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Journal articles on the topic 'Immunophilins'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

De Leo, Sonia A., Nadia R. Zgajnar, Gisela I. Mazaira, Alejandra G. Erlejman, and Mario D. Galigniana. "Role of the Hsp90-Immunophilin Heterocomplex in Cancer Biology." Current Cancer Therapy Reviews 16, no. 1 (February 6, 2020): 19–28. http://dx.doi.org/10.2174/1573394715666190102120801.

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The identification of new factors that may function as cancer markers and become eventual pharmacologic targets is a challenge that may influence the management of tumor development and management. Recent discoveries connecting Hsp90-binding immunophilins with the regulation of signalling events that can modulate cancer progression transform this family of proteins in potential unconventional factors that may impact on the screening and diagnosis of malignant diseases. Immunophilins are molecular chaperones that group a family of intracellular receptors for immunosuppressive compounds. A subfamily of the immunophilin family is characterized by showing structural tetratricopeptide repeats, protein domains that are able to interact with the C-terminal end of the molecular chaperone Hsp90, and via the proper Hsp90-immunophilin complex, the biological properties of a number of client-proteins involved in cancer biology are modulated. Recent discoveries have demonstrated that two of the most studied members of this Hsp90- binding subfamily of immunophilins, FKBP51 and FKBP52, participate in several cellular processes such as apoptosis, carcinogenesis progression, and chemoresistance. While the expression levels of some members of the immunophilin family are affected in both cancer cell lines and human cancer tissues compared to normal samples, novel regulatory mechanisms have emerged during the last few years for several client-factors of immunophilins that are major players in cancer development and progression, among them steroid receptors, the transctiption factor NF-κB and the catalytic subunit of telomerase, hTERT. In this review, recent findings related to the biological properties of both iconic Hsp90-binding immunophilins, FKBP51 and FKBP52, are reviewed within the context of their interactions with those chaperoned client-factors. The potential roles of both immunophilins as potential cancer biomarkers and non-conventional pharmacologic targets for cancer treatment are discussed.

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2

Marks, A. R. "Cellular functions of immunophilins." Physiological Reviews 76, no. 3 (July 1, 1996): 631–49. http://dx.doi.org/10.1152/physrev.1996.76.3.631.

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Immunophilins are members of a highly conserved family of proteins all of which are cis-trans peptidyl-prolyl isomerases. The prototypic members of the immunophilin family, cyclophilin A and FKPB12, were discovered on the basis of their ability to bind and mediate the immunosuppressive effects of the drugs cyclosporin, FK506, and rapamycin. However, the prolyl isomerase activity of these proteins is not involved in any of the immunosuppressive effects. Indeed, despite the fact that all members of the family are prolyl isomerases, the cellular role of this enzymatic function has not been clearly defined. In many cases, immunophilins are widely expressed and are present at high levels in some tissues. Moreover, while the number of proteins that belong to the immunophilin family continues to grow, the natural cellular functions of all but a few remain obscure. An example where immunophilins do appear to have a defined cellular role, in the absence of immunosuppressive ligands, is the modulation of intracellular calcium release channel function by FKBP12 and FKBP12.6. In this case, FKBPs are integral parts of three types of calcium release channel complexes, skeletal and cardiac ryanodine receptors and the inositol 1,4,5-trisphosphate receptor. In each case, FKBPs modulate channel function possibly by enhancing the cooperativity between subunits.

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3

Schreiber, Stuart L., Jun Lui, Mark W. Albers, Michael K. Rosen, Robert F. Standaert, Thomas J. Wandless, and Patricia K. Somers. "Molecular Recognition of Immunophilins and Immunophilin-Ligand Complexes." Tetrahedron 48, no. 13 (March 1992): 2545–58. http://dx.doi.org/10.1016/s0040-4020(01)88520-3.

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4

Tomašić Paić, Ana, and Hrvoje Fulgosi. "Chloroplast immunophilins." Protoplasma 253, no. 2 (May 12, 2015): 249–58. http://dx.doi.org/10.1007/s00709-015-0828-z.

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5

Wiederrecht, Greg, and Felicia Etzkorn. "The immunophilins." Perspectives in Drug Discovery and Design 2, no. 1 (August 1994): 57–84. http://dx.doi.org/10.1007/bf02171737.

