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Bibliographies thématiques / Pregnenolone-16-a-carbonitrile

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Littérature scientifique sur le sujet « Pregnenolone-16-a-carbonitrile »

Auteur : Grafiati

Publié le 7 juin 2025

Mis à jour le 2 août 2025

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Articles de revues sur le sujet "Pregnenolone-16-a-carbonitrile"

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Konzack, Anja, Mikko Karpale, Tomáš Smutný, et al. "LIM and SH3 protein 2 (Lasp2) is a novel pregnane X receptor target gene in mouse liver." Molecular Pharmacology 107, no. 3 (2025): 100019. https://doi.org/10.5281/zenodo.14959048.

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LIM and Src homology 3 (SH3) protein 2 (LASP2) is a small focal adhesion protein first identified as a splice variant of the nebulette gene (<em>Nebl</em>). As the newest member of the nebulin protein family, the regulation and function of LASP2 remain largely unknown. Our previous RNA-sequencing results identified <em>Nebl</em> as one of the most highly induced genes in the mouse liver in response to the activation of pregnane X receptor (PXR). In this study, we investigated this phenomenon further and show that PXR induces <em>Lasp2</em> instead of <em>Nebl</em>, whi

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Kapitulnik, J., J. P. Hardwick, J. D. Ostrow, C. C. Webster, S. S. Park, and H. V. Gelboin. "Increase in a specific cytochrome P-450 isoenzyme in the liver of congenitally jaundiced Gunn rats." Biochemical Journal 242, no. 1 (1987): 297–300. http://dx.doi.org/10.1042/bj2420297.

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Congenitally jaundiced (jj) Gunn rats had a greater hepatic microsomal content of a cytochrome P-450 isoenzyme, P-450c, than did the non-jaundiced (Jj) rats. No differences in content of P-450b, P-450d and pregnenolone-16 alpha-carbonitrile-induced (PCN) P-450 were found between jj and Jj rats. This is the first demonstration of a constitutive increase in a specific cytochrome P-450 isoenzyme in association with a genetic defect.

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Hostetler, K. A., S. A. Wrighton, P. Kremers, and P. S. Guzelian. "Immunochemical evidence for multiple steroid-inducible hepatic cytochromes P-450 in the rat." Biochemical Journal 245, no. 1 (1987): 27–33. http://dx.doi.org/10.1042/bj2450027.

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It has been established that there are glucocorticoid-inducible hepatic cytochromes P-450 in the rat (P-450p), the rabbit (LM3c) and man (HLp) which share extensive structural, functional and regulatory features. We prepared immunochemical probes to P-450p and identified a unique monoclonal antibody, 1G8, that recognizes purified P-450p, but neither purified LM3c nor HLp, on immunoblot analysis. The N-terminal amino acid sequence of purified samples of P-450p was identical with that previously reported for P-450PCN1 [Gonzalez, Nebert, Hardwick & Kasper (1985) J. Biol. Chem. 260, 7435-7441]

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Gonzalez, F. J., D. W. Nebert, J. P. Hardwick, and C. B. Kasper. "Complete cDNA and protein sequence of a pregnenolone 16 alpha-carbonitrile-induced cytochrome P-450. A representative of a new gene family." Journal of Biological Chemistry 260, no. 12 (1985): 7435–41. http://dx.doi.org/10.1016/s0021-9258(17)39626-6.

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Wolf, C. R., S. Seilman, F. Oesch, R. T. Mayer, and M. D. Burke. "Multiple forms of cytochrome P-450 related to forms induced marginally by phenobarbital. Differences in structure and in the metabolism of alkoxyresorufins." Biochemical Journal 240, no. 1 (1986): 27–33. http://dx.doi.org/10.1042/bj2400027.

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The properties of five structurally related forms of cytochrome P-450 (PB1a, PB1b, PB2a, PB2b and PB2d) isolated from rats treated with phenobarbital have been compared with two forms isolated previously now termed ‘PB1c’ and ‘PB2c’ These enzymes were characterized by their marginal inducibility by phenobarbital and are clearly distinguishable from the major phenobarbital-inducible proteins. PB1a and PB1b differed in Mr (52,700 and 52,900), absorption spectra and papain-proteolysis fragments. However, they had identical N-terminal sequences. PB2a, PB2b and PB2d had apparent Mr values of 52,900

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Shimada, T., and F. P. Guengerich. "Participation of a rat liver cytochrome P-450 induced by pregnenolone 16 alpha-carbonitrile and other compounds in the 4-hydroxylation of mephenytoin." Molecular Pharmacology 28, no. 2 (1985): 215–19. https://doi.org/10.1016/s0026-895x(25)13510-4.

