主要塩基性タンパク質 MBP
WordNet
- of the field of academic study in which one concentrates or specializes; "his major field was mathematics"
- a commissioned military officer in the United States Army or Air Force or Marines; below lieutenant colonel and above captain
- a university student who is studying a particular field as the principal subject; "she is a linguistics major"
- the principal field of study of a student at a university; "her major is linguistics"
- greater in number or size or amount; "a major portion (a majority) of the population"; "Ursa Major"; "a major portion of the winnings"
- greater in scope or effect; "a major contribution"; "a major improvement"; "a major break with tradition"; "a major misunderstanding"
- have as ones principal field of study; "She is majoring in linguistics"
- of a scale or mode; "major scales"; "the key of D major"
- of full legal age
- of greater importance or stature or rank; "a major artist"; "a major role"; "major highways"
- of greater seriousness or danger; "a major earthquake"; "a major hurricane"; "a major illness"
- of the elder of two boys with the same family name; "Jones major"
- pertaining to or constituting a base or basis; "a basic fact"; "the basic ingredients"; "basic changes in public opinion occur because of changes in priorities"
- (usually plural) a necessary commodity for which demand is constant (同)staple
- reduced to the simplest and most significant form possible without loss of generality; "a basic story line"; "a canonical syllable pattern" (同)canonic, canonical
- serving as a base or starting point; "a basic course in Russian"; "basic training for raw recruits"; "a set of basic tools"; "an introductory art course" (同)introductory
- of or denoting or of the nature of or containing a base
- 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"
- a popular programming language that is relatively easy to learn; an acronym for beginners all-purpose symbolic instruction code; no longer in general use
- a statement of fundamental facts or principles (同)rudiments
PrepTutorEJDIC
- 『大きい』(『多い』)『ほうの』,いっそう重要な / (音階が)長調の,長音階の / 《英》《昔の学校で同姓または兄弟生徒を区別するために姓の後につけて》年長の,兄の / 《しばしばM-》陸軍(空軍)少佐 / 《米》専攻科目;専攻学生 / 《the majors》《米》=major leagues / (科目を)専攻する《+『in』+『名』》
- 『基礎の』,基本的な(fundamental) / 塩基性(アルカリ性)の
- 蛋白(たんばく)質
- 基本,基礎
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/03/16 01:40:49」(JST)
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Proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein) |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1H8U, 2BRS
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Identifiers |
Symbols |
PRG2 ; BMPG; MBP; MBP1 |
External IDs |
OMIM: 605601 MGI: 103294 HomoloGene: 2044 GeneCards: PRG2 Gene |
Gene ontology |
Molecular function |
• heparin binding
• carbohydrate binding
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Cellular component |
• extracellular region
• transport vesicle
• extracellular vesicular exosome
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Biological process |
• immune response
• defense response to bacterium
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
5553 |
19074 |
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Ensembl |
ENSG00000186652 |
ENSMUSG00000027073 |
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UniProt |
P13727 |
Q61878 |
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RefSeq (mRNA) |
NM_001243245 |
NM_008920 |
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RefSeq (protein) |
NP_001230174 |
NP_032946 |
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Location (UCSC) |
Chr 11:
57.15 – 57.16 Mb |
Chr 2:
84.98 – 84.98 Mb |
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PubMed search |
[1] |
[2] |
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Proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein), also known as PRG2, is a protein which in humans is encoded by the PRG2 gene.[1]
Contents
- 1 Function
- 2 Structure
- 3 Interactions
- 4 See also
- 5 References
- 6 External links
- 7 Further reading
§Function
The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin, and in immune hypersensitivity reactions. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases.[1]
PRG2 is a 117-residue protein that predominates in eosinophil granules. It is a potent enzyme against helminths and is toxic towards bacteria and mammalian cells in vitro. The eosinophil major basic protein also causes the release of histamine from mast cells and basophils, and activates neutrophils and alveolar macrophages.
§Structure
Structurally the major basic protein (MBP) is similar to lectins (sugar-binding proteins), and has a fold similar to that seen in C-type lectins. However, unlike other C-type lectins (those that bind various carbohydrates in the presence of calcium), MBP does not bind either calcium or any of the other carbohydrates that this family recognize.
