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  Expression of Type XXIII Collagen mRNA and Protein

Koch, M., Veit, G., Stricker, S., Bhatt, P., Kutsch, S., Zhou, P., et al. (2006). Expression of Type XXIII Collagen mRNA and Protein. Journal of Biological Chemistry, 281(30), 21546-21557. doi:10.1074/jbc.M604131200.

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Genre: Zeitschriftenartikel
Alternativer Titel : J Biol Chem

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Koch.pdf (beliebiger Volltext), 889KB
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Koch, Manuel, Autor
Veit, Guido, Autor
Stricker, Sigmar1, Autor           
Bhatt, Pinaki, Autor
Kutsch, Stefanie, Autor
Zhou, Peihong, Autor
Reinders, Elina, Autor
Hahn, Rita A., Autor
Song, Rich, Autor
Burgeson, Robert E., Autor
Gerecke, Donald R., Autor
Mundlos, Stefan1, Autor           
Gordon, Marion K., Autor
Affiliations:
1Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433557              

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 Zusammenfassung: Collagen XXIII is a member of the transmembranous subfamily of collagens containing a cytoplasmic domain, a membrane-spanning hydrophobic domain, and three extracellular triple helical collagenous domains interspersed with non-collagenous domains. We cloned mouse, chicken, and human{alpha}1(XXIII) collagen cDNAs and showed that this non-abundant collagen has a limited tissue distribution in non-tumor tissues. Lung, cornea, brain, skin, tendon, and kidney are the major sites of expression. In contrast, five transformed cell lines were tested for collagen XXIII expression, and all expressed the mRNA. In vivo the {alpha}1(XXIII) mRNA is found in mature and developing organs, the latter demonstrated using stages of embryonic chick cornea and mouse embryos. Polyclonal antibodies were generated in guinea pig and rabbit and showed that collagen XXIII has a transmembranous form and a shed form. Comparison of collagen XXIII with its closest relatives in the transmembranous subfamily of collagens, types XIII and XXV, which have the same number of triple helical and non-collagenous regions, showed that there is a discontinuity in the alignment of domains but that striking similarities remain despite this.

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Sprache(n): eng - English
 Datum: 2006-07-28
 Publikationsstatus: Erschienen
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 Identifikatoren: eDoc: 313089
DOI: 10.1074/jbc.M604131200
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Titel: Journal of Biological Chemistry
  Alternativer Titel : J Biol Chem
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 281 (30) Artikelnummer: - Start- / Endseite: 21546 - 21557 Identifikator: ISSN: 0021-9258