グリコアルブミン GA
WordNet
- a book of blank pages with pockets or envelopes; for organizing photographs or stamp collections etc
- one or more recordings issued together; originally released on 12-inch phonograph records (usually with attractive record covers) and later on cassette audiotape and compact disc (同)record album
- a simple water-soluble protein found in many animal tissues and liquids (同)albumen
PrepTutorEJDIC
- General Admiral / (またGa)Georgia
- (写真・切手・切り抜きなどを貼る)『アルバム』 / (いくつかの曲・劇などを収録した)組レコード,アルバム / 画帳
- アルブミン(蛋白質の一種)
UpToDate Contents
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English Journal
- Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin.
- Miki Y1, Dambara H, Tachibana Y, Hirano K, Konishi M, Beppu M.Author information 1School of Pharmacy, Tokyo University of Pharmacy and Life Sciences.AbstractAdvanced glycosylation end-products (AGEs) are non-enzymatically glycosylated proteins that play an important role in several diseases and aging processes, including angiopathy, renal failure, diabetic complications, and some neurodegenerative diseases. In particular, glyceraldehyde (GCA)- and glycolaldehyde (GOA)-derived AGEs are deemed toxic AGEs, due to their cytotoxicity. Recently, the shuttling-protein nucleolin has been shown to possess scavenger receptor-activity. Here, we investigated whether or not macrophages recognize toxic AGEs through nucleolin receptors expressed on their surface. Free amino acid groups and arginine residues found in bovine serum albumin (BSA) were time-dependently modified by incubation with GCA and GOA. In addition, average molecular size was increased by incubation with GCA and GOA. While GCA-treated BSA (GCA-BSA) and GOA-treated BSA (GOA-BSA) were recognized by thioglycollate-elicited mouse peritoneal macrophages in proportion to their respective aldehyde-modification ratios, aldehyde-untreated control-BSA was not. Surface plasmon-resonance analysis revealed that nucleolin strongly associated with GCA-BSA and GOA-BSA, but not with control-BSA. Further, pretreating macrophages with anti-nucleolin antibody, but not control-Immunoglobulin G, inhibited recognition of GCA-BSA and GOA-BSA by macrophages. Additionally, AGRO, a nucleolin-specific oligonucleotide aptamer, inhibited recognition of GCA-BSA and GOA-BSA. Moreover, nucleolin-transfected HEK293 cells recognized more GCA-BSA and GOA-BSA than control HEK cells did. Binding of nucleolin and GCA-BSA/GOA-BSA was also blocked by anti-nucleolin antibody at molecular level. These results indicate that nucleolin is a receptor that allows macrophages to recognize toxic AGEs.
- Biological & pharmaceutical bulletin.Biol Pharm Bull.2014 Apr 1;37(4):588-96. Epub 2014 Feb 7.
- Advanced glycosylation end-products (AGEs) are non-enzymatically glycosylated proteins that play an important role in several diseases and aging processes, including angiopathy, renal failure, diabetic complications, and some neurodegenerative diseases. In particular, glyceraldehyde (GCA)- and glyco
- PMID 24521707
- Preparation of hydrazine functionalized polymer brushes hybrid magnetic nanoparticles for highly specific enrichment of glycopeptides.
- Huang G1, Sun Z, Qin H, Zhao L, Xiong Z, Peng X, Ou J, Zou H.Author information 1State Key Laboratory of Fine Chemicals, Dalian University of Technology, Dalian 116024, China. hanfazou@dicp.ac.cn.AbstractHydrazide chemistry is a powerful technique in glycopeptides enrichment. However, the low density of the monolayer hydrazine groups on the conventional hydrazine-functionalized magnetic nanoparticles limits the efficiency of glycopeptides enrichment. Herein, a novel magnetic nanoparticle grafted with poly(glycidyl methacrylate) (GMA) brushes was fabricated via reversible addition-fragmentation chain transfer (RAFT) polymerization, and a large amount of hydrazine groups were further introduced to the GMA brushes by ring-opening the epoxy groups with hydrazine hydrate. The resulting magnetic nanoparticles (denoted as Fe3O4@SiO2@GMA-NHNH2) demonstrated the high specificity of capturing glycopeptides from a tryptic digest of the sample comprising a standard non-glycosylated protein bovine serum albumin (BSA) and four standard glycoproteins with a weight ratio of 50 : 1, and the detection limit was as low as 130 fmol. In the analysis of a real complex biological sample, the tryptic digest of hepatocellular carcinoma, 179 glycosites were identified by the Fe3O4@SiO2@GMA-NHNH2 nanoparticles, surpassing that of 68 glycosites by Fe3O4@SiO2-single-NHNH2 (with monolayer hydrazine groups on the surface). It can be expected that the magnetic nanoparticles modified with hydrazine functionalized polymer brushes via RAFT technique will improve the specificity and the binding capacity of glycopeptides from complex samples, and show great potential in the analysis of protein glycosylation in biological samples.