Instead, MBP recognises heparan sulfate proteoglycans. Two crystallographic structures of MBP have been determined.[2][3]
§Interactions
Major basic protein has been shown to interact with Pregnancy-associated plasma protein A.[4][5][6]
§See also
arylsulfatase
§References
- ^ a b "Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)".
- ^ PDB 1h8u; Swaminathan GJ, Weaver AJ, Loegering DA, Checkel JL, Leonidas DD, Gleich GJ, Acharya KR (July 2001). "Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity". J. Biol. Chem. 276 (28): 26197–26203. doi:10.1074/jbc.M100848200. PMID 11319227.
- ^ PDB 2brs; Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR (November 2005). "Eosinophil-granule major basic protein, a C-type lectin, binds heparin". Biochemistry 44 (43): 14152–14158. doi:10.1021/bi051112b. PMID 16245931.
- ^ Overgaard, M T; Haaning J; Boldt H B; Olsen I M; Laursen L S; Christiansen M; Gleich G J; Sottrup-Jensen L; Conover C A; Oxvig C (October 2000). "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor". J. Biol. Chem. (UNITED STATES) 275 (40): 31128–31133. doi:10.1074/jbc.M001384200. ISSN 0021-9258. PMID 10913121.
- ^ Overgaard, Michael T; Sorensen Esben S, Stachowiak Damian, Boldt Henning B, Kristensen Lene, Sottrup-Jensen Lars, Oxvig Claus (January 2003). "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment". J. Biol. Chem. (United States) 278 (4): 2106–2117. doi:10.1074/jbc.M208777200. ISSN 0021-9258. PMID 12421832.
- ^ Oxvig, C; Sand O; Kristensen T; Gleich G J; Sottrup-Jensen L (June 1993). "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein". J. Biol. Chem. (UNITED STATES) 268 (17): 12243–6. ISSN 0021-9258. PMID 7685339.
§External links
- Eosinophil Major Basic Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
§Further reading
- Vanhaesebroeck B, Alessi DR (2000). "The PI3K-PDK1 connection: more than just a road to PKB". Biochem. J. 346 (3): 561–76. doi:10.1042/0264-6021:3460561. PMC 1220886. PMID 10698680.
- Yoshimatsu K; Ohya Y; Shikata Y et al. (1992). "Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins". Mol. Immunol. 29 (4): 537–546. doi:10.1016/0161-5890(92)90012-M. PMID 1565101.
- Barker RL; Loegering DA; Arakawa KC et al. (1990). "Cloning and sequence analysis of the human gene encoding eosinophil major basic protein". Gene 86 (2): 285–289. doi:10.1016/0378-1119(90)90292-Y. PMID 2323577.
- Gabay JE; Scott RW; Campanelli D et al. (1989). "Antibiotic proteins of human polymorphonuclear leukocytes". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5610–5614. doi:10.1073/pnas.86.14.5610. PMC 297672. PMID 2501794.
- Wasmoen TL; McKean DJ; Benirschke K et al. (1990). "Evidence of eosinophil granule major basic protein in human placenta". J. Exp. Med. 170 (6): 2051–2063. doi:10.1084/jem.170.6.2051. PMC 2189540. PMID 2584934.
- Barker RL, Gleich GJ, Pease LR (1988). "Acidic precursor revealed in human eosinophil granule major basic protein cDNA". J. Exp. Med. 168 (4): 1493–1498. doi:10.1084/jem.168.4.1493. PMC 2189086. PMID 3171483.
- McGrogan M; Simonsen C; Scott R et al. (1989). "Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein". J. Exp. Med. 168 (6): 2295–2308. doi:10.1084/jem.168.6.2295. PMC 2189145. PMID 3199069.
- Wasmoen TL; Bell MP; Loegering DA et al. (1988). "Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein". J. Biol. Chem. 263 (25): 12559–63. PMID 3410852.
- Weller PF, Ackerman SJ, Smith JA (1988). "Eosinophil granule cationic proteins: major basic protein is distinct from the smaller subunit of eosinophil peroxidase". J. Leukoc. Biol. 43 (1): 1–4. PMID 3422083.
- Kristensen T; Oxvig C; Sand O et al. (1994). "Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA". Biochemistry 33 (6): 1592–1598. doi:10.1021/bi00172a040. PMID 7508748.
- Oxvig C, Haaning J, Højrup P, Sottrup-Jensen L (1994). "Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum". Biochem. Mol. Biol. Int. 33 (2): 329–36. PMID 7524900.