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Barnes, T. S., P. M. Shaw, M. D. Burke та W. T. Melvin. "Monoclonal antibodies against human cytochrome P-450 recognizing different pregnenolone 16α-carbonitrile-inducible rat cytochromes P-450". Biochemical Journal 248, № 1 (1987): 301–4. http://dx.doi.org/10.1042/bj2480301.

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Six murine monoclonal antibodies against human hepatic cytochrome P-450 have been raised, using human liver microsomes (microsomal fractions) or semi-purified human cytochrome P-450 as immunogen. All six antibodies recognized the same highly purified of human liver cytochrome P-450 of molecular mass 53 kDa and gave rise to a single band at 53 kDa on immunoblots of human liver microsomes from 11 individuals. The antibodies also recognized proteins at 52 kDa and 54 kDa on immunoblots of control and induced male-rat liver microsomes, showing four different banding patterns. Antibodies HL4 and HP1

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Salamat, Julia M., Elizabeth M. Ayala, Chen-Che J. Huang, et al. "Pregnenolone 16-Alpha Carbonitrile, an Agonist of Rodent Pregnane X Receptor, Regulates Testosterone Biosynthesis in Rodent Leydig Cells." Journal of Xenobiotics 14, no. 3 (2024): 1256–67. http://dx.doi.org/10.3390/jox14030071.

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Leydig cells (LCs) in the testes produce the male sex hormone testosterone (T). Several xenobiotics, including clinical drugs, supplements, and environmental chemicals, are known to disrupt T homeostasis. Notably, some of these xenobiotics are known to activate the pregnane X receptor (PXR), a ligand-dependent nuclear receptor. However, it is currently unknown whether PXR is expressed in LCs and whether PXR activation alters T synthesis in rodent LCs. Therefore, in this study, we sought to determine whether PXR is expressed in rodent LCs and whether pregnenolone 16-alpha carbonitrile (PCN), th

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Gonzalez, F. J., B. J. Song, and J. P. Hardwick. "Pregnenolone 16 alpha-carbonitrile-inducible P-450 gene family: gene conversion and differential regulation." Molecular and Cellular Biology 6, no. 8 (1986): 2969–76. http://dx.doi.org/10.1128/mcb.6.8.2969-2976.1986.

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A cytochrome P-450 cDNA clone, designated pP450PCN2, homologous to the previously characterized pregnenolone 16 alpha-carbonitrile (PCN)-induced P-450 cDNA (pP450PCN1; F. J. Gonzalez, D. W. Nebert, J. P. Hardwick, and C. B. Kasper, J. Biol. Chem. 260:7435-7441), was isolated from a rat liver cDNA expression library by use of a polyclonal anti-P450PCN1 antibody. This P-450 cDNA contains 2,014 base pairs and yields an open reading frame of a protein consisting of 504 amino acids (Mr = 57,760). P450PCN2 cDNA and protein shared 90% nucleotide and 89% amino acid similarity with P450PCN1 cDNA and pr

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Gonzalez, F. J., B. J. Song, and J. P. Hardwick. "Pregnenolone 16 alpha-carbonitrile-inducible P-450 gene family: gene conversion and differential regulation." Molecular and Cellular Biology 6, no. 8 (1986): 2969–76. http://dx.doi.org/10.1128/mcb.6.8.2969.

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A cytochrome P-450 cDNA clone, designated pP450PCN2, homologous to the previously characterized pregnenolone 16 alpha-carbonitrile (PCN)-induced P-450 cDNA (pP450PCN1; F. J. Gonzalez, D. W. Nebert, J. P. Hardwick, and C. B. Kasper, J. Biol. Chem. 260:7435-7441), was isolated from a rat liver cDNA expression library by use of a polyclonal anti-P450PCN1 antibody. This P-450 cDNA contains 2,014 base pairs and yields an open reading frame of a protein consisting of 504 amino acids (Mr = 57,760). P450PCN2 cDNA and protein shared 90% nucleotide and 89% amino acid similarity with P450PCN1 cDNA and pr

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