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6

Mesa, Annia, Jason A. Somarelli, and Rene J. Herrera. "Spliceosomal immunophilins." FEBS Letters 582, no. 16 (June 9, 2008): 2345–51. http://dx.doi.org/10.1016/j.febslet.2008.06.006.

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7

Nair, S. C., R. A. Rimerman, E. J. Toran, S. Chen, V. Prapapanich, R. N. Butts, and D. F. Smith. "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor." Molecular and Cellular Biology 17, no. 2 (February 1997): 594–603. http://dx.doi.org/10.1128/mcb.17.2.594.

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A cDNA for human FKBP51 has been cloned and sequenced, and protein products have been expressed in both in vitro and bacterial systems. The deduced amino acid sequence for human FKBP51 is 90% identical to sequences of recently described murine proteins and is 55% identical to the sequence of human FKBP52. Human FKBP51 mRNA is expressed in a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by FK506 but not cyclosporine. FKBP51 is the same as a previously described progesterone receptor-associated immunophilin that, similar to FKBP52 and cyclophilin 40, is an Hsp90-binding protein and appears in functionally mature steroid receptor complexes along with Hsp90 and p23. Each of the three receptor-associated immunophilins displays interactions with progesterone receptor that are more dynamic than Hsp90-receptor interactions. Whereas FKBP52 and FKBP51 compete about equally well for binding to Hsp90 in a purified system, FKBP51 accumulates preferentially in progesterone receptor complexes assembled in a cell-free system. This observation provides a precedent for differential interactions between Hsp90-associated immunophilins and target proteins such as steroid receptors.

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8

Norville, Isobel H., Katherine O'Shea, Mitali Sarkar-Tyson, Suxin Zheng, Richard W. Titball, Gabriele Varani, and Nicholas J. Harmer. "The structure of a Burkholderia pseudomallei immunophilin–inhibitor complex reveals new approaches to antimicrobial development." Biochemical Journal 437, no. 3 (July 13, 2011): 413–22. http://dx.doi.org/10.1042/bj20110345.

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Mips (macrophage infectivity potentiators) are a subset of immunophilins associated with virulence in a range of micro-organisms. These proteins possess peptidylprolyl isomerase activity and are inhibited by drugs including rapamycin and tacrolimus. We determined the structure of the Mip homologue [BpML1 (Burkholderia pseudomallei Mip-like protein 1)] from the human pathogen and biowarfare threat B. pseudomallei by NMR and X-ray crystallography. The crystal structure suggests that key catalytic residues in the BpML1 active site have unexpected conformational flexibility consistent with a role in catalysis. The structure further revealed BpML1 binding to a helical peptide, in a manner resembling the physiological interaction of human TGFβRI (transforming growth factor β receptor I) with the human immunophilin FKBP12 (FK506-binding protein 12). Furthermore, the structure of BpML1 bound to the class inhibitor cycloheximide N-ethylethanoate showed that this inhibitor mimics such a helical peptide, in contrast with the extended prolyl-peptide mimicking shown by inhibitors such as tacrolimus. We suggest that Mips, and potentially other bacterial immunophilins, participate in protein–protein interactions in addition to their peptidylprolyl isomerase activity, and that some roles of Mip proteins in virulence are independent of their peptidylprolyl isomerase activity.

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9

Hamilton, G. S., and J. P. Steiner. "Immunophilins: Beyond Immunosuppression." Journal of Medicinal Chemistry 41, no. 26 (December 1998): 5119–43. http://dx.doi.org/10.1021/jm980307x.

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10

Zgajnar, Nadia, Sonia De Leo, Cecilia Lotufo, Alejandra Erlejman, Graciela Piwien-Pilipuk, and Mario Galigniana. "Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52." Biomolecules 9, no. 2 (February 1, 2019): 52. http://dx.doi.org/10.3390/biom9020052.

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Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects.

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11

Han, Ruifang, Ying Wang, Chen Chen, Zhuo Zhao, and Huaifeng Mi. "De-Novo Cloning of FKBP23 cDNA from Pig ER Using Nested PCR." Zeitschrift für Naturforschung C 64, no. 3-4 (April 1, 2009): 297–302. http://dx.doi.org/10.1515/znc-2009-3-423.