- Bonno M; Oxvig C; Kephart GM et al. (1994). "Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta". Lab. Invest. 71 (4): 560–6. PMID 7526035.
- Li MS; Sun L; Satoh T et al. (1995). "Human eosinophil major basic protein, a mediator of allergic inflammation, is expressed by alternative splicing from two promoters". Biochem. J. 305 (3): 921–7. PMC 1136346. PMID 7531438.
- Oxvig C; Haaning J; Kristensen L et al. (1995). "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma". J. Biol. Chem. 270 (23): 13645–13651. doi:10.1074/jbc.270.23.13645. PMID 7539791.
- Oxvig C; Sand O; Kristensen T et al. (1993). "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein". J. Biol. Chem. 268 (17): 12243–6. PMID 7685339.
- Levi-Schaffer F; Lacy P; Severs NJ et al. (1995). "Association of granulocyte-macrophage colony-stimulating factor with the crystalloid granules of human eosinophils". Blood 85 (9): 2579–86. PMID 7727786.
- Oxvig C, Gleich GJ, Sottrup-Jensen L (1994). "Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein". FEBS Lett. 341 (2–3): 213–217. doi:10.1016/0014-5793(94)80459-1. PMID 8137941.
- Shikata Y; Hayashi Y; Yoshimatsu K et al. (1993). "Pro-major basic protein has three types of sugar chains at the pro-portion". Biochim. Biophys. Acta 1163 (3): 243–9. doi:10.1016/0167-4838(93)90158-N. PMID 8507662.
- Nittoh T; Watanabe M; Okayama H et al. (1996). "Cloning of cDNA for rat eosinophil major basic protein". Biochim. Biophys. Acta 1264 (3): 261–4. doi:10.1016/0167-4781(95)00183-2. PMID 8547309.
- Delcommenne M; Tan C; Gray V et al. (1998). "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase". Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11211–11216. doi:10.1073/pnas.95.19.11211. PMC 21621. PMID 9736715.
PDB gallery
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1h8u: CRYSTAL STRUCTURE OF THE EOSINOPHIL MAJOR BASIC PROTEIN AT 1.8A: AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY
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2brs: EMBP HEPARIN COMPLEX
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Antimicrobial peptides: Granulocyte granule contents
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Azurophilic granules (1°) |
- Myeloperoxidase
- Defensins
- neutral serine proteases (Proteinase 3)
- Lysozyme
- Bactericidal/permeability increasing protein
- Collagenase
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Specific granules (2°) |
Neutrophil
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- Alkaline phosphatase
- Lactoferrin
- Lysozyme
- NADPH oxidase
- Collagenase
- Cathelicidin
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Eosinophil
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- Cathepsin
- Major basic protein
- Eosinophil cationic protein
- Eosinophil peroxidase
- Eosinophil-derived neurotoxin
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Basophil
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see also platelet alpha-granule, dense granule
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Index of cells from bone marrow
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Description |
- Immune system
- Cells
- Physiology
- coagulation
- proteins
- granule contents
- colony-stimulating
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Disease |
- Red blood cell
- Monocyte and granulocyte
- Neoplasms and cancer
- Histiocytosis
- Symptoms and signs
- Blood tests
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Treatment |
- Transfusion
- Drugs
- thrombosis
- bleeding
- other
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UpToDate Contents
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English Journal
- Effect of electron beam on chemical changes of nutrients in infant formula.
- Tesfai A, Beamer SK, Matak KE, Jaczynski J.Author information West Virginia University, Division of Animal and Nutritional Sciences, P.O. Box 6108, Morgantown, WV 26506, USA.AbstractInfant milk formula has recently been implicated as a transmission vehicle for an emerging foodborne pathogen, Enterobacter sakazakii, resulting in high mortality rates. Electron beam (e-beam) efficiently and non-thermally inactivates foodborne pathogens, including E. sakazakii, in infant milk formula. However, the effects of e-beam on chemical changes of nutrients in infant formula have not been determined. Therefore, the objective of this study was to fulfill this gap. Dehydrated infant milk formula was processed with e-beam at 0 (control) to 25 kGy. Amino acid, fatty acid, and mineral profiles (AAP, FAP, and MP, respectively), as well as protein degradation and lipid oxidation, were determined. There were no differences (P>0.05) in FAP, AAP, and MP. SDS-PAGE electrophoresis qualitatively detected three major protein bands in all samples up to 25 kGy. Densitometry analysis of SDS-PAGE gels confirmed no size degradation (P>0.05) as a function of increased e-beam dose. Totol-volatile-basic-nitrogen (TVBN) excluded (P>0.05) protein degradation due to microbial activity. There was no increase (P>0.05) in lipid oxidation, as assessed with thiobarbituric-reactive-substances (TBARS), except in samples processed at 25 kGy. Dehydrated formula has low water activity, which likely protected nutrients from e-beam-induced chemical changes. This study demonstrates that proteins, lipids, and minerals in infant milk formula are stable when processed with e-beam up to 25 kGy at low temperature and under anaerobic conditions.
