Disease relevance of PPIL2

• Therefore, Cyp60 may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor, such as cancer, human immunodeficiency virus infection, or rheumatoid arthritis [1].

High impact information on PPIL2

• Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60 [1].
• We have determined the solution structure of the two domain protein hPin1-(1-163) and its separately expressed PPIase domain (50-163) (hPin1PPIase) with an root mean square deviation of <0.5 A over backbone atoms using NMR [2].
• Also crucial were active site residues of CyPA, because rotamase-defective CyPA mutants failed to initiate signaling events [3].
• The association of PPIL2 with BACE expression and its requirement for Abeta production suggests new approaches to discover disease modifying agents for AD [4].
• In addition, hCyP-60 contains a tyrosine residue (Tyr 389) instead of a tryptophan residue found in most eukaryotic cyclophilins at a position important for cyclosporin binding [5].

Biological context of PPIL2

• Suppression of Cyp60 expression using RNA interference had an effect similar to that of cyclosporin A: reduction of cell surface expression of CD147 [1].

Anatomical context of PPIL2

• Mutation of this proline residue abrogated co-immunoprecipitation of CD147 and Cyp60 and reduced surface expression of CD147 on the plasma membrane [1].

Physical interactions of PPIL2

• We have identified a novel human cyclophilin (hCyP-60) which interacts with the proteinase inhibitor eglin c using the yeast two-hybrid system [5].

Other interactions of PPIL2

• These results suggest that Cyp60 plays an important role in the translocation of CD147 to the cell surface [1].

References