- The Analyst.Analyst.2014 Mar 31;139(9):2199-206. doi: 10.1039/c4an00076e.
- Hydrazide chemistry is a powerful technique in glycopeptides enrichment. However, the low density of the monolayer hydrazine groups on the conventional hydrazine-functionalized magnetic nanoparticles limits the efficiency of glycopeptides enrichment. Herein, a novel magnetic nanoparticle grafted wit
- PMID 24615010
- Glycated hemoglobin measurement and prediction of cardiovascular disease.
- Emerging Risk Factors Collaboration, Di Angelantonio E1, Gao P1, Khan H1, Butterworth AS1, Wormser D1, Kaptoge S1, Kondapally Seshasai SR2, Thompson A1, Sarwar N1, Willeit P1, Ridker PM3, Barr EL4, Khaw KT1, Psaty BM5, Brenner H6, Balkau B7, Dekker JM8, Lawlor DA9, Daimon M10, Willeit J11, Njølstad I12, Nissinen A13, Brunner EJ14, Kuller LH15, Price JF16, Sundström J17, Knuiman MW18, Feskens EJ19, Verschuren WM20, Wald N21, Bakker SJ22, Whincup PH2, Ford I23, Goldbourt U24, Gómez-de-la-Cámara A25, Gallacher J26, Simons LA27, Rosengren A28, Sutherland SE29, Björkelund C30, Blazer DG31, Wassertheil-Smoller S32, Onat A33, Marín Ibañez A34, Casiglia E35, Jukema JW36, Simpson LM37, Giampaoli S38, Nordestgaard BG39, Selmer R40, Wennberg P41, Kauhanen J42, Salonen JT43, Dankner R44, Barrett-Connor E45, Kavousi M46, Gudnason V47, Evans D48, Wallace RB49, Cushman M50, D'Agostino RB Sr51, Umans JG52, Kiyohara Y53, Nakagawa H54, Sato S55, Gillum RF56, Folsom AR57, van der Schouw YT58, Moons KG58, Griffin SJ1, Sattar N23, Wareham NJ1, Selvin E59, Thompson SG1, Danesh J1.Author information 1University of Cambridge, Cambridge, United Kingdom.2St George's University of London, London, United Kingdom.3Brigham and Women's Hospital, Boston, Massachusetts.4Baker IDI Heart and Diabetes Institute, Victoria, Australia.5University of Washington, Seattle6Group Health Research Institute, Seattle, Washington.6German Cancer Research Center, Heidelberg, Germany.7Inserm, Villejuif, France9University Paris-Sud, Villejuif, France.8Vrije Universiteit Medical Center, Amsterdam, the Netherlands.9University of Bristol, Bristol, United Kingdom.10Yamagata University, Japan.11Medical University Innsbruck, Austria.12University of Tromsø, Tromsø, Norway.13National Institute of Health and Welfare, Helsinki, Finland.14University College London, London, United Kingdom.15University of Pittsburgh.16University of Edinburgh, Edinburgh, United Kingdom.17Uppsala University, Uppsala, Sweden.18University of Western Australia, Perth, Australia.19Wageningen University, Wageningen, the Netherlands.20National Institute for Public Health and the Environment (RIVM), Bilthoven, the Netherlands.21Wolfson Institute of Preventive Medicine, London, United Kingdom.22University of Groningen, University Medical Center Groningen, the Netherlands.23University of Glasgow, Glasgow, United Kingdom.24Sheba Medical Center, Tel Hashomer, Israel.25Hospital 12 de Octubre, Madrid, Spain.26Cardiff University, Cardiff, United Kingdom.27University of New South Wales, Kensington, Australia.28Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.29Medical University of South Carolina, Charleston.30University of Gothenburg, Gothenburg, Sweden.31Duke University Medical Center, Durham, North Carolina.32Albert Einstein College of Medicine, New York, New York.33University of Istanbul, Istanbul, Turkey.34San Jose Norte Health Centre, Zaragoza, Spain.35University of Padova, Padova, Italy.36Leiden University Medical Center, Leiden, the Netherlands.37University of Texas School of Public Health, Houston.38Istituto Superiore di Sanità, Rome, Italy.39Herlev Hospital, Copenhagen University Hospital, University of Copenhagen, Copenhagen, Denmark.40Norwegian Institute of Public Health, Oslo, Norway.41Umeå University, Umeå, Sweden.42University of Eastern Finland, Kuopio, Finland.43University of Helsinki, Helsinki, Finland.44The Gertner Institute for Epidemiology and Health Policy Research, Tel Hashomer, Israel47Tel Aviv University, Tel Aviv, Israel48The Feinstein Institute for Medical