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Abstract:

Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms and subcellular compartments, and their amino acid sequences are conserved phylogenetically. Immunophilins possess the ability to function as molecular chaperones favoring the proper folding and biological regulation of their biological actions. Their ability to interact via their TPR domains with the 90-kDa heat-shock protein, and through this chaperone, with several signalling cascade factors is of particular importance. Among the family members, the highly homologous proteins FKBP51 and FKBP52 were first characterized due to their ability to interact with steroid hormone receptors. Since then, much progress has been made in understanding the mechanisms by which they regulate receptor signaling and the resulting roles they play not only in endocrine processes, but also in cell architecture, neurodifferentiation, and tumor progression. In this article we review the most relevant features of these two immunophilins and their potential as pharmacologic targets. © 2014 Bentham Science Publishers.

Registro:

Documento: Artículo
Título:Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
Autor:Erlejman, A.G.; Lagadari, M.; Harris, D.C.; Cox, M.B.; Galigniana, M.D.
Filiación:Departamento de Química Biológica/IQUIBICEN, Universidad de Buenos Aires, Argentina
Instituto de Biología Medicina Experimental/CONICET, Buenos Aires, Argentina
The Border Biomedical Research Center and Department of Biological Sciences, University of Texas at El Paso, El Paso, TX, United States
Palabras clave:FK506; FKBP51; FKBP52; Hsp70; Hsp90; Immunophilin; Peptidylprolyl isomerase; TPR; chaperone; cyclosporin A; fk 506 binding protein; heat shock protein 90; immunophilin; peptidylprolyl isomerase; proline rich protein; protein FKB52; protein FKBP51; protein S 100; rapamycin; tacrolimus; tau protein; unclassified drug; chaperone; fk 506 binding protein; steroid receptor; tacrolimus binding protein 4; tacrolimus binding protein 5; Alzheimer disease; article; breast cancer; cell growth; cell proliferation; complex formation; cytoskeleton; gene expression; gene overexpression; human; nerve cell differentiation; nonhuman; ovary cancer; protein assembly; protein binding; protein domain; protein expression; protein function; protein interaction; protein localization; protein phosphorylation; tetratricopeptide repeat; chemistry; metabolism; protein folding; protein tertiary structure; Humans; Molecular Chaperones; Protein Folding; Protein Structure, Tertiary; Receptors, Steroid; Tacrolimus Binding Proteins
Año:2014
Volumen:15
Número:3
Página de inicio:205
Página de fin:215
Título revista:Current Protein and Peptide Science
Título revista abreviado:Curr. Protein Pept. Sci.
ISSN:13892037
CODEN:CPPSC
CAS:cyclosporin A, 59865-13-3, 63798-73-2; peptidylprolyl isomerase, 95076-93-0; rapamycin, 53123-88-9; tacrolimus, 104987-11-3; Molecular Chaperones; Receptors, Steroid; tacrolimus binding protein 4; tacrolimus binding protein 5; Tacrolimus Binding Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman

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Citas:

---------- APA ----------
Erlejman, A.G., Lagadari, M., Harris, D.C., Cox, M.B. & Galigniana, M.D. (2014) . Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52. Current Protein and Peptide Science, 15(3), 205-215.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman [ ]
---------- CHICAGO ----------
Erlejman, A.G., Lagadari, M., Harris, D.C., Cox, M.B., Galigniana, M.D. "Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52" . Current Protein and Peptide Science 15, no. 3 (2014) : 205-215.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman [ ]
---------- MLA ----------
Erlejman, A.G., Lagadari, M., Harris, D.C., Cox, M.B., Galigniana, M.D. "Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52" . Current Protein and Peptide Science, vol. 15, no. 3, 2014, pp. 205-215.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman [ ]
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Erlejman, A.G., Lagadari, M., Harris, D.C., Cox, M.B., Galigniana, M.D. Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52. Curr. Protein Pept. Sci. 2014;15(3):205-215.
Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman [ ]