Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity 1 1Edited by M. Yaniv

We describe a novel interaction of human T cell cyclophilin18

Anja Jäschke; Huaifeng Mi; Maximilian Tropschug

2002

Scholarcy highlights

  • Cyclophilins define a family of proteins binding to the immunosuppressive drug cyclosporin A
  • We describe a novel interaction of human T cell cyclophilin
  • Abundant cytosolic human T cell cyclophilin18 binds to the thiol-specific antioxidant protein Aop and stimulates its enzymatic activity
  • The interaction of both proteins seem to be specific, since other peptidyl-prolyl cis-trans isomerase do not have any stimulatory effect on Aop
  • Due to its amino acid sequence derived from the cloned cDNA, Aop belongs to the TSA/aphC family of thiol-specific antioxidative enzymes Chae et al 1994, Santoro and Thiele 1997
  • One hundred and thirty-two patients had a final diagnosis made by ultrasound-guided core needle biopsy and did not undergo surgery
  • This study aimed to examine the diagnostic yield of fine needle aspiration cytology and ultrasound-guided core needle biopsy in the diagnosis of parotid neoplasia
  • We conclude that Prx glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling

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