The core molecule from type H proteoglycan. Release of mannose-containing oligosaccharides by digestion with <i>N</i>-oligosaccharide glycopeptidase

Takahashi, Nobutaka; Ishihara, Hideko; Tejima, Setsuzo; Oike, Y; Kimata, Koji; Shinomura, Tamayuki; Suzuki, Sakaru

doi:10.1042/bj2290561

Cited by 11 publications

(3 citation statements)

References 34 publications

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“…PA oligosaccharide (about 50-100 nmol each) isolated by HPLC was methylated by the method of Hakomori (1964). The permethylated products were analyzed as described by Takahashi et al (1985) on a JEOL-DX 300 gas chromatograph-mass spectrometer.…”

Section: Methodsmentioning

confidence: 99%

Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein

Tomiya

Yamaguchi²,

Awaya³

et al. 1988

Biochemistry

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The structures of asparagine-linked oligosaccharides of porcine pancreatic beta-kallikrein are reported. Asparagine-linked neutral oligosaccharides were released by N-oligosaccharide glycopeptidase digestion, and the reducing ends of the oligosaccharides were derivatized with a fluorescent reagent, 2-aminopyridine. The mixture of pyridylamino oligosaccharides was separated by reverse-phase and amide-adsorption high-performance liquid chromatography. The pyridylamino oligosaccharides were separated into more than 50 kinds of oligosaccharides. The structures of 5 kinds of triantennary and 12 kinds of tetraantennary oligosaccharides were determined by the use of high-resolution proton nuclear magnetic resonance spectroscopy and methylation analysis. Furthermore, the structures of five kinds of oligomannose-type oligosaccharides were elucidated by a combination of exoglycosidase digestion and high-performance liquid chromatography. 1H NMR data for 14 out of the 17 kinds of N-acetyllactosamine-type oligosaccharides reported here have not previously been described in the literature. (1) It has been shown that fucose containing tri- and tetraantennary oligosaccharides is predominant in porcine pancreatic beta-kallikrein B. (2) It has also been shown that the heterogeneity of the structure in these types of oligosaccharides is derived from the variety of the positions of galactose residues linked to outer N-acetylglucosamine residues. (3) The distribution of oligosaccharides into two glycosylation sites, asparagine-95 and asparagine-239, of beta-kallikrein B was determined. It has been found that oligomannose-type oligosaccharides are exclusively present at asparagine-239, although N-acetyllactosamine-type oligosaccharides occur at both glycosylation sites.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Methodsmentioning

confidence: 99%

Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein

Tomiya

Yamaguchi²,

Awaya³

et al. 1988

Biochemistry

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“…Oligosaccharide (about 50-100 µg each as neutral sugar) separated by TLC was reduced and methylated by the method of Hakomori (1964). The permethylated products were analyzed as described by Takahashi et al, (1985) on a JEOL-DX300 gas chromatograph-mass spectrometer.…”

Section: Methodsmentioning

confidence: 99%

Xylose-containing common structural unit in N-linked oligosaccharides of laccase from sycamore cells

Takahashi¹,

Hotta²,

Ishihara³

et al. 1986

Biochemistry

121

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“…Cartilage PG isolated from chick embryo cartilage (PG-H) was neither incorporated into the matrix nor corrected the abnormalities of mutant chondrocyte nodules as well as the mammalian proteoglycans. PG-H differs from the chondrosarcoma cartilage PG in that it contains keratan sulfate side chains (22,23), is rich in high mannose-typed N-linked oligosaccharides (30), and has a homologous, but partially different, core polypeptide (unpublished observations). It may be that some of these species-specific structural factors interfere with proteoglycan-link protein interaction involved in the formation of stable proteoglycan aggregates.…”

Section: Discussionmentioning

confidence: 95%

Correction of abnormal matrix formed by cmd/cmd chondrocytes in culture by exogenously added cartilage proteoglycan.

Takeda¹,

Iwata²,

Suzuki³

et al. 1986

The Journal of Cell Biology

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. Address offprint requests to K. Kimata.Abstract. The cartilage matrix deficiency (cmd/cmd) mouse fails to synthesize the core protein of cartilagecharacteristic proteoglycan (cartilage PG). Chondrocytes from the cmd/cmd cartilage cultured in vitro produced nodules with greatly reduced extracellular matrix. Immunofluorescence staining revealed that the nodules of mutant cells differed from the normal in lacking cartilage PG and in uneven and reduced deposition of type II collagen. Exogenously added cartilage PG prepared from either normal mouse cartilage or Swarm rat chondrosarcoma to the culture medium was incorporated exclusively into the extracellular matrices of the nodules, with a concurrent correction of the abnormal distribution pattern of type II collagen. The incorporation of cartilage PG into the matrix was disturbed by hyaluronic acid or decasaccharide derived therefrom, suggesting that the incorporation process involves the interaction of added proteoglycan with hyaluronic acid. Both the hyaluronic acid-binding region and the protein-enriched core molecule prepared from rat chondrosarcoma cartilage PG could also be incorporated but, unlike the intact cartilage PG, they were distributed equally in the surrounding zones where fibroblast-like cells predominate. The results indicate that the intact form of cartilage PG is required for specific incorporation into the chondrocyte nodules, and further suggest that cartilage PG plays a regulatory role in the assembly of the matrix macromolecules.T HE extracellular matrix of cartilage is composed primarily of cartilage-characteristic proteoglycan (cartilage PG) t and type II collagen. Cartilage PG is present in the matrix as high molecular weight aggregates in which proteoglycan monomers bind specifically to hyaluronic acid at regular intervals through stabilization by link protein (8). Type II collagen molecules also are assembled to form fibrils with characteristic size and morphology (for review, see reference 33).Cartilage matrix deficiency (cmd/cmd) is an autosomal recessive lethal mutation in mice resulting in a syndrome including disproportionate dwarfism, short snout, and cleft palate (26). These abnormalities have been shown to result from failure in the synthesis of cartilage PG core protein (15). Other matrix components, such as type II collagen, small proteoglycans, hyaluronic acid, and link protein are synthesized nearly at normal rates (3,15,18). Therefore, the cell culture of cmd/cmd chondrocytes provides a useful system in which the function in matrix assembly of cartilage PG may be studied. We show here that cmd/cmd chondrocytes in monolayer culture exhibit an abnormal extracellular matrix and that the abnormality could be corrected by adding cartilage PG to the culture medium. Evidence is presented to show that the exogenous cartilage PG is integrated into the matrix of mutant chondrocytes through the processes in which the interactions of an intact form of cartilage PG with the other matrix molecules are involved. Abbreviations used in thi...

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The core molecule from type H proteoglycan. Release of mannose-containing oligosaccharides by digestion with N-oligosaccharide glycopeptidase

Cited by 11 publications

References 34 publications

Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein

Structural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein

Xylose-containing common structural unit in N-linked oligosaccharides of laccase from sycamore cells

Correction of abnormal matrix formed by cmd/cmd chondrocytes in culture by exogenously added cartilage proteoglycan.

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