Protein Never in Mitosis Gene A Interacting-1 (PIN1) regulates degradation of inducible nitric oxide synthase in endothelial cells
Abstract
The peptidyl-proline isomerase Protein Never in Mitosis Gene A Interacting-1 (PIN1) increases the level or activity of several transcription factors that can induce the inducible nitric oxide (NO) synthase (iNOS). PIN1 can also regulate mRNA and protein turnover. Here, the effect of depletion of PIN1 on induction of iNOS by Escherichia coli endotoxin (LPS) and interferon-gamma (IFNgamma) in murine aortic endothelial cells (MAEC) was determined. Suppression of PIN1 by 85% with small hairpin RNA enhanced the induction of NO and iNOS protein by LPS-IFNgamma. There was no effect on induction of iNOS mRNA, suggesting a posttranscriptional effect. The enhanced levels of iNOS protein were functionally significant since LPS-IFNgamma was cytotoxic to MAEC lacking PIN1 but not MAEC harboring an inactive control construct, and because cytotoxicity was blocked by the NO synthase inhibitor N(omega)-nitro-L-arginine methyl ester. Consistent with posttranscriptional action, knockdown of PIN1 increased the stability of iNOS protein in cycloheximide-treated cells. Furthermore, loss of iNOS was blocked by the calpain inhibitor carbobenzoxy-valinyl-phenylalaninal but not by the selective proteasome inhibitor epoxomicin. Immunoprecipitation indicated that PIN1 can interact with iNOS. Pull down of iNOS with a wild-type glutathione-S-transferase-PIN1 fusion protein, but not with a mutant of the amino terminal phospho-(serine/threonine)-proline binding WW domain of PIN1, indicated that this domain…
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Pin1 regulates degradation of inducible nitric oxide synthase and inhibits the production of LPS-induced nitric oxide in murine aortic endothelial cells (MAEC).
“Pin1 regulates degradation of inducible nitric oxide synthase and inhibits the production of LPS-induced nitric oxide in murine aortic endothelial cells (MAEC) [8].”
From Prolyl Isomerase Pin1 Protects Mice from Endotoxin Shock (2011) · cites this paper as [8]
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Snedecor, G. W., Cochran, W. G., & STOUT, B. B. (1939) · Soil Science · doi:10.1097/00010694-193902000-00006 · Cited by 19,423 · see citing works
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Goll, D. E., Thompson, V. F., Li, H., WEI, W., & Cong, J. (2003) · Physiological Reviews · doi:10.1152/physrev.00029.2002 · Cited by 2,826 · see citing works
A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen
Moffat, J., Grueneberg, D. A., Yang, X., Kim, S. Y., Kloepfer, A. M., Hinkle, G., Piqani, B., Eisenhaure, T., Luo, B., Grenier, J. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.01.040 · Cited by 1,803 · see citing works
Lentivirus-delivered stable gene silencing by RNAi in primary cells.
Stewart, S. A., Dykxhoorn, D. M., Palliser, D., Mizuno, H., Yu, E. Y., An, D., Sabatini, D., Chen, I. S. Y., Hahn, W., Sharp, P., et al. (2003) · RNA: A publication of the RNA Society · doi:10.1261/rna.2192803 · Cited by 1,619 · see citing works
Xie, Q. W., Whisnant, R., & Nathan, C. F. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.6.1779 · Cited by 1,118 · see citing works
Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 926 · see citing works
Nitric Oxide: Pathophysiological Mechanisms
Gross, S. S., & Wolin, M. S. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.003513 · Cited by 888 · see citing works
Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791 · see citing works
Yaffe, M. B., Schutkowski, M., Shen, M., Zhou, X. Z., Stukenberg, P. T., Rahfeld, J., Xu, J., Kuang, J., Kirschner, M. W., Fischer, G. S., et al. (1997) · Science · doi:10.1126/science.278.5345.1957 · Cited by 770 · see citing works
Regulation of the expression of inducible nitric oxide synthase
Kleinert, H., Pautz, A., Linker, K., & Schwarz, P. M. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.07.030 · Cited by 705 · see citing works
Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
Xia, Y., & Zweier, J. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6954 · Cited by 691 · see citing works
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682 · see citing works
Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y., Wulf, G. M., Rottapel, R. K., Yamaoka, S., & Lu, K. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00490-8 · Cited by 632 · see citing works
Wulf, G. M., Ryo, A., Wulf, G. G., Lee, S. W., Niu, T., Petkova, V., & Lu, K. P. (2001) · The EMBO Journal · doi:10.1093/emboj/20.13.3459 · Cited by 529 · see citing works
Nitric Oxide: Cytotoxicity versus Cytoprotection— How, Why, When, and Where?
