WordNet
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
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- 蛋白(たんばく)質
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- 1. プロテインS欠乏症：臨床症状および診断 protein s deficiency clinical manifestations and diagnosis
- 2. 幼児の食物蛋白誘発性直腸炎/大腸炎および腸疾患 food protein induced proctitis colitis and enteropathy of infancy
- 3. プロテインC欠乏症：臨床症状および診断 protein c deficiency clinical manifestations and diagnosis
- 4. 第V因子ライデンおよび活性化プロテインC抵抗性：臨床症状および診断 factor v leiden and activated protein c resistance clinical manifestations and diagnosis
- 5. 肥大型心筋症の遺伝学 genetics of hypertrophic cardiomyopathy
English Journal
- Atorvastatin inhibits CXCR7 induction to reduce macrophage migration.
- Ma W1, Liu Y1, Wang C1, Zhang L1, Crocker L1, Shen J2.Author information 1Division of Pharmacology, Department of Drug Discovery & Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, United States.2Division of Pharmacology, Department of Drug Discovery & Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, United States. Electronic address: jzs0019@auburn.edu.AbstractWe have recently reported that CXCR7, the alternate high affinity SDF-1 receptor, is induced during monocyte-to-macrophage differentiation, leading to increased macrophage phagocytosis linked to atherosclerosis. Statins, the most widely used medications for atherosclerosis, were shown to have pleiotropic beneficial effects independent of their cholesterol-lowering activity. This study aimed to determine whether induction of CXCR7 during macrophage differentiation is inhibited by statins and its significance on macrophage physiology. Here we show for the first time that atorvastatin dose-dependently inhibited CXCR7 mRNA and protein expression in THP-1 macrophages, without affecting the other SDF-1 receptor, CXCR4. Pharmacotherapy relevant dose of atorvastatin affected neither cell viability nor macrophage differentiation. Suppression of CXCR7 expression was completely reversed by supplementation with mevalonate. Inhibition of squalene synthase, the enzyme committed to cholesterol biosynthesis, also decreased CXCR7 induction, albeit not as efficacious as atorvastatin. However, the geranylgeranyl transferase inhibitor, GGTI-286, the farnesyl transferase inhibitor, FTI-276, and the Rho kinase inhibitor, Y-27632, all failed to mimic the effect of atorvastatin, suggesting that the protein prenylation pathways are not critical for atorvastatin inhibition of CXCR7 induction. Interestingly, the dramatic effect of atorvastatin was only partially mimicked by other statins including pravastatin, fluvastatin, mevastatin, and simvastatin. Furthermore, activation of CXCR7 by SDF-1, TC14012, or I-TAC all prompted macrophage migration, which was significantly suppressed by atorvastatin treatment, but not by the CXCR4 antagonist. We conclude that atorvastatin modulates macrophage migration by down-regulating CXCR7 expression, suggesting a new CXCR7-dependent mechanism of atorvastatin to benefit atherosclerosis treatment beyond its lipid lowering effect.
- Biochemical pharmacology.Biochem Pharmacol.2014 May 1;89(1):99-108. doi: 10.1016/j.bcp.2014.02.014. Epub 2014 Feb 28.
- We have recently reported that CXCR7, the alternate high affinity SDF-1 receptor, is induced during monocyte-to-macrophage differentiation, leading to increased macrophage phagocytosis linked to atherosclerosis. Statins, the most widely used medications for atherosclerosis, were shown to have pleiot
- PMID 24582769
- A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: Biochemical characterization and structural insight into the regioselective prenylation.
- Miyamoto K1, Ishikawa F1, Nakamura S2, Hayashi Y1, Nakanishi I2, Kakeya H3.Author information 1Department of System Chemotherapy and Molecular Sciences, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.2Faculty of Pharmacy, Kinki University, 3-4-1 Kowakae, Higashi-osaka 577-8502, Japan.3Department of System Chemotherapy and Molecular Sciences, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. Electronic address: scseigyo-hisyo@pharm.kyoto-u.ac.jp.AbstractA putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His6-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of l-tryptophan at the C7 position of the indole moiety in the presence of dimethylallyl diphosphate; thus, it functions as a 7-DMATS. In this study, we describe the biochemical characterization of 7-DMATS from Neosartorya sp., referred to as 7-DMATS(Neo), and the structural basis of the regioselective prenylation of l-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATS(Neo) with FgaPT2 (4-DMATS) from Aspergillus fumigatus.
- Bioorganic & medicinal chemistry.Bioorg Med Chem.2014 Apr 15;22(8):2517-28. doi: 10.1016/j.bmc.2014.02.031. Epub 2014 Mar 12.
