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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/06/14 11:14:41」(JST)
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- 1. 糸球体足細胞のバイオロジー biology of glomerular podocytes
English Journal
- Slit diaphragm protein Neph1 and it's signaling: a novel therapeutic target for protection of podocytes against glomerular injury.
- Arif E1, Rathore YS, Kumari B, Ashish F, Wong HN, Holzman LB, Nihalani D.Author information 1University of Pennsylvania, United States;AbstractPodocytes are specialized epithelial cells that are critical components of the glomerular filtration barrier and their dysfunction leads to proteinuria and renal failure. Therefore, preserving podocyte function is therapeutically significant. In this study, we identified Neph1 signaling as a therapeutic target which upon inhibition prevented podocyte damage from a glomerular injury inducing agent PAN (puromycin aminonucleosinde). To specifically inhibit Neph1 signaling we used a protein transduction approach, where the cytoplasmic domain of Neph1 (Neph1CD) tagged with a protein transduction domain TAT (trans-activator of transcription) was transduced in cultured podocytes prior to treatment with PAN. The PAN induced Neph1 phosphorylation was significantly reduced in Neph1CD transduced cells; in addition, these cells were resistant to PAN-induced cytoskeletal damage. The biochemical analysis using subfractionation studies showed that unlike control cells, Neph1 was retained in the lipid raft fractions in the transduced cells following treatment with PAN, indicating that transduction of Neph1CD in podocytes prevented PAN induced mislocalization of Neph1. In accordance, the immunofluorescence analysis further suggested that Neph1CD transduced cells had increased ability to retain endogenous Neph1 at the membrane in response to PAN-induced injury. Similar results were obtained when Angiotensin was used as an injury-inducing agent. Consistent with these observations, maintaining high levels of Neph1 at the membrane using a podocyte cell line overexpressing chimeric Neph1 increased the ability of podocytes to resist, PAN-induced injury and PAN-induced albumin leakage. Using a zebrafish in vivo PAN and adriamycin injury models, we further demonstrated the ability of transduced Neph1CD to preserve glomerular function. Collectively, these results support the conclusion that inhibiting Neph1 signaling is therapeutically significant in preventing podocyte damage from glomerular injury.
- The Journal of biological chemistry.J Biol Chem.2014 Feb 19. [Epub ahead of print]
- Podocytes are specialized epithelial cells that are critical components of the glomerular filtration barrier and their dysfunction leads to proteinuria and renal failure. Therefore, preserving podocyte function is therapeutically significant. In this study, we identified Neph1 signaling as a therape
- PMID 24554715
- Mechanism of the Photoinduced Uncaging Reaction of Puromycin Protected by a 6-Nitroveratryloxycarbonyl Group.
- Kohl-Landgraf J, Buhr F, Lefrancois D, Mewes JM, Schwalbe H, Dreuw A, Wachtveitl JL.AbstractThe cleavage of a photolabile nitroveratryloxycarbonyl protecting group (NVOC), which is widely used as caging group, was studied by femtosecond-transient absorption spectroscopy in the visible and infrared spectral range and by flash-photolysis experiments on the longer time scale. Based on quantum chemical calculations it is shown that directly after excitation triplet absorption dominates the transient spectrum which is not part of the reactive pathway and that the molecules following the triplet pathway are trapped in a non-reactive triplet state. By contrast photolysis proceeds from the singlet manifold. Therefore trapping in the triplet state lowers the quantum yield of the process for this compound compared to other ortho-nitrobenzyl protecting groups. With our integrated approach of time-resolved UV and IR measurements and calculations we can characterize the entire uncaging mechanism and identify the most relevant intermediate states along the reaction pathway. The final uncaging is accomplished within 32 µs.
- Journal of the American Chemical Society.J Am Chem Soc.2014 Feb 11. [Epub ahead of print]
- The cleavage of a photolabile nitroveratryloxycarbonyl protecting group (NVOC), which is widely used as caging group, was studied by femtosecond-transient absorption spectroscopy in the visible and infrared spectral range and by flash-photolysis experiments on the longer time scale. Based on quantum
- PMID 24517286
- Probing the Leucyl/Phenylalanyl tRNA Protein Transferase Active Site with tRNA Substrate Analogues.
