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High-affinity receptor proteins in the cytoplasm that combine with immunosuppressant drugs leading to rotamase inhibition and, in T cells, thus to interruption of cell activation.
[immune + G. philos, fond, + in]
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Other techniques or approaches include nerve grafting (11), nerve reconstruction (12), pharmacological neuromodulation using immunophilins (13), neuroprotection using erythropoietin (14), electro-stimulation of the CN or pelvic ganglion (15), regulation of FK506-binding protein (16) and transferring of the herpes simplex virus vector (17).
In addition, the immunophilins FKBP family was known to be involved in meiosis, calcium homeostasis, clathrin-coated vesicles, and membrane fusions (Raudsepp et al., 2012).
CsA and FK506 bind to different immunophilins as cyclophilins and FK-binding proteins, respectively.
Peptidylproline cis-trans-isomerases: immunophilins. Eur J Biochem 1993; 216: 689-707.
Rapamycin binding to immunophilins, such as FKBP12 (FK binding protein, 12kDa), forms an FKBP12-rapamycin complex.
Cyclophilins (CYPs) are a subgroup of a large family of proteins called immunophilins, with a peptidyl-prolyl cistrans isomerase (PPIase) activity [16].
[20] Rapamycin belongs to the class of macrocyclic immunosuppressive drugs that are active only when bound to immunophilins. Intracellularly, rapamycin binds to FKBP12 (FK binding protein 12 kDa), an immunophilin and forms a complex FKBP12-rapamycin.
foeminea are histones which are normally restricted to the nucleus and involved in chromosome organization, Granule-bound starch synthase which synthesizes amylose in the chloroplast, BIP isoform A which is a molecular chaperone located on the endoplasmic reticulum, and immunophilins such as peptidyl-prolyl cis-trans isomerase which are found in a number of locations within the cell.
Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands.
FKBP52 was initially discovered as a cochaperone of steroid receptor heterocomplexes [19, 20] and is a member of the FK506binding protein (FKBP) of immunophilins. FKBP52, which possesses a chaperone function, has a PPIase domain also called FK506-binding domain (FKBD), composed of the first 138 amino acids from the N-terminal, exhibits peptidylprolyl isomerase (PPIase) activity, and plays an important role in regulating tau proteins.