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FKBP10  -  FK506 binding protein 10, 65 kDa

Homo sapiens

Synonyms: 65 kDa FK506-binding protein, 65 kDa FKBP, FK506-binding protein 10, FKBP-10, FKBP-65, ...
 
 
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Disease relevance of FKBP10

 

High impact information on FKBP10

 

Chemical compound and disease context of FKBP10

  • To test the hypothesis that FKBP65 is upregulated at times when extracellular matrix proteins are being actively synthesized and assembled, adult mice were treated with bleomycin to cause reinitiation of matrix protein production during the ensuing development of pulmonary fibrosis [1].
 

Biological context of FKBP10

  • Unlike any other FKBP characterized so far, FKBP65 is developmentally regulated and may be intimately involved in organogenesis [4].
  • Using human lung fibroblast cultures, we showed that FKBP65 does not undergo the unfolded protein response, a response associated with an upregulation of resident ER proteins that occurs after increased ER stress [1].
  • Mouse Fkbp10 contains 10 exons and 9 introns encompassing 8.5 kb [4].
  • Cellular localization and glycosylation studies revealed the hFKBP65 protein to be localized in the endoplasmic reticulum, and to be N-glycosylated [2].
 

Anatomical context of FKBP10

  • AFKBP65 (65-kDa FK506-binding protein) is an endoplasmic reticulum (ER)-localized peptidyl-prolyl cis-trans isomerase predicted to play a role in the folding and trafficking of secretory proteins [1].
 

Associations of FKBP10 with chemical compounds

  • After bleomycin instillation, FKBP65 expression was reactivated in the lung with a pattern similar to that observed for tropoelastin and type I collagen [1].
 

Other interactions of FKBP10

  • RbFKBP52, like HuFKBP52, is made up of 10 exons and 9 introns, a feature shared with other large immunophilins such as FKBP65 and Cyclophilin 40, and which appears widely conserved [5].
 

Analytical, diagnostic and therapeutic context of FKBP10

  • Western blot analysis of matched tumors and normal mucosa supported the finding of increased hFKBP65 expression in tumors compared with normal mucosa, in addition to identifying the molecular mass of hFKBP65 to approximately 72 kDa [2].

References

  1. Developmental regulation and coordinate reexpression of FKBP65 with extracellular matrix proteins after lung injury suggest a specialized function for this endoplasmic reticulum immunophilin. Patterson, C.E., Abrams, W.R., Wolter, N.E., Rosenbloom, J., Davis, E.C. Cell Stress Chaperones (2005) [Pubmed]
  2. Human FK506 binding protein 65 is associated with colorectal cancer. Olesen, S.H., Christensen, L.L., Sørensen, F.B., Cabezón, T., Laurberg, S., Orntoft, T.F., Birkenkamp-Demtröder, K. Mol. Cell Proteomics (2005) [Pubmed]
  3. Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein. Patterson, C.E., Schaub, T., Coleman, E.J., Davis, E.C. Mol. Biol. Cell (2000) [Pubmed]
  4. Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family. Patterson, C.E., Gao, J., Rooney, A.P., Davis, E.C. Genomics (2002) [Pubmed]
  5. Promoter activity and gene structure of rabbit FKBP52. Massol, N., Lebeau, M.C., Schumacher, M., Baulieu, E.E. DNA Cell Biol. (2003) [Pubmed]
 
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