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FK506 binding proteins (FKBPs) in cells are known as immunophilins. We have identifi ed and characterized a cDNA encoding an endoplasmic reticulum (ER) immunophilin, FKBP23, from pig liver by nested PCR. The predicted amino acid sequence of pig FKBP23 shows high identity to those of human FKBP23 and mouse FKBP23. It possesses a conserved FKBP-type peptidylprolyl cis-trans isomerase (PPIase) domain and EF-hand domain. We constructed a plasmid to express pFKBP23. Furthermore, we proved that the recombinant pFKBP23 can specifi cally bind to natural BiP, the main protein of the molecular chaperone Hsp70 in ER lumen; the binding is interrelated with the Ca2+ concentration just as the FKBP23 from mice.

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12

LENEGHAN, DARREN, and ANGUS BELL. "Immunophilin–protein interactions inPlasmodium falciparum." Parasitology 142, no. 11 (July 9, 2015): 1404–14. http://dx.doi.org/10.1017/s0031182015000803.

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SUMMARYImmunophilins comprise two protein families, cyclophilins (CYPs) and FK506-binding proteins (FKBPs), and are the major receptors for the immunosuppressive drugs cyclosporin A (CsA) and FK506 (tacrolimus), respectively. Most eukaryotic species have at least one immunophilin and some of them have been associated with pathogenesis of infectious or parasitic diseases or the action of antiparasitic drugs. The human malarial parasitePlasmodium falciparumhas 13 immunophilin or immunophilin-like genes but the functions of their products are unknown. We set out to identify the parasite proteins that interact with the major CYPs, PfCYP19A and PfCYP19B, and the FKBP, PfFKBP35, using a combination of co-immunoprecipitation and yeast two-hybrid screening. We identified a cohort of putative interacting partners and further investigation of some of these revealed potentially novel roles in parasite biology. We demonstrated that (i)P. falciparumCYPs interacted with the heat shock protein 70, (ii) treatment of parasites with CYP ligands disrupted transport of the rhoptry-associated protein 1, and (iii) PfFKBP35 interacted with parasite histones in a way that might modulate gene expression. These findings begin to elucidate the functions of immunophilins in malaria. Furthermore, the known antimalarial effects of CsA, FK506 and non-immunosuppressive derivatives of these immunophilin ligands could be mediated through these partner proteins.

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13

Calderon-Sanchez, E., M. Rodriguez-Moyano, and T. Smani. "Immunophilins and Cardiovascular Complications." Current Medicinal Chemistry 18, no. 35 (December 1, 2011): 5408–13. http://dx.doi.org/10.2174/092986711798194379.

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14

Lopez, E., J. A. Rosado, and P. C. Redondo. "Immunophilins and Thrombotic Disorders." Current Medicinal Chemistry 18, no. 35 (December 1, 2011): 5414–23. http://dx.doi.org/10.2174/092986711798194405.

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15

Gough, N. R. "Targeting Immunophilins for Neuroprotection." Science Signaling 1, no. 2 (January 8, 2008): ec18-ec18. http://dx.doi.org/10.1126/stke.12ec18.

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16

Snyder, Solomon H., and David M. Sabatini. "Immunophilins and nervous system." Nature Medicine 1, no. 1 (January 1995): 32–37. http://dx.doi.org/10.1038/nm0195-32.

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17

Cunningham, Earlene Brown. "An Inositolphosphate-Binding Immunophilin, IPBP12." Blood 94, no. 8 (October 15, 1999): 2778–89. http://dx.doi.org/10.1182/blood.v94.8.2778.420k10_2778_2789.

