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・ Collagen, type IX, alpha 1
・ Collagen, type V, alpha 1
・ Collagen, type VI, alpha 1
・ Collagen, type VII, alpha 1
・ Collagen, type VIII, alpha 1
・ Collagen, type X, alpha 1
・ Collagen, type XI, alpha 1
・ Collagen, type XII, alpha 1
・ Collagen, type XIII, alpha 1
・ Collagen, type XIV, alpha 1
・ Collagen, type XIX, alpha 1
・ Collagen, type XV, alpha 1
・ Collagen, type XVI, alpha 1
・ Collagen, type XVII, alpha 1
・ Collagen, type XVIII, alpha 1
Collagen, type XXIII, alpha 1
・ Collagen, type XXV, alpha 1
・ Collagen, type XXVII, alpha 1
・ Collagen-induced arthritis
・ Collagenase
・ Collagenase clostridium histolyticum
・ Collagenase IV
・ Collagenopathy, types II and XI
・ Collagenous colitis
・ Collagenous fibroma
・ Collagenous spherulosis
・ Collages (novel)
・ Collagna
・ Collagonum
・ Collagraphy


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Collagen, type XXIII, alpha 1 : ウィキペディア英語版
Collagen, type XXIII, alpha 1

Collagen α-1 (XXIII) chain is a protein encoded by COL23A1 gene, which is located on chromosome 5q35 in humans, and on chromosome 11B1+2 in mice. The location of this gene was discovered by genomic sequence analysis.
Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens. This kind of collagens have a single pass hydrophobic transmembrane domain. The molecule of collagen XXIII can be found either in membrane-bond form or in shed form.
Type XXIII collagen is expressed in both adult tissues and developing organs. It can be found in the epidermis and other epithelia such as those in tongue, gut and lung, but also in the brain, the kidney and the cornea. It has been shown that in prostate collagen XXIII expression is associated with tumor progression.
The functions of collagen XXIII are still unknown, although it is believed that they could be similar to other transmembrane proteins, such as collagen XIII.
== Discovery ==

Collagen XXIII was first identified and isolated from rat prostate carcinoma cells by Jacqueline Banyard, Lere Bao and Bruce R. Zetter in 2003. They also identified this protein in human tissue. They concluded that at the nucleotide level, human and rat collagen XXIII alpha 1 show 76% identity.
Furthermore, cellular localization of collagen XXIII was determined by immunofluorescence staining, using an antibody that recognizes the carboxyl terminus of the protein. It was demonstrated that the carboxyl terminus of collagen XXIII is present on the cell surface.

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