Research, New York, New York.45University of California, San Diego.46Erasmus Medical Center, Rotterdam, the Netherlands.47Icelandic Heart Association, Reyjavik, Iceland52University of Iceland, Reykjavik, Iceland.48Rush University Medical Center, Chicago, Illinois.49University of Iowa College of Public Health, Iowa City.50University of Vermont, Burlington.51Boston University, Boston, Massachusetts.52Georgetown University Medical Centre, Washington, DC.53Kyushu University, Kyushu, Japan.54Kanazawa Medical University, Ishikawa, Japan.55Osaka Medical Center for Health Science and Promotion/Chiba Prefectural Institute of Public Health, Osaka, Japan.56Howard University, Washington, DC.57University of Minnesota, Minneapolis.58Julius Center for Health Sciences and Primary Care, University Medical Center Utrecht, Utrecht, the Netherlands.59Johns Hopkins University, Baltimore, Maryland.AbstractIMPORTANCE: The value of measuring levels of glycated hemoglobin (HbA1c) for the prediction of first cardiovascular events is uncertain.
- JAMA : the journal of the American Medical Association.JAMA.2014 Mar 26;311(12):1225-33. doi: 10.1001/jama.2014.1873.
- IMPORTANCE: The value of measuring levels of glycated hemoglobin (HbA1c) for the prediction of first cardiovascular events is uncertain.OBJECTIVE: To determine whether adding information on HbA1c values to conventional cardiovascular risk factors is associated with improvement in prediction of cardi
- PMID 24668104
Japanese Journal
- Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin
- Miki Yuichi,Dambara Hikaru,Tachibana Yoshihiro,Hirano Kazuya,Konishi Mio,Beppu Masatoshi
- Biological and Pharmaceutical Bulletin 37(4), 588-596, 2014
- … Advanced glycosylation end-products (AGEs) are non-enzymatically glycosylated proteins that play an important role in several diseases and aging processes, including angiopathy, renal failure, diabetic complications, and some neurodegenerative diseases. … Free amino acid groups and arginine residues found in bovine serum albumin (BSA) were time-dependently modified by incubation with GCA and GOA. …
- NAID 130003390979
- Discrimination of glycoproteins via two-color laser-induced fluorescence detection coupled with postcolumn derivatization in capillary electrophoresis
- Tabara Ayumi,Kaneta Takashi
- Electrophoresis 34(16), 2316-2322, 2013-08
- … The method can be used to discriminate glycoproteins in a protein mixture containing both glycosylated and unglycosylated proteins. … So, a protein can be assigned as glycosylated if it shows a peak at the same migration time in both electropherograms. … According to the proposed principle, in a single run we discriminated a glycosylated protein (thyroglobulin) from an unglycosylated protein (albumin) in the presence of rhodamine-labeled Con A. …
- NAID 120005311971
- Factors Related to Tooth Loss Among Community-Dwelling Middle-aged and Elderly Japanese Men
- Ando Ayumi,Ohsawa Masaki,Yaegashi Yumi,Sakata Kiyomi,Tanno Kozo,Onoda Toshiyuki,Itai Kazuyoshi,Tanaka Fumitaka,Makita Shinji,Omama Shinichi,Ogasawara Kuniaki,Ogawa Akira,Ishibashi Yasuhiro,Kuribayashi Toru,Koyama Tomiko,Okayama Akira
- Journal of Epidemiology 23(4), 301-306, 2013
- … In addition, men with 19 or fewer teeth were more likely to have a low body mass index and low serum albumin level and less likely to be current alcohol drinkers. …
- NAID 130003364507
Related Links
- Glycosylated Albumin Human serum albumin is a single chain polypeptide which composes about 60% of the plasma proteins. In normal serum approximately 10% of the albumin is modified by non-enzymatic glycosylation which ...
- 1. Diabetes. 1980 Jun;29(6):417-22. Increased glycosylation of serum albumin in diabetes mellitus. Dolhofer R, Wieland OH. The level of glycosylated albumin has been determined in the serum of normal and diabetic ...
★リンクテーブル★
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- 関
- glycosylate、glycosylation
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- 関
- glycosylated、glycosylation