- Food chemistry.Food Chem.2014 Apr 15;149:208-14. doi: 10.1016/j.foodchem.2013.10.110. Epub 2013 Nov 1.
- Infant milk formula has recently been implicated as a transmission vehicle for an emerging foodborne pathogen, Enterobacter sakazakii, resulting in high mortality rates. Electron beam (e-beam) efficiently and non-thermally inactivates foodborne pathogens, including E. sakazakii, in infant milk formu
- PMID 24295697
- Comparative proteomic analysis of the contractile-protein-depleted fraction from normal versus dystrophic skeletal muscle.
- Carberry S1, Zweyer M2, Swandulla D2, Ohlendieck K3.Author information 1Department of Biology, National University of Ireland, Maynooth, Kildare, Ireland.2Department of Physiology II, University of Bonn, D-53115 Bonn, Germany.3Department of Biology, National University of Ireland, Maynooth, Kildare, Ireland. Electronic address: kay.ohlendieck@nuim.ie.AbstractIn basic and applied myology, gel-based proteomics is routinely used for studying global changes in the protein constellation of contractile fibers during myogenesis, physiological adaptations, neuromuscular degeneration, and the natural aging process. Since the main proteins of the actomyosin apparatus and its auxiliary sarcomeric components often negate weak signals from minor muscle proteins during proteomic investigations, we have here evaluated whether a simple prefractionation step can be employed to eliminate certain aspects of this analytical obstacle. To remove a large portion of highly abundant contractile proteins from skeletal muscle homogenates without the usage of major manipulative steps, differential centrifugation was used to decisively reduce the sample complexity of crude muscle tissue extracts. The resulting protein fraction was separated by two-dimensional gel electrophoresis, and 2D-landmark proteins were identified by mass spectrometry. To evaluate the suitability of the contractile-protein-depleted fraction for comparative proteomics, normal versus dystrophic muscle preparations were examined. The mass spectrometric analysis of differentially expressed proteins, as determined by fluorescence difference in-gel electrophoresis, identified 10 protein species in dystrophic mdx hindlimb muscles. Interesting new biomarker candidates included Hsp70, transferrin, and ferritin, whereby their altered concentration levels in dystrophin-deficient muscle were confirmed by immunoblotting.
- Analytical biochemistry.Anal Biochem.2014 Feb 1;446:108-15. doi: 10.1016/j.ab.2013.08.004. Epub 2013 Aug 14.
- In basic and applied myology, gel-based proteomics is routinely used for studying global changes in the protein constellation of contractile fibers during myogenesis, physiological adaptations, neuromuscular degeneration, and the natural aging process. Since the main proteins of the actomyosin appar
- PMID 23954569
- β-Cyclodextrin Complex Containing Lippia grata Leaf Essential Oil Reduces Orofacial Nociception in Mice - Evidence of Possible Involvement of Descending Inhibitory Pain Modulation Pathway.
