collagen XXIII

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  • For instance, higher levels of collagen XXIII have been associated with higher levels of catenins in cells.
  • The molecule of collagen XXIII can be found either in membrane-bond form or in shed form.
  • It has been shown that in prostate collagen XXIII expression is associated with tumor progression.
  • It has been shown that loss of collagen XXIII may complicate cellular adhesion and reduce lung cancer cell retention.
  • It was demonstrated that the carboxyl terminus of collagen XXIII is present on the cell surface.
  • 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.
  • This characteristic can be also applicable to collagen XXIII.
  • These heightened levels of collagen helped facilitate adhesions and anchorage-independent cell growth and provided evidence of collagen XXIII's role in mediating metastasis.
  • They concluded that at the nucleotide level, human and rat collagen XXIII alpha 1 show 76% identity.
  • Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens.
  • Some experiments suggest that collagen XXIII influences cellular adhesion and stimulates metastasis development by facilitating cancer cells growth and survival when they are rounded and not able to spread.
  • The distribution of both collagen XXIII forms is tissue-specific, since there are organs such as the brain where the shed form is predominant, whereas in the lungs the molecule is generally found as the full-length form.
  • Furin proteases are not able to reach collagen XXIII molecules when they are inside lipid rafts, therefore, collagen XXIII molecules can conserve their full-length form.
  • It has been reported that the cell is able to regulate the amounts of collagen XXIII in the membrane-bound form and in the secreted shed form, influencing the production of one form or the other when it is needed.
  • Collagen XXIII molecule might be shed at Golgi apparatus or the cellular membrane.
  • Full-length molecules of collagen XXIII are usually found in lipid rafts, which are cholesterol-rich and sphingolipid-rich, tightly-packed microdomains of the cell membrane.
  • Furthermore, cellular localization of collagen XXIII was determined by immunofluorescence staining, using an antibody that recognizes the carboxyl terminus of the protein.
  • Collagen XXIII plays a role as a biomarker for detection and recurrence of NCLSC cells (non-small cell lung carcinoma) and the reappearance of prostate cancer.
  • For that reason, the shedding process of collagen XXIII has been described as a selective proteolysis, carried out principally by furin, although there are other enzymes, like serine and cysteine proteases, which are able to shed the molecule too.
  • In case that these molecules lose the lipid raft protection (i.e. when membrane cholesterol levels decrease) furin proteases can act, cleaving the protein right outside the cell, releasing the shed form of collagen XXIII directly to the extracellular matrix.
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