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A novel inositolphosphate-binding protein has been identified and shown to be an immunophilin. This protein, which was isolated from human erythrocyte membranes and from K562 (human erythroleukemia) cell membranes, has robust peptidylprolyl cis-trans isomerase activity that is strongly inhibited by nanomolar concentrations of FK506 or rapamycin, indicating a member of the FKBP (FK506-binding protein) class. However, unlike the cytosolic FKBP12, the isomerase activity of this membrane-associated immunophilin is strongly inhibited by nanomolar concentrations of inositol 1,4,5-trisphosphate (IP3), inositol 1,3,4,5-tetrakisphosphate (IP4), and phosphatidylinositol 4- and 4,5-phosphates, which are suggested to be physiological ligands. The demonstration of a single 12-kD protein that binds both IP4 or IP3and anti-FKBP12 provides strong support for the inositolphosphate-binding immunophilin having an apparent mass of 12 kD, and it is suggested that the protein might be called IPBP12 for 12-kD inositol phosphate binding protein. When an internal tryptic peptide derived from IPBP12 was sequenced, a sequence also present in human cytokeratin 10 was identified, suggesting a cytoskeletal localization for the immunophilin. While purifying IPBP12, it was found that it is immunoprecipitated with specific proteins that include a protein kinase and a phosphoprotein phosphatase. The latter is indicated to be phosphoprotein phosphatase 2A (PP-2A). It is suggested that immunophilins promote the assembly of multiprotein complexes that often include a protein kinase or a phosphoprotein phosphatase or both.

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18

Nigam, S. K., Y. J. Jin, M. J. Jin, K. T. Bush, B. E. Bierer, and S. J. Burakoff. "Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum." Biochemical Journal 294, no. 2 (September 1, 1993): 511–15. http://dx.doi.org/10.1042/bj2940511.

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The function of the immunophilins, FKBP 12 and FKBP 13, which are binding proteins for the immunosuppressant drug FK506 and rapamycin, remains poorly defined, although it has been suggested that immunophilins and immunophilin-like proteins may play a role in protein sorting/folding and intracellular calcium ion regulation. As a first step towards understanding the function of FKBP 13, we studied its subcellular localization by immunoblotting of well-defined subcellular fractions from a canine pancreatic homogenate and immunocytochemical analysis of an overexpressed cloned cDNA for FKBP 13. Whereas FKBP 12 fractionated entirely into the cytosol, virtually all FKBP 13 was found in the rough microsomal fraction which consisted of highly purified rough endoplasmic reticulum (ER), along with several well-characterized ER markers [the immunoglobulin heavy-chain binding protein (BiP), grp 94 and ribophorin I]. Moreover, FKBP 13 co-banded with the ER markers on isopycnic sucrose gradients. By immunofluorescence, the overexpressed cDNA for FKBP 13 in Hela cells gave an ER-staining pattern highly similar to that of known ER proteins. Addition of the ligand FK506 did not appear to alter the distribution of FKBP 13. Separation of the ER luminal contents and membrane revealed FKBP 13 to be a luminal ER protein. Since the lumen of the ER is where the folding of membrane and secreted proteins occurs, as well as a major site of intracellular calcium storage, it seems possible that FKBP 13 may be involved in one of these functions.

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19

Bram, R. J., D. T. Hung, P. K. Martin, S. L. Schreiber, and G. R. Crabtree. "Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location." Molecular and Cellular Biology 13, no. 8 (August 1993): 4760–69. http://dx.doi.org/10.1128/mcb.13.8.4760.

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The immunosuppressants cyclosporin A (CsA) and FK506 appear to block T-cell function by inhibiting the calcium-regulated phosphatase calcineurin. While multiple distinct intracellular receptors for these drugs (cyclophilins and FKBPs, collectively immunophilins) have been characterized, the functionally active ones have not been discerned. We found that overexpression of cyclophilin A or B or FKBP12 increased T-cell sensitivity to CsA or FK506, respectively, demonstrating that they are able to mediate the inhibitory effects of their respective immunosuppressants in vivo. In contrast, cyclophilin C, FKBP13, and FKBP25 had no effect. Direct comparison of the Ki of each drug-immunophilin complex for calcineurin in vitro revealed that although calcineurin binding was clearly necessary, it was not sufficient to explain the in vivo activity of the immunophilin. Subcellular localization was shown also to play a role, since gene deletions of cyclophilins B and C which changed their intracellular locations altered their activities significantly. Cyclophilin B has been shown previously to be located within calcium-containing intracellular vesicles; its ability to mediate CsA inhibition implies that certain components of the signal transduction machinery are also spatially restricted within the cell.

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20

Bram, R. J., D. T. Hung, P. K. Martin, S. L. Schreiber, and G. R. Crabtree. "Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location." Molecular and Cellular Biology 13, no. 8 (August 1993): 4760–69. http://dx.doi.org/10.1128/mcb.13.8.4760-4769.1993.

