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Journal articles on the topic 'Immunophilins'

Author: Grafiati

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 subfa

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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 clearl

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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

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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

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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

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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

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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

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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)

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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. Whe

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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, cyclophil

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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, cyclophil

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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 germlin

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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 cognat

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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 obser

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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 indic

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36

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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37

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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38

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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39

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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40

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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41

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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43

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)

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44

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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45

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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46

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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47

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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48

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

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49

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

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50

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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