Reference

Cyclosporin A and FK506 mediate differential effects on T cell activation in vivo

Cyclosporin A and FK506 mediate differential effects on T cell activation in vivo. Bishop, D. Keith; Li, Wenhua (Sch. Med., Univ. Utah, Salt Lake City, UT 84132, USA). J. Immunol., 148(4), 1049-54 (English) 1992. CODEN: JOIMA3. ISSN: 0022-1767. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Modified limiting diln. anal. techniques were used to evaluate the effects of the immunosuppressants cyclosporin A (CsA) and FK506 on alloantigen-induced T cell activation in vivo. Treatment of sponge matrix allograft recipients with either CsA or FK506 inhibited lymphocytic infiltration of the allograft, a process thought to be dependent on local lymphokine prodn. In addn., both immunosuppressants markedly reduced the abs. no. of lymphocytes recovered from the draining lymph nodes (LN) and prevented CTL activation in the LN. However, Ag-primed helper T lymphocytes (HTL) were present in the draining LN of sponge allograft recipients treated with CsA, but not in recipients treated with FK506. T cells depletion expts. were performed to det. the phenotype of primed HTL in the LN of untreated and CsA-treated sponge allograft recipients. In untreated sponge allograft recipients, CD4+ and CD8+ Ag-primed HTL were present in the draining LN in equiv.In this experiment, several chemicals are used like 59865-13-3 and 104987-11-3 nos. In contrast, the majority of primed HTL in the LN of CsA-treated sponge allograft recipients were CD8+, rather than CD4+ T cells. These observations indicate that CsA and FK506 exert distinct in vivo effects at the level of HTL priming, and CD4+ and CD8+ HTL exhibit differential sensitivity to CsA in vivo. .

FK-506 binding protein from Tolypocladium inflatum: resistance of FKBP/FK-506 complex against proteolysis

FK-506 binding protein from Tolypocladium inflatum: resistance of FKBP/FK-506 complex against proteolysis. Lee, Chan; Hoffmann, Kai; Zocher, Rainer (Inst. Biochem. Mol. Biol., Tech. Univ. Berlin, Berlin D-1000/10, Germany). Biochem. Biophys. Res. Commun., 182(3), 1282-7 (English) 1992. CODEN: BBRCA9. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) A 12-kDa peptidyl-prolyl-cis/trans-isomerase was purified 225-fold to homogeneity from the cyclosporin producing fungus T. inflatum. The enzyme is highly sensitive to the immunosuppressant FK-506 but not to cyclosporin and thus belongs to the class of FK-506 binding proteins (FKBP).In this experiment, several chemicals are used like 104987-11-3 Interestingly the FKBP/FK-506 complex is resistant to proteolytic digestion by the endoproteases GluC and LysC, in contrast to the free FKBP, which is readily cleaved by these proteases. This protection may play a role in the effects of FK-506 in the living cell. .