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The immunosuppressants cyclosporin A (CsA) and FK506 appear to block T-cell function by inhibiting the calcium-regulated phosphatase calcineurin. While multiple distinct intracellular receptors for these drugs (cyclophilins and FKBPs, collectively immunophilins) have been characterized, the functionally active ones have not been discerned. We found that overexpression of cyclophilin A or B or FKBP12 increased T-cell sensitivity to CsA or FK506, respectively, demonstrating that they are able to mediate the inhibitory effects of their respective immunosuppressants in vivo. In contrast, cyclophilin C, FKBP13, and FKBP25 had no effect. Direct comparison of the Ki of each drug-immunophilin complex for calcineurin in vitro revealed that although calcineurin binding was clearly necessary, it was not sufficient to explain the in vivo activity of the immunophilin. Subcellular localization was shown also to play a role, since gene deletions of cyclophilins B and C which changed their intracellular locations altered their activities significantly. Cyclophilin B has been shown previously to be located within calcium-containing intracellular vesicles; its ability to mediate CsA inhibition implies that certain components of the signal transduction machinery are also spatially restricted within the cell.

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21

Harikishore, Amaravadhi, and Ho Sup Yoon. "Immunophilins: Structures, Mechanisms and Ligands." Current Molecular Pharmacology 9, no. 1 (December 7, 2015): 37–47. http://dx.doi.org/10.2174/1874467208666150519113427.

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22

Snyder, Solomon H., Michael M. Lai, and Patrick E. Burnett. "Immunophilins in the Nervous System." Neuron 21, no. 2 (August 1998): 283–94. http://dx.doi.org/10.1016/s0896-6273(00)80538-3.

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23

Hamilton, G. S., and J. P. Steiner. "ChemInform Abstract: Immunophilins: Beyond Immunosuppression." ChemInform 30, no. 15 (June 16, 2010): no. http://dx.doi.org/10.1002/chin.199915314.

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24

GALAT, Andrzej. "Peptidylproline cis-trans-isomerases: immunophilins." European Journal of Biochemistry 216, no. 3 (September 1993): 689–707. http://dx.doi.org/10.1111/j.1432-1033.1993.tb18189.x.

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25

Minder, D., J. Böni, J. Schüpbach, and H. Gehring. "Immunophilins and HIV-1 infection." Archives of Virology 147, no. 8 (August 2002): 1531–42. http://dx.doi.org/10.1007/s00705-002-0826-2.

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26

Fretz, Heinz, Mark W. Albers, Andrzej Galat, Robert F. Standaert, William S. Lane, Steven J. Burakoff, Barbara E. Bierer, and Stuart L. Schreiber. "Rapamycin and FK506 binding proteins (immunophilins)." Journal of the American Chemical Society 113, no. 4 (February 1991): 1409–11. http://dx.doi.org/10.1021/ja00004a051.

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27

Davis, Diane L., Jayasimha N. Murthy, and Steven J. Soldin. "Biochemical characterization of the minor immunophilins." Clinical Biochemistry 33, no. 2 (March 2000): 81–87. http://dx.doi.org/10.1016/s0009-9120(99)00100-9.

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28

Ivery, Michael T. G. "Immunophilins: Switched on protein binding domains?" Medicinal Research Reviews 20, no. 6 (2000): 452–84. http://dx.doi.org/10.1002/1098-1128(200011)20:6<452::aid-med2>3.0.co;2-6.

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29

Stein, Ross L. "Exploring the catalytic activity of immunophilins." Current Biology 1, no. 4 (August 1991): 234–36. http://dx.doi.org/10.1016/0960-9822(91)90067-7.

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30

Barik, S. "Immunophilins: for the love of proteins." Cellular and Molecular Life Sciences 63, no. 24 (October 31, 2006): 2889–900. http://dx.doi.org/10.1007/s00018-006-6215-3.

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31

Dawson, Ted M. "Immunosuppressants, immunophilins, and the nervous system." Annals of Neurology 40, no. 4 (October 1996): 559–60. http://dx.doi.org/10.1002/ana.410400403.

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32

Munn, Kirsteen, and Ruth Steward. "The shut-down Gene of Drosophila melanogaster Encodes a Novel FK506-Binding Protein Essential for the Formation of Germline Cysts During Oogenesis." Genetics 156, no. 1 (September 1, 2000): 245–56. http://dx.doi.org/10.1093/genetics/156.1.245.