- Siqueira-Lima PS, Araújo AA, Lucchese AM, Quintans JS, Menezes PP, Alves PB, de Lucca Júnior W, Santos MR, Bonjardim LR, Quintans-Júnior LJ.Author information Biotechnology Graduate Program, The State University of Feira de Santana, Feira de Santana, BA, Brazil; Department of Pharmacy, Federal University of Sergipe, Aracaju, SE, Brazil.AbstractThe treatment of orofacial pain remains a major challenge for modern medicine. Thus, we prepared and physicochemically characterized a new β-cyclodextrin complex containing Lippia grata leaf essential oil (β-CD/EO) to investigate their possible antinociceptive activity in animal models of orofacial pain. The results of Differential scanning calorimeter (DSC) and Thermogravimetry/derivative thermogravimetry (TG/DTG) showed that the products prepared by Slurry complexation (SC) method were able to incorporate greater amounts of EO. In the X-ray diffractogram, it was shown that complex between EO and β-CD was formed. Male Swiss mice were pre-treated with β-CD/EO (6, 12 or 24 mg/kg, per os, gavage, p.o.), morphine (5 mg/kg, i.p.) or vehicle (distilled water, p.o.) 1 hr before treatment with formalin (20 μL, 2%), capsaicin (20 μL, 2.5 μg) or glutamate (40 μL, 25 μM) into the right upper lip. Our results demonstrated that p.o. treatment with β-CD/EO was significantly (p < 0.05 or p < 0.001) capable of reducing the nociceptive face-rubbing behaviour in both phases of the formalin test. β-CD/EO-treated mice were also significantly (p < 0.05 or p < 0.001) protected against nociception induced by capsaicin and glutamate. For the action in the central nervous system (CNS), ninety minutes after the treatment, the mice were perfused, the brains collected, crioprotected, cut in a criostate and submitted to an immunofluorescence protocol for Fos protein. The immunofluorescence protocol demonstrated that the β-CD/EO significantly activated (p < 0.05; p < 0.01 or p < 0.001) the motor cortex, the Locus ceruleus, the nucleus raphe magnus and the periaqueductal gray of the CNS. These effects apparently did not alter, in tested doses, the motor coordination of mice in the rota-rod test. Our results proposed that β-CD/EO might present an important draft of drug to the study of new compounds for the treatment of orofacial pain.
- Basic & clinical pharmacology & toxicology.Basic Clin Pharmacol Toxicol.2014 Feb;114(2):188-96. doi: 10.1111/bcpt.12145. Epub 2013 Nov 8.
- The treatment of orofacial pain remains a major challenge for modern medicine. Thus, we prepared and physicochemically characterized a new β-cyclodextrin complex containing Lippia grata leaf essential oil (β-CD/EO) to investigate their possible antinociceptive activity in animal models of orofacia
- PMID 24119304
Japanese Journal
- O53-5 Major basic protein (MBP)はRSウイルスによる気道上皮細胞のアポトーシスおよび気道炎症を増強する(O53 気道上皮細胞・線維芽細胞,口演,第63回日本アレルギー学会秋季学術大会)
- 7. 茵〓蒿湯(インチンコウトウ)の肝庇護作用に関する基礎的・臨床的研究 : 特に大量肝切除前投与の有用性について(<特集>外科医のためのKampo EBM UP TO DATE)
- 横山 幸浩,國料 俊男,河合 清貴 [他],水谷 哲史,渡辺 真哉,梛野 正人
- 日本外科学会雑誌 114(5), 256-260, 2013-09-01
- NAID 110009657877
- 泉二 登志子,王 艶華,MOTOJI Toshiko,WANG Yan-Hua
- 東京女子医科大学雑誌 83(E2), E451-E457, 2013-03-31
- … その代表的な機序であるABCトランスポーターは、multidrug resistance 1(MDR1)と産物であるP-glycprotein(P-gp)、ABCG2遺伝子とその産物であるbreast cancer related protein(BCRP)、ABCC1遺伝子の産物であるmultidrug resistance-related protein(MRP1)などがある。 …
- NAID 110009575051
Related Links
- Proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein) Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1H8U, 2BRS Identifiers Symbols PRG2; BMPG; MBP ...
- major basic protein major basic protein An 11-kD major cytotoxic and helminthotoxic protein encoded by PRG2 on chromosome 11q12, which forms a characteristic crystalloid and is found in the granules of eosinophils and other ...
Related Pictures
★リンクテーブル★
[★]
[★]
- 英
- major basic protein、MBP
- 同
- 大基幹蛋白
[★]
好酸球主要塩基性タンパク質
[★]
- 基礎の、基礎的な、基本の、基本的な、(化学)塩基の、塩基性の、ベーシックな
- 関
- basal、base、bases、basically、basicity、basis、cardinal、element、elemental、elementary、essential、essentially、fundamental、fundamentally、fundamentals
[★]
- 関
- cardinal、chief、chiefly、foremost、main、mainly、master、mostly、predominant、predominantly、primarily、primary、principal、principally
[★]