Kröncke, K., Fehsel, K., & Kolb-Bachofen, V. (1997) · Nitric Oxide · doi:10.1006/niox.1997.0118 · Cited by 511 · see citing works
Ryo, A., Nakamura, M., Wulf, G. M., Liou, Y.-C., & Lu, K. P. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-793 · Cited by 467 · see citing works
Pinning down proline-directed phosphorylation signaling
Lu, K. P., Liou, Y.-C., & Zhou, X. Z. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02253-5 · Cited by 351 · see citing works
Shen, M., Stukenberg, P. T., Kirschner, M. W., & Lu, K.-P. (1998) · Genes & Development · doi:10.1101/gad.12.5.706 · Cited by 341 · see citing works
Regulation of the Transcriptional Activity of c-Fos by ERK
Monje, P. V., Hernández‐Losa, J., Lyons, R. J., Castellone, M. D., & Gutkind, J. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500353200 · Cited by 272 · see citing works
PIN1, the cell cycle and cancer
Yeh, E. S., & Means, A. R. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2107 · Cited by 268 · see citing works
Immortalization and transformation of primary human airway epithelial cells by gene transfer
Lundberg, A., Randell, S., Stewart, S. A., Elenbaas, B., Hartwell, K. A., Brooks, M., Fleming, M., Olsen, J., Miller, S., Weinberg, R., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205550 · Cited by 267 · see citing works
Phosphorylation-specific prolyl isomerization: is there an underlying theme?
Wulf, G. M., Finn, G., Suizu, F., & Lu, K. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0505-435 · Cited by 238 · see citing works
The WW domain: Linking cell signalling to the membrane cytoskeleton
Ilsley, J. L., Sudol, M., & Winder, S. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00236-4 · Cited by 183 · see citing works
Inducible Nitric-oxide Synthase Is Regulated by the Proteasome Degradation Pathway
Musial, A., & Eissa, N. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100725200 · Cited by 157 · see citing works
Kok, R. J., Schraa, A. J., Bos, E. J., Moorlag, H. E., Ásgeirsdóttir, S. A., Everts, M., Meijer, D. K. F., & Molema, G. (2001) · Bioconjugate Chemistry · doi:10.1021/bc015561+ · Cited by 146 · see citing works
Shen, Z.-J., Esnault, S. J., & Malter, J. S. (2005) · Nature Immunology · doi:10.1038/ni1266 · Cited by 127 · see citing works
Walker, G., Pfeilschifter, J. M., & Kunz, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16679 · Cited by 127 · see citing works
Heat Shock Protein 90 as an Endogenous Protein Enhancer of Inducible Nitric-oxide Synthase
Yoshida, M., & Xia, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305214200 · Cited by 119 · see citing works
Ubiquitination of inducible nitric oxide synthase is required for its degradation
Kolodziejski, P. J., Musial, A., Koo, J.-S., & Eissa, N. T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192345199 · Cited by 119 · see citing works
Regulation of Human Nitric Oxide Synthase 2 Expression by Wnt β-Catenin Signaling
Du, Q., Park, K. S., Guo, Z., He, P., Nagashima, M., Shao, L., Sahai, R., Geller, D. A., & Hussain, S. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4110 · Cited by 107 · see citing works
A Role for Nitric Oxide-Mediated Peroxynitrite Formation in a Model of Endotoxin-Induced Shock
