Disease relevance of FKBP10

• When fibroblasts were treated with transforming growth factor (TGF)-beta1, which is upregulated during the development of pulmonary fibrosis and known to induce matrix production, FKBP65 expression and synthesis was also increased [1].
• In conclusion, the protein hFKBP65 is associated with colorectal cancer, and we hypothesize the protein to be involved in fibroblast and transformed epithelial cell-specific protein synthesis in the endoplasmic reticulum [2].
• Analysis of 31 colorectal adenocarcinomas and 14 normal colorectal mucosa by RealTime PCR for hFKBP10 showed a significant up-regulation in tumors, when compared with normal mucosa [2].

High impact information on FKBP10

• Using subcellular fractionation, Triton X-114 phase separation, protease protection assays, and immunofluorescence microscopy (IF), we have identified that FKBP65 is contained within the lumen of the endoplasmic reticulum (ER) [3].
• Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein [3].
• Taken together, these results support an ER-localized FKBP65-tropoelastin interaction that occurs specifically during growth and development of tissues [3].
• Immunohistochemical localization of FKBP65 in developing lung showed strong staining of vascular and airway smooth muscle cells [3].
• Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family [4].

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