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Abstract In Drosophila melanogaster, the process of oogenesis is initiated with the asymmetric division of a germline stem cell. This division results in the self-renewal of the stem cell and the generation of a daughter cell that undergoes four successive mitotic divisions to produce a germline cyst of 16 cells. Here, we show that shut-down is essential for the normal function of the germline stem cells. Analysis of weak loss-of-function alleles confirms that shut-down is also required at later stages of oogenesis. Clonal analysis indicates that shut-down functions autonomously in the germline. Using a positional cloning approach, we have isolated the shut-down gene. Consistent with its function, the RNA and protein are strongly expressed in the germline stem cells and in 16-cell cysts. The RNA is also present in the germ cells throughout embryogenesis. shut-down encodes a novel Drosophila protein similar to the heat-shock protein-binding immunophilins. Like immunophilins, Shut-down contains an FK506-binding protein domain and a tetratricopeptide repeat. In plants, high-molecular-weight immunophilins have been shown to regulate cell divisions in the root meristem in response to extracellular signals. Our results suggest that shut-down may regulate germ cell divisions in the germarium.

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33

Periyasamy, Sumudra, Manya Warrier, Manoranjani P. M. Tillekeratne, Weinian Shou, and Edwin R. Sanchez. "The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms." Endocrinology 148, no. 10 (October 1, 2007): 4716–26. http://dx.doi.org/10.1210/en.2007-0145.

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The androgen receptor (AR) contributes to growth of prostate cancer even under conditions of androgen ablation. Thus, new strategies to target AR activity are needed. The AR interacts with the immunophilin FK506-binding protein 52 (FKBP52), and studies in the FKBP52 knockout mouse have shown that this protein is essential to AR activity in the prostate. Therefore, we tested whether the immunophilin ligand FK506 affected AR activity in prostate cancer cell lines. We also tested the hypothesis that the AR interacts with another immunophilin, cyclophilin 40 (Cyp40), and is regulated by its cognate ligand cyclosporin A (CsA). We show that levels of FKBP52, FKBP51, Cyp40, and a related co-chaperone PP5 were much higher in prostate cancer cells lines [(LNCaP), PC-3, and DU145] compared with primary prostate cells, and that the AR of LNCaP cells can interact with Cyp40. In the absence of androgen, CsA caused inhibition of cell growth in the AR-positive LNCaP and AR-negative PC-3 and DU145 cell lines. Interestingly, FK506 only inhibited LNCaP cells, suggesting a dependence on the AR for this effect. Both CsA and FK506 inhibited growth without inducing apoptosis. In LNCaP cells, CsA completely blocked androgen-stimulated growth, whereas FK506 was partially effective. Further studies in LNCaP cells revealed that CsA and FK506 were able to block or attenuate several stages of AR signaling, including hormone binding, nuclear translocation, and activity at several AR-responsive reporter and endogenous genes. These findings provide the first evidence that CsA and FK506 can negatively modulate proliferation of prostate cells in vitro. Immunophilins may now serve as new targets to disrupt AR-mediated prostate cancer growth.

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34

Hong, Jiyoung, Sung Tae Kim, Susanne Tranguch, David F. Smith, and Sudhansu K. Dey. "Deficiency of co-chaperone immunophilin FKBP52 compromises sperm fertilizing capacity." Reproduction 133, no. 2 (February 2007): 395–403. http://dx.doi.org/10.1530/rep-06-0180.

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FKBP52 is a member of the FK506-binding family of immunophilins and serves as a co-chaperone for steroid hormone nuclear receptors to govern appropriate hormone action in target tissues. Male mice missingFkbp52are infertile, and this infertility has been ascribed to compromised sensitivity of the anterior prostate, external genitalia, and other accessory sex organs to androgen. Here, we show additional defects contributing to infertility. We found that epididymalFkbp52−/−sperm are sparse often with aberrant morphology, and they have reduced fertilizing capacity. This phenotype, initially observed in null males on a C57BL/6/129 background, is also maintained on a CD1 background. Expression studies show that while FKBP52 and androgen receptor are co-expressed in similar cell types in the epididymis, FKBP52 is also present in epididymal sperm flagella. Collectively, our results suggest that reduced number and abnormal morphology contribute to compromised fertilizing capacity ofFkbp52−/−sperm. This study is clinically relevant because unraveling the role of immunophilin signaling in male fertility will help identify new targets for male contraceptives and/or alleviate male infertility.

