same cells, are predominantly 6-sulfated (21). Some connective tissues do, however, show a slight increase in the proportion of 6-sulfate with age in their dermatan sulfate proteoglycans (15).…”

Section: Discussionmentioning

confidence: 99%

The dermatan sulfate proteoglycans of the adult human meniscus

Roughley

White

1992

Journal Orthopaedic Research

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The dermatan sulfate proteoglycans decorin and biglycan were extracted from pooled adult human menisci with 4 M guanidinium chloride and purified by successive cesium chloride density gradient centrifugation, ion exchange chromatography, and gel filtration. A final yield of about 2 mg of dermatan sulfate proteoglycan per gram of wet tissue was obtained. The proteoglycan is predominantly decorin with some biglycan, and the dermatan sulfate chains contain about 70% of their uronic acid residues as iduronate and possess about three times as much 4-sulfation as 6-sulfation of their N-acetylgalactosamine residues. On gel filtration under associative conditions, about half of the proteoglycan exhibits self-association. This includes most of the biglycan but also a substantial proportion of decorin. The molecules that show self-association appear to have longer dermatan sulfate chains, though there is no apparent difference in their overall composition. The predominance of decorin in the adult meniscus and its ability to interact both with itself and collagen fibrils is compatible with a role in maintaining tissue integrity and strength.

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Age-Related Changes of the Dermatan Sulfate Containing Small Proteoglycans in Bovine Tendon

Cited by 11 publications

References 22 publications

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II

The dermatan sulfate proteoglycans of the adult human meniscus

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