Cuzzocrea, S., Mazzon, E., Paola, R. D., Esposito, E., Macarthur, H., Matuschak, G. M., & Salvemini, D. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.108100 · Cited by 102 · see citing works
Sensitivity of mice to lipopolysaccharide is increased by a high saturated fat and cholesterol diet
Huang, H., Liu, T., Rose, J. L., Stevens, R. L., & Hoyt, D. G. (2007) · Journal of Inflammation · doi:10.1186/1476-9255-4-22 · Cited by 85 · see citing works
Self-citationEsnault, S. J., Shen, Z.-J., Whitesel, E., & Malter, J. S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.10.6999 · Cited by 72 · see citing works
Tyrosine phosphorylated Disabled 1 recruits Crk family adapter proteins
Huang, Y., Magdaleno, S. M., Hopkins, R., Slaughter, C. A., Curran, T., & Keshvara, L. M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.04.023 · Cited by 71 · see citing works
Self-citationMorikawa, A., Koide, N., Kato, Y., Sugiyama, T., Chakravortty, D., Yoshida, T., & Yokochi, T. (2000) · Infection and Immunity · doi:10.1128/iai.68.11.6209-6214.2000 · Cited by 66 · see citing works
Yamazaki, T., YOKOYAMA, T., Akatsu, H., Tukiyama, T., & Tokiwa, T. (2003) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1290/1543-706x(2003)039 · Cited by 59 · see citing works
Self-citationHuang, H., Rose, J. L., & Hoyt, D. G. (2004) · Molecular Pharmacology · doi:10.1124/mol.66.2.302 · Cited by 49 · see citing works
Self-citationPin1 Modulates the Type 1 Immune Response
Esnault, S. J., Braun, R. K., Shen, Z.-J., Xiang, Z., Héninger, E., Love, R. B., Sándor, M., & Malter, J. S. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000226 · Cited by 46 · see citing works
Mei, J. M., Hord, N. G., Winterstein, D., Donald, S. P., & Phang, J. M. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.9.1188 · Cited by 44 · see citing works
Hausel, P., Latado, H., Courjault-Gautier, F., & Felley‐Bosco, E. (2005) · Oncogene · doi:10.1038/sj.onc.1209030 · Cited by 41 · see citing works
Lentiviral Delivery of RNAi in Hippocampal Neurons
Janas, J. A., Skowroński, J., & Aelst, L. V. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)06046-0 · Cited by 39 · see citing works
Proteolytic cleavage of inducible nitric oxide synthase (iNOS) by calpain I
Walker, G., Pfeilschifter, J. M., Otten, U., & Kunz, D. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(01)00223-9 · Cited by 38 · see citing works
Superoxide Production in the Vasculature of Lipopolysaccharide-Treated Rats and Pigs
Javeshghani, D., Hussain, S. N. A., Scheidel, J., Quinn, M. T., & Magder, S. A. (2003) · Shock · doi:10.1097/01.shk.0000054374.88889.37 · Cited by 33 · see citing works
Shelton, J. L., Wang, L., Cepinskas, G., Sandig, M., Scott, J. A., North, M. L., Inculet, R., & Mehta, S. (2007) · Microvascular Research · doi:10.1016/j.mvr.2007.02.008 · Cited by 29 · see citing works
Smallwood, H. S., Shi, L., & Squier, T. C. (2006) · Biochemistry · doi:10.1021/bi060485p · Cited by 23 · see citing works
Rose, J. L., Reeves, K. C., Likhotvorik, R. I., & Hoyt, D. G. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.113498 · Cited by 23 · see citing works
Self-citationWhat sense lies in antisense inhibition of inducible nitric oxide synthase expression?