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35

Graziani, Francesca, Laura Aldegheri, and Georg C. Terstappen. "High Throughput Scintillation Proximity Assay for the Identification of FKBP-12 Ligands." Journal of Biomolecular Screening 4, no. 1 (February 1999): 3–7. http://dx.doi.org/10.1177/108705719900400102.

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A high throughput scintillation proximity assay (SPA) was developed to identify novel ligands of FKBP-12, an immunophilin with peptidyl prolyl isomerase (rotamase) activity. Recombinant histidine-tagged FKBP-12 was expressed in Escherichia coli, purified by metal ion affinity chromatography, and immobilized to SPA beads by an antibody that recognizes the histidine tag of the recombinant protein. Using 1 nM [3H] FK506, a well-known macrolid ligand of FKBP-12, specific binding was saturable and accounted for 95% of total binding. Analysis of saturation and homologous displacement isotherms indicated the existence of a single binding site with a KD value of 1.6 nM. The specificity of [3H] FK506 binding was demonstrated in displacement experiments and showed that rapamycin, another macrolid, was as active as FK506 (IC50 of 3.5 and 3.2 nM, respectively), whereas GPI-1046, a prototype of small molecular compounds with neurotrophic properties and affinity for FKBP-type immunophilins, was more than 1000-fold less active. The high signal-to-noise ratio of 30, together with small standard deviations, makes this novel assay well suited for automated high throughput screening.

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Avramut, M., and C. Achim. "Immunophilins in Nervous System Degeneration and Regeneration." Current Topics in Medicinal Chemistry 3, no. 12 (August 1, 2003): 1376–82. http://dx.doi.org/10.2174/1568026033451871.

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Dornan, Jacqueline, Paul Taylor, and Malcolm Walkinshaw. "Structures of Immunophilins and their Ligand Complexes." Current Topics in Medicinal Chemistry 3, no. 12 (August 1, 2003): 1392–409. http://dx.doi.org/10.2174/1568026033451899.

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Lehnart, Stephan, Fannie Huang, Steven Marx, and Andrew Marks. "Immunophilins and Coupled Gating of Ryanodine Receptors." Current Topics in Medicinal Chemistry 3, no. 12 (August 1, 2003): 1383–91. http://dx.doi.org/10.2174/1568026033451907.

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Adams, Brian, Alla Musiyenko, Rajinder Kumar, and Sailen Barik. "A Novel Class of Dual-family Immunophilins." Journal of Biological Chemistry 280, no. 26 (April 21, 2005): 24308–14. http://dx.doi.org/10.1074/jbc.m500990200.

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Fruman, David A., Steven J. Burakoff, and Barbara E. Bierer. "Immunophilins in protein folding and immunosuppression 1." FASEB Journal 8, no. 6 (April 1994): 391–400. http://dx.doi.org/10.1096/fasebj.8.6.7513288.

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Sinkins, William G., Monu Goel, Mark Estacion, and William P. Schilling. "Association of Immunophilins with Mammalian TRPC Channels." Journal of Biological Chemistry 279, no. 33 (June 15, 2004): 34521–29. http://dx.doi.org/10.1074/jbc.m401156200.

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42

Somarelli, J. A., J. L. Coll, A. Velandia, L. Martinez, and R. J. Herrera. "Characterization of immunophilins in the silkmothBombyx mori." Archives of Insect Biochemistry and Physiology 65, no. 4 (2007): 195–209. http://dx.doi.org/10.1002/arch.20177.

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Wang, Jingjing, Qunfang Weng, and Qiongbo Hu. "Effects of Destruxin A on Silkworm’s Immunophilins." Toxins 11, no. 6 (June 18, 2019): 349. http://dx.doi.org/10.3390/toxins11060349.

