A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo.

Kimata, Koji; Oike, Y; Tani, Kazuhide; Shinomura, Tamayuki; Yamagata, Masahito; Uritani, Masahiro; Suzuki, Sakaru

doi:10.1016/s0021-9258(18)67049-8

Cited by 186 publications

(23 citation statements)

References 51 publications

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“…cDNA was produced from poly A+ RNA from cultured 10-d chick embryo fibroblasts (CEF) primed with oligo dT nucleotides and inserted into the kgtll phage vector using EcoRI linkers as described previously (Obara et al ., 1988) . A total of 5 x 105 plaques using E. coli strain Y1090 was screened with rabbit polyclonal antibodies raised against type M proteoglycan (PG-M) (Kimata et al ., 1986) by the method of Huynh et al . (1985) .…”

Section: Molecular Cloningmentioning

confidence: 99%

“…We had initially intended to isolate a cDNA clone for the core protein of PG-M chondroitin sulfate proteoglycan (Kimata et al ., 1986;Yamagata et al, 1986Yamagata et al, , 1989 . For this purpose, a cDNA library from chick embryonic fibroblasts was constructed in the Agtll vector by a standard protocol with oligo dT primers (Obara et al ., 1988), and was screened with antibodies to PG-M.…”

Section: Molecular Cloning and Structure Oftype XII Collagenmentioning

confidence: 99%

“…For this purpose, a cDNA library from chick embryonic fibroblasts was constructed in the Agtll vector by a standard protocol with oligo dT primers (Obara et al ., 1988), and was screened with antibodies to PG-M. Characterization and specificity of the antibody were described previously (Kimata et al, 1986) .…”

Section: Molecular Cloning and Structure Oftype XII Collagenmentioning

confidence: 99%

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The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site.

Yamagata

Yamada

et al. 1991

The Journal of Cell Biology

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111

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. Extracellular matrix molecules are generally categorized as collagens, elastin, proteoglycans, or other noncollagenous structural/cell interaction proteins. Many of these extracellular proteins contain distinctive repetitive modules, which can sometimes be found in other proteins . We describe the complete primary structure of an al chain of type XII collagen from chick embryonic fibroblasts. This large, structurally chimeric molecule identified by cDNA analysis combines previously unrelated molecular domains into a single large protein 3,124 residues long (ti340 kD) . The deduced chicken type XII collagen sequence starts at the amino terminus with one unit of the type III motif of fibronectin, which is followed by one unit homologous to the von Willebrand factor A domain, then one more fibronectin type III module, a second A domain from von Willebrand factor, 6 units of type III motif and a third A domain, 10 consecutive units of type III motif and a fourth A domain, a domain homologous to the NC4 domain peptide of type IX collagen, and finally two short collagenous regions previ-E xTRACELLULAR matrices can influence a variety of cell and tissue functions; their components are generally classified into collagens, elastin, proteogly cans, or a group of various noncollagenous structural/interactive glycoproteins (Hay, 1981 ;Piez and Reddi, 1984). Recent progress in the structural analysis of extracellular matrix molecules reveals that they generally contain distinctive modules, which are reiterated in the protein and are

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Section: Molecular Cloningmentioning

confidence: 99%

Section: Molecular Cloning and Structure Oftype XII Collagenmentioning

confidence: 99%

Section: Molecular Cloning and Structure Oftype XII Collagenmentioning

confidence: 99%

See 1 more Smart Citation

The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site.

Yamagata

Yamada

et al. 1991

The Journal of Cell Biology

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111

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“…These ECM molecules can arbitrarily be divided into two overlapping groups: those which appear early in differentiation and may therefore promote this process, and those which are present in the differentiated tissue and have a predominantly structural role. Collagen type I, fibronectin, and a large chondroitin sulfate proteoglycan increase in density in the cartilage anlage of the embryonic chick limb bud at the time of mesenchymal condensation (11,17). As cartilage differentiation proceeds, collagen type I and the large chondroitin sulfate proteoglycan are replaced by the cartilage-specific collagen type 1I and a cartilage-specific proteoglycan which persist throughout differentiation (11,17,31).…”

mentioning

confidence: 99%

“…Collagen type I, fibronectin, and a large chondroitin sulfate proteoglycan increase in density in the cartilage anlage of the embryonic chick limb bud at the time of mesenchymal condensation (11,17). As cartilage differentiation proceeds, collagen type I and the large chondroitin sulfate proteoglycan are replaced by the cartilage-specific collagen type 1I and a cartilage-specific proteoglycan which persist throughout differentiation (11,17,31). Hyaluronic acid con-1.…”

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confidence: 99%

Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro.

Mackie

Thesleff

Chiquet‐Ehrismann

1987

The Journal of Cell Biology

339

207

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Abstract. The tissue distribution of the extracellular matrix glycoprotein, tenascin, during cartilage and bone development in rodents has been investigated by immunohistochemistry. Tenascin was present in condensing mesenchyme of cartilage anlagen, but not in the surrounding mesenchyme. In fully differentiated cartilages, tenascin was only present in the perichondrium. In bones that form by endochondral ossification, tenascin reappeared around the osteogenic cells invading the cartilage model. Tenascin was also present in the condensing mesenchyme of developing bones that form by intramembranous ossification and later was present around the spicules of forming bone.Tenascin was absent from mature bone matrix but persisted on periosteal and endosteal surfaces.Immunofluorescent staining of wing bud cultures from chick embryos showed large amounts of tenascin in the forming cartilage nodules. Cultures grown on a substrate of tenascin produced more cartilage nodules than cultures grown on tissue culture plastic. Tenascin in the culture medium inhibited the attachment of wing bud cells to fibronectin-coated substrates. We propose that tenascin plays an important role in chondrogenesis by modulating fibronectin-cell interactions and causing cell rounding and condensation.T HE extracellular matrix (ECM) ~ is important for cartilage and bone differentiation and is the very basis of the function of the fully differentiated hard tissues. Cartilage differentiation begins with the rounding and condensation of mesenchymal cells, followed by differentiation which is characterized by the synthesis of cartilage-specific matrix components. Bone development can occur either by intramembranous or endochondral ossification. Intramembranous ossification takes place within a layer of mesenchyme, whereas endochondral ossification occurs within a cartilage model in which the chondrocytes hypertrophy and are then replaced by invading osteogenic cells.Several immunohistochemical studies have been carried out which have demonstrated changes in ECM components during cartilage and bone differentiation. These ECM molecules can arbitrarily be divided into two overlapping groups: those which appear early in differentiation and may therefore promote this process, and those which are present in the differentiated tissue and have a predominantly structural role. Collagen type I, fibronectin, and a large chondroitin sulfate proteoglycan increase in density in the cartilage anlage of the embryonic chick limb bud at the time of mesenchymal condensation (11,17). As cartilage differentiation proceeds, collagen type I and the large chondroitin sulfate proteoglycan are replaced by the cartilage-specific collagen type 1I and a cartilage-specific proteoglycan which persist throughout differentiation (11,17,31). Hyaluronic acid con- In vitro and in vivo studies have confirmed the importance of many of these ECM molecules in cartilage or bone differentiation. Chondrogenesis in vitro is stimulated by type I and type II collagen (18), chondroitin sulfate pro...

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Syndecan-3 in limb skeletal development

Kosher

1998

Microsc. Res. Tech.

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A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo.

Cited by 186 publications

References 51 publications

The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site.

The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site.

Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro.

Syndecan-3 in limb skeletal development

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