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Molecular characterization of chicken syndecan-2 proteoglycan.

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Molecular characterization of chicken syndecan-2 proteoglycan. / Chen, Ligong; Couchman, John R; Smith, Jacqueline; Woods, Anne.

I: Biochemical Journal, Bind 366, Nr. Pt 2, 2002, s. 481-90.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Chen, L, Couchman, JR, Smith, J & Woods, A 2002, 'Molecular characterization of chicken syndecan-2 proteoglycan.', Biochemical Journal, bind 366, nr. Pt 2, s. 481-90. https://doi.org/10.1042/BJ20020711

APA

Chen, L., Couchman, J. R., Smith, J., & Woods, A. (2002). Molecular characterization of chicken syndecan-2 proteoglycan. Biochemical Journal, 366(Pt 2), 481-90. https://doi.org/10.1042/BJ20020711

Vancouver

Chen L, Couchman JR, Smith J, Woods A. Molecular characterization of chicken syndecan-2 proteoglycan. Biochemical Journal. 2002;366(Pt 2):481-90. https://doi.org/10.1042/BJ20020711

Author

Chen, Ligong ; Couchman, John R ; Smith, Jacqueline ; Woods, Anne. / Molecular characterization of chicken syndecan-2 proteoglycan. I: Biochemical Journal. 2002 ; Bind 366, Nr. Pt 2. s. 481-90.

Bibtex

@article{aad4cb90596e11dd8d9f000ea68e967b,
title = "Molecular characterization of chicken syndecan-2 proteoglycan.",
abstract = "A partial syndecan-2 sequence (147 bp) was obtained from chicken embryonic fibroblast poly(A)+ RNA by reverse transcription-PCR. This partial sequence was used to produce a 5'-end-labelled probe. A chicken liver cDNA library was screened with this probe, and overlapping clones were obtained encompassing the entire cDNA of 3 kb. The open reading frame encodes a protein of 201 amino acids. The cytoplasmic domain is identical with that of mammalian syndecan-2, and highly similar to those of Xenopus laevis and zebrafish syndecan-2. The transmembrane domain is identical with that of mammalian and zebrafish syndecan-2, and highly similar to that of Xenopus laevis syndecan-2. The ectodomain is 45-62% identical with that of zebrafish, Xenopus laevis and mammalian syndecan-2. Two coding single nucleotide polymorphisms were observed. In vitro transcription and translation yielded a product of 30 kDa. Western blotting of chicken embryonic fibroblast cell lysates with species-specific monoclonal antibody mAb 8.1 showed that chicken syndecan-2 is substituted with heparan sulphate, and that the major form of chicken syndecan-2 isolated from chicken fibroblasts is consistent with the formation of SDS-resistant dimers, which is common for syndecans. A 5'-end-labelled probe hybridized to two mRNA species in chicken embryonic fibroblasts, while Northern analysis with poly(A)+ RNAs from different tissues of chicken embryos showed wide and distinct distributions of chicken syndecan-2 during embryonic development. This pattern was different from that reported for syndecan-4, but consistent with the roles of syndecan-2 in neural maturation and in mesenchymal-matrix interactions.",
author = "Ligong Chen and Couchman, {John R} and Jacqueline Smith and Anne Woods",
note = "Keywords: Amino Acid Sequence; Animals; Base Sequence; Chick Embryo; Chickens; DNA, Complementary; Fibroblasts; Gene Library; Humans; Liver; Mammals; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Polymorphism, Genetic; Proteoglycans; Recombinant Proteins; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Syndecan-2; Xenopus Proteins; Zebrafish Proteins",
year = "2002",
doi = "10.1042/BJ20020711",
language = "English",
volume = "366",
pages = "481--90",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - Molecular characterization of chicken syndecan-2 proteoglycan.

AU - Chen, Ligong

AU - Couchman, John R

AU - Smith, Jacqueline

AU - Woods, Anne

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Chick Embryo; Chickens; DNA, Complementary; Fibroblasts; Gene Library; Humans; Liver; Mammals; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Polymorphism, Genetic; Proteoglycans; Recombinant Proteins; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Syndecan-2; Xenopus Proteins; Zebrafish Proteins

PY - 2002

Y1 - 2002

N2 - A partial syndecan-2 sequence (147 bp) was obtained from chicken embryonic fibroblast poly(A)+ RNA by reverse transcription-PCR. This partial sequence was used to produce a 5'-end-labelled probe. A chicken liver cDNA library was screened with this probe, and overlapping clones were obtained encompassing the entire cDNA of 3 kb. The open reading frame encodes a protein of 201 amino acids. The cytoplasmic domain is identical with that of mammalian syndecan-2, and highly similar to those of Xenopus laevis and zebrafish syndecan-2. The transmembrane domain is identical with that of mammalian and zebrafish syndecan-2, and highly similar to that of Xenopus laevis syndecan-2. The ectodomain is 45-62% identical with that of zebrafish, Xenopus laevis and mammalian syndecan-2. Two coding single nucleotide polymorphisms were observed. In vitro transcription and translation yielded a product of 30 kDa. Western blotting of chicken embryonic fibroblast cell lysates with species-specific monoclonal antibody mAb 8.1 showed that chicken syndecan-2 is substituted with heparan sulphate, and that the major form of chicken syndecan-2 isolated from chicken fibroblasts is consistent with the formation of SDS-resistant dimers, which is common for syndecans. A 5'-end-labelled probe hybridized to two mRNA species in chicken embryonic fibroblasts, while Northern analysis with poly(A)+ RNAs from different tissues of chicken embryos showed wide and distinct distributions of chicken syndecan-2 during embryonic development. This pattern was different from that reported for syndecan-4, but consistent with the roles of syndecan-2 in neural maturation and in mesenchymal-matrix interactions.

AB - A partial syndecan-2 sequence (147 bp) was obtained from chicken embryonic fibroblast poly(A)+ RNA by reverse transcription-PCR. This partial sequence was used to produce a 5'-end-labelled probe. A chicken liver cDNA library was screened with this probe, and overlapping clones were obtained encompassing the entire cDNA of 3 kb. The open reading frame encodes a protein of 201 amino acids. The cytoplasmic domain is identical with that of mammalian syndecan-2, and highly similar to those of Xenopus laevis and zebrafish syndecan-2. The transmembrane domain is identical with that of mammalian and zebrafish syndecan-2, and highly similar to that of Xenopus laevis syndecan-2. The ectodomain is 45-62% identical with that of zebrafish, Xenopus laevis and mammalian syndecan-2. Two coding single nucleotide polymorphisms were observed. In vitro transcription and translation yielded a product of 30 kDa. Western blotting of chicken embryonic fibroblast cell lysates with species-specific monoclonal antibody mAb 8.1 showed that chicken syndecan-2 is substituted with heparan sulphate, and that the major form of chicken syndecan-2 isolated from chicken fibroblasts is consistent with the formation of SDS-resistant dimers, which is common for syndecans. A 5'-end-labelled probe hybridized to two mRNA species in chicken embryonic fibroblasts, while Northern analysis with poly(A)+ RNAs from different tissues of chicken embryos showed wide and distinct distributions of chicken syndecan-2 during embryonic development. This pattern was different from that reported for syndecan-4, but consistent with the roles of syndecan-2 in neural maturation and in mesenchymal-matrix interactions.

U2 - 10.1042/BJ20020711

DO - 10.1042/BJ20020711

M3 - Journal article

C2 - 12038962

VL - 366

SP - 481

EP - 490

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 2

ER -

ID: 5162875