Hemmrich, K., Kröncke, K., Suschek, C. V., & Kolb-Bachofen, V. (2005) · Nitric Oxide · doi:10.1016/j.niox.2005.04.003 · Cited by 9 · see citing works
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Farrell, A. S., Pelz, C., Wang, X., Daniel, C. J., Wang, Z., Su, Y., Janghorban, M., Zhang, X., Morgan, C. W., Impey, S., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01455-12 · Cited by 140 · see citing works
Su, Y., Pelz, C., Huang, T., Torkenczy, K. A., Wang, X., Cherry, A. E., Daniel, C. J., Liang, J. B., Nan, X., Dai, M., et al. (2018) · Genes & Development · doi:10.1101/gad.314377.118 · Cited by 65 · see citing works
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Ruan, L., Torres, C. M., Qian, J., Chen, F., MINTZ, J. D., Stepp, D. W., Fulton, D. J., & Venema, R. C. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.213181 · Cited by 55 · see citing works
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Chiasson, V. L., Munshi, N., Chatterjee, P., Young, K. J., & Mitchell, B. M. (2011) · Hypertension · doi:10.1161/hypertensionaha.111.172338 · Cited by 35 · see citing works
Xu, L., Ren, Z., Chow, F. E., Tsai, R., Liu, T., Rizzolio, F., Boffo, S., Xu, Y., Huang, S., Lippa, C. F., et al. (2017) · Neural Plasticity · doi:10.1155/2017/3270725 · Cited by 33 · see citing works
Self-citationZhang, M., Lin, L., Xu, C., Chai, D., Peng, F., & Lin, J. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1714896 · Cited by 33 · see citing works
Zhao, Y., Cui, G., Zhang, N., Liu, Z., Sun, W., & Peng, Q. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.09.023 · Cited by 26 · see citing works
Cui, G., Zhao, Y., Zhang, N.-N., Liu, Z., Sun, W., & Peng, Q. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.155 · Cited by 23 · see citing works
Li, J., Chen, S., Feng, J.-D., Zhang, M., & Liu, X. (2014) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2014.02.010 · Cited by 19 · see citing works
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Akiyama, H., Misawa, T., Ono, M., Uchida, C., & Uchida, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014656 · Cited by 17 · see citing works
Loh, S., Lee, C., Tsai, Y., Shih, S., Chen, L.-W., Cheng, T., Chang, C., & Tsai, C.-S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090273 · Cited by 17 · see citing works
Wang, J.-Z., Zhu, W., Xu, Z., Du, W.-T., Zhang, H., Sun, X., & Wang, X.-H. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.11.023 · Cited by 15 · see citing works
Wang, J.-Z., Li, S.-R., Li, Y., Yong-ze, Z., Zhang, T., Zhao, C., Yao, C.-X., & Du, L. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.08.020 · Cited by 13 · see citing works
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Liu, T., Schneider, R. A., Shah, V., Huang, Y., Likhotvorik, R. I., Keshvara, L., & Hoyt, D. G. (2009) · Journal of Inflammation · doi:10.1186/1476-9255-6-20 · Cited by 13 · see citing works
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Liu, T., Schneider, R. A., Lee, N. Y., & Hoyt, D. G. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.089 · Cited by 2 · see citing works
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- Authors
- Liu, T., Huang, Y., Likhotvorik, R. I., Keshvara, L., & Hoyt, D. G.
- Affiliations
- The Ohio State University (US)
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2008-09
- Volume
- 295
- Issue
- 3
- Pages
- C819-C827
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2018409037
- Cited by
- 25
- References
- 51
- Citations by year
- 2024: 3 · 2021: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2014: 3 · 2013: 3 · 2012: 2
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Keywords
- Pin1, peptidyl-prolyl isomerase, inducible nitric oxide synthase, endothelial cells, endotoxin, interferon-gamma, post-transcriptional regulation, protein stability, WW domain, nitric oxide synthase inhibitors, cytotoxicity
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Animals, Calpain, Cell Survival, Cells, Cultured, Dipeptides, Enzyme Inhibitors, Interferon-gamma, Lipopolysaccharides, Nitric Oxide, Oligopeptides, Protein Binding, Protein Processing, Post-Translational, Recombinant Proteins, RNA, Messenger, Time Factors, NG-Nitroarginine Methyl Ester, Peptidylprolyl Isomerase, Escherichia coli Proteins, RNA Interference, RNA, Small Interfering, Endothelial Cells, Proteasome Endopeptidase Complex, Mice, Nitric Oxide Synthase Type II, Proteasome Inhibitors
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