- A putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His6-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of l-tryptophan at the C7 position of the indole moiety in the presence of dim
- PMID 24657051
- Upregulation of endogenous farnesyl diphosphate synthase overcomes the inhibitory effect of bisphosphonate on protein prenylation in Hela cells.
- Das S1, Edwards PA2, Crockett JC3, Rogers MJ4.Author information 1Musculoskeletal Research Programme, Division of Applied Medicine, School of Medicine and Dentistry, University of Aberdeen, Aberdeen, UK.2School of Medicine, University of California, Los Angeles, CA 90095, USA.3Musculoskeletal Research Programme, Division of Applied Medicine, School of Medicine and Dentistry, University of Aberdeen, Aberdeen, UK. Electronic address: j.c.crockett@abdn.ac.uk.4Bone Biology Division, Garvan Institute of Medical Research, Darlinghurst, NSW 2010, Australia; St. Vincent's Clinical School, University of New South Wales, Australia.AbstractNitrogen-containing bisphosphonates (N-BPs) such as zoledronic acid (ZOL) are the gold standard treatment for diseases of excessive bone resorption. N-BPs inactivate osteoclasts via inhibition of farnesyl diphosphate synthase (FPPS), thereby preventing the prenylation of essential small GTPases. Not all patients respond to N-BP therapy to the same extent, and some patients, for example with tumour-associated bone disease or Paget's disease, appear to develop resistance to N-BPs. The extent to which upregulation of FPPS might contribute to these phenomena is not clear. Using quantitative PCR and western blot analysis we show that levels of FPPS mRNA and protein can be upregulated in HeLa cells by culturing in lipoprotein deficient serum (LDS) or by over-expression of SREBP-1a. Upregulated, endogenous FPPS was predominantly localised to the cytosol and did not co-localise with peroxisomal or mitochondrial markers. Upregulation of endogenous FPPS conferred resistance to the inhibitory effect of low concentrations of ZOL on the prenylation of the small GTPase Rap1a. These observations suggest that an increase in the expression of endogenous FPPS could confer at least partial resistance to the pharmacological effect of N-BP drugs such as ZOL in vivo.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Apr;1841(4):569-73. doi: 10.1016/j.bbalip.2013.12.010. Epub 2013 Dec 22.
- Nitrogen-containing bisphosphonates (N-BPs) such as zoledronic acid (ZOL) are the gold standard treatment for diseases of excessive bone resorption. N-BPs inactivate osteoclasts via inhibition of farnesyl diphosphate synthase (FPPS), thereby preventing the prenylation of essential small GTPases. Not
- PMID 24369118
Japanese Journal
- Modification and Translocation of Rac/Rop Guanosine 5′-Triphosphate-Binding Proteins of Scoparia dulcis in Response to Stimulation with Methyl Jasmonate
- Mitamura Toshiaki,Yamamura Yoshimi,Kurosaki Fumiya
- Biological & Pharmaceutical Bulletin 34(6), 845-849, 2011
- … Recombinant Sdrac-2 protein was found to bind to prenyl chain in the presence of cell extracts prepared from methyl jasmonate-treated S. … These results suggest that both Sdrac-1 and Sdrac-2 translocate to plant membranes by the stimulation with methyl jasmonate, however, targeting of these proteins is triggered by the independent modification mechanisms, palmitoylation for Sdrac-1 and prenylation for Sdrac-2. …
- NAID 130000738059
- Simvastatin Suppresses Leptin Expression in 3T3-L1 Adipocytes via Activation of the Cyclic AMP-PKA Pathway Induced by Inhibition of Protein Prenylation
- MAEDA Toyonobu,HORIUCHI Noboru
- The journal of biochemistry 145(6), 771-781, 2009-06-01
- NAID 10025187027
Related Links
- 1. Annu Rev Biochem. 1996;65:241-69. Protein prenylation: molecular mechanisms and functional consequences. Zhang FL(1), Casey PJ. Author information: (1)Department of Molecular Cancer Biology, Duke University ...
- 1. Nat Rev Mol Cell Biol. 2016 Feb;17(2):110-22. doi: 10.1038/nrm.2015.11. Epub 2016 Jan 21. Protein prenylation: unique fats make their mark on biology. Wang M(1), Casey PJ(1,)(2). Author information: (1)Program in ...
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★リンクテーブル★
| リンク元 | 「protein farnesylation」「タンパク質プレニル化」「protein geranylgeranylation」「protein isoprenylation」 |
| 関連記事 | 「prenylation」 |