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Updated: Aug 8, 2026

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
Published on: July 23, 2015
Expression of type XXIII collagen mRNA and protein
Manuel Koch1, Guido Veit2, Sigmar Stricker3
1Center for Biochemistry, University of Cologne, Joseph-Stelzmann Strasse 52, 50931 Cologne, Germany; Department of Dermatology, University of Cologne, Joseph-Stelzmann Strasse 52, 50931 Cologne, Germany; Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann Strasse 52, 50931 Cologne, Germany.
Abstract:
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 humanalpha1(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 alpha1(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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