- Fung AW, Ebhardt HA, Krishnakumar KS, Moore J, Xu Z, Strazewski P, Fahlman RP1.Author information 1474 Medical Sciences Building. Department of Biochemistry. University of Alberta. Edmonton, Alberta, T6G 2H7, Canada. rfahlman@ualberta.ca.AbstractAminoacyl-tRNA protein transferases post-translationally conjugate an amino acid from an aminoacyl-tRNA onto the N-terminus of a target polypeptide. The eubacterial aminoacyl-tRNA protein transferase, L/F transferase, utilizes both leucyl-tRNALeu and phenylalanyl-tRNAPhe as substrates. X-ray crystal structures with substrate analogues, the minimal substrate phenylalanyl adenosine (rA-Phe) and inhibitor puromycin, have been used to characterize tRNA recognition by L/F transferase. However analyses of these two X-ray crystal structures reveal significant differences in binding. Through structural analyses, mutagenesis, and enzymatic activity assays, we rationalize and demonstrate that the substrate analogues bind to L/F transferase with similar binding affinities using a series of different interactions by the various chemical groups of the analogues. Our data also demonstrates that enlarging the hydrophobic pocket of L/F transferase selectively enhances puromycin inhibition and may aid in the development of improved inhibitors for this class of enzymes.
- Protein and peptide letters.Protein Pept Lett.2014 Feb 11. [Epub ahead of print]
- Aminoacyl-tRNA protein transferases post-translationally conjugate an amino acid from an aminoacyl-tRNA onto the N-terminus of a target polypeptide. The eubacterial aminoacyl-tRNA protein transferase, L/F transferase, utilizes both leucyl-tRNALeu and phenylalanyl-tRNAPhe as substrates. X-ray crystal
- PMID 24521222
Japanese Journal
- SPECIFIC INHIBITORS OF PUROMYCIN-SENSITIVE AMINOPEPTIDASE WITH A 3-(HALOGENATED PHENYL)-2,4(1H,3H)-QUINAZOLINEDIONE SKELETON (Dedicated to Professor Dr. Ei-ichi Negishi on the occasion of his 77th birthday)
- Matsumoto Yotaro,Noguchi-Yachide Tomomi,Nakamura Masaharu [他]
- Heterocycles : an international journal for reviews and communications in heterocyclic chemistry 86(2), 1449-1463, 2012-12-31
- NAID 40019534016
- Effect of Pamamycin-607 on Secondary Metabolite Production by Streptomyces spp.
- Hashimoto Makoto,Katsura Hirotaka,Kato Risako [他],KAWAIDE Hiroshi,NATSUME Masahiro
- Bioscience, biotechnology, and biochemistry 75(9), 1722-1726, 2011-09-23
- … Exposure to 6.6 μM pamamycin-607 stimulated by 2.7 fold the puromycin production by <I>Streptomyces alboniger</I> …
- NAID 10029757098
- Microintaglio Printing of Biomolecules and Its Application to In situ Production of Messenger Ribonucleic Acid Display Microarray
- Biyani Manish,Osawa Terutsune,Nemoto Naoto [他],Ichiki Takanori
- Applied physics express 4(4), 047001-047001-3, 2011-04-25
- … Furthermore, one-step conversion from an mRNA microarray into an mRNA-protein fusion microarray was performed by simultaneous cell-free protein synthesis and fusion reaction using a puromycin-labeled oligonucleotide linker. …
- NAID 150000001203
Related Links
- Puromycin is an aminonucleoside antibiotic produced by the bacterium Streptomyces alboniger. It inhibits protein synthesis by disrupting peptide transfer on ribosomes causing premature chain termination during translation. It is a ...
- Puromycin is an aminonucleoside antibiotic produced by the bacterium Streptomyces alboniger. It inhibits protein synthesis by disrupting peptide transfer on ribosomes causing premature chain termination during translation. It is a ...
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★リンクテーブル★
| リンク元 | 「PM」「ピューロマイシン」 |
| 拡張検索 | 「puromycin aminonucleoside」 |