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Destruxin A (DA), a major secondary metabolite of Metarhizium anisopliae, has anti-immunity to insects. However, the detailed mechanism and its interactions with target proteins are elusive. Previously, three immunophilins, peptidyl–prolyl cis–trans isomerase (BmPPI), FK506 binding-protein 45 (BmFKBP45) and BmFKBP59 homologue, were isolated from the silkworm, Bombyx mori Bm12 cell line following treatment with DA, which suggested that these proteins were possible DA-binding proteins. To validate the interaction between DA and the three immunophilins, we performed bio-layer interferometry (BLI) assay, and the results showed that DA has interaction with BmPPI, whose affinity constant value is 1.98 × 10−3 M and which has no affinity with FKBP45 and FKBP59 homologue in vitro. Furthermore, we investigated the affinity between DA and human PPI protein (HsPPIA) and the affinity constant (KD) value is 2.22 × 10−3 M. Additionally, we compared the effects of silkworm and human PPI proteins produced by DA and immunosuppressants, cyclosporine A (CsA), and tacrolimus (FK506), by employing I2H (insect two-hybrid) in the SF-9 cell line. The results indicated that in silkworm, the effects created by DA and CsA were stronger than FK506. Furthermore, the effects created by DA in silkworm were stronger than those in humans. This study will offer new thinking to elucidate the molecular mechanism of DA in the immunity system of insects.

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Davis, D. L., J. N. Murthy, and S. J. Soldin. "FURTHER BIOCHEMICAL CHARACTERIZATION OF THE MINOR IMMUNOPHILINS." Therapeutic Drug Monitoring 21, no. 4 (August 1999): 478. http://dx.doi.org/10.1097/00007691-199908000-00208.

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Romano, Patrick, Julie Gray, Peter Horton, and Sheng Luan. "Plant immunophilins: functional versatility beyond protein maturation." New Phytologist 166, no. 3 (March 14, 2005): 753–69. http://dx.doi.org/10.1111/j.1469-8137.2005.01373.x.

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Sabatini, David M., Michael M. Lai, and Solomon H. Snyder. "Neural roles of immunophilins and their ligands." Molecular Neurobiology 15, no. 2 (October 1997): 223–39. http://dx.doi.org/10.1007/bf02740635.

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Hopkins, Sam, and Philippe A. Gallay. "The role of immunophilins in viral infection." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 10 (October 2015): 2103–10. http://dx.doi.org/10.1016/j.bbagen.2014.11.011.

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McKeen, Hayley D., Kerry McAlpine, Andrea Valentine, Derek J. Quinn, Keeva McClelland, Christopher Byrne, Martin O'Rourke, et al. "A Novel FK506-Like Binding Protein Interacts with the Glucocorticoid Receptor and Regulates Steroid Receptor Signaling." Endocrinology 149, no. 11 (July 31, 2008): 5724–34. http://dx.doi.org/10.1210/en.2008-0168.

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FKBP-like (FKBPL) protein is a novel immunophilin-like protein that plays a role in the cellular stress response. Its three tetratricopeptide repeat motifs are homologous to the heat shock protein 90 interaction sites of other immunophilins that have roles in steroid hormone receptor signaling. In this study, using biomolecular complementation and coimmunoprecipitation techniques, we show that FKBPL also colocalizes and interacts with the components of the heat shock protein 90-glucocorticoid receptor (GR) complex and demonstrate that the PPIase domain of FKBPL is important for the interaction between this complex and the dynein motor protein, dynamitin. Treatment of DU145 cells with the GR ligand, dexamethasone, induced a rapid and coordinated translocation of both GR and FKBPL to the nucleus; this response was perturbed when FKBPL was knocked down with a targeted small interfering RNA. Furthermore, overexpression of FKBPL increased GR protein levels and transactivation of a luciferase reporter gene in response to dexamethasone in DU145 cells. However, these responses were cell line dependent. In summary, these data suggest that FKBPL can be classed as a new member of the FKBP protein family with a role in steroid receptor complexes and signaling.

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Lagadari, Mariana, Sonia A. De Leo, Maria F. Camisay, Mario D. Galigniana, and Alejandra G. Erlejman. "Regulation of NF-κB signalling cascade by immunophilins." Current Molecular Pharmacology 9, no. 2 (December 7, 2015): 99–108. http://dx.doi.org/10.2174/1874467208666150519113833.

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Cao, Weihuan, and Mary Konsolaki. "FKBP immunophilins and Alzheimer’s disease: A chaperoned affair." Journal of Biosciences 36, no. 3 (July 23, 2011): 493–98. http://dx.doi.org/10.1007/s12038-011-9080-7.

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