免疫グロブリン重鎖

WordNet

unusually great in degree or quantity or number; "heavy taxes"; "a heavy fine"; "heavy casualties"; "heavy losses"; "heavy rain"; "heavy traffic"
a serious (or tragic) role in a play
an actor who plays villainous roles
slowly as if burdened by much weight; "time hung heavy on their hands" (同)heavily
requiring or showing effort; "heavy breathing"; "the subject made for labored reading" (同)labored, laboured
lacking lightness or liveliness; "heavy humor"; "a leaden conversation" (同)leaden
darkened by clouds; "a heavy sky" (同)lowering, sullen, threatening
slow and laborious because of weight; "the heavy tread of tired troops"; "moved with a lumbering sag-bellied trot"; "ponderous prehistoric beasts"; "a ponderous yawn" (同)lumbering, ponderous
(of sleep) deep and complete; "a heavy sleep"; "fell into a profound sleep"; "a sound sleeper"; "deep wakeless sleep" (同)profound, sound, wakeless
full and loud and deep; "heavy sounds"; "a herald chosen for his sonorous voice" (同)sonorous
full of; bearing great weight; "trees heavy with fruit"; "vines weighed down with grapes" (同)weighed down
(of an actor or role) being or playing the villain; "Iago is the heavy role in `Othello"
(physics, chemistry) being or containing an isotope with greater than average atomic mass or weight; "heavy hydrogen"; "heavy water"
dense or inadequately leavened and hence likely to cause distress in the alimentary canal; "a heavy pudding"
large and powerful; especially designed for heavy loads or rough work; "a heavy truck"; "heavy machinery"
made of fabric having considerable thickness; "a heavy coat"
marked by great psychological weight; weighted down especially with sadness or troubles or weariness; "a heavy heart"; "a heavy schedule"; "heavy news"; "a heavy silence"; "heavy eyelids"
of comparatively great physical weight or density; "a heavy load"; "lead is a heavy metal"; "heavy mahogany furniture"
of great intensity or power or force; "a heavy blow"; "the fighting was heavy"; "heavy seas"
of relatively large extent and density; "a heavy line"
of the military or industry; using (or being) the heaviest and most powerful armaments or weapons or equipment; "heavy artillery"; "heavy infantry"; "a heavy cruiser"; "heavy guns"; "heavy industry involves large-scale production of basic products (such as steel) used by other industries"
sharply inclined; "a heavy grade"
fasten or secure with chains; "Chain the chairs together"
a unit of length
a necklace made by a stringing objects together; "a string of beads"; "a strand of pearls"; (同)string, strand
a linked or connected series of objects; "a chain of daisies"
a series of (usually metal) rings or links fitted into one another to make a flexible ligament
anything that acts as a restraint
(chemistry) a series of linked atoms (generally in an organic molecule) (同)chemical chain
a series of things depending on each other as if linked together; "the chain of command"; "a complicated concatenation of circumstances" (同)concatenation
(business) a number of similar establishments (stores or restaurants or banks or hotels or theaters) under one ownership
connect or arrange into a chain by linking
a class of proteins produced in lymph tissue in vertebrates and that function as antibodies in the immune response (同)Ig, immune serum globulin, immune gamma globulin, immune_globulin
British biochemist (born in Germany) who isolated and purified penicillin, which had been discovered in 1928 by Sir Alexander Fleming (1906-1979) (同)Ernst Boris Chain, Sir Ernst Boris Chain

PrepTutorEJDIC

『重い』,重量のある / (分量・程度・規模・強さなどが)『激しい』,大きい, / 『厳しい』,耐えがたい,つらい / 悲しい,陰気な / (動作が)のろい,ぎこちない / ものうい,だるい / (空が)曇った,うっとうしい,(海が)荒れた / (食物が)消化の悪い / 敵役,悪役
『鎖』;(装飾用の)鎖 / 《複数形で》『束縛』,拘束;囚人をつなぐ鎖 / (物事の)『連続』,つながり《+『of』+『名』》 / (商店・銀行・ホテルなどの)チェーン(一連の店が同一資本のもとで連携して経営される方式;その店) / チェーン(測量で用いられる単位;約21.7m) / …'を'『鎖でつなぐ』《+『up』(『together』)+『名,』+『名』+『up』(『together』)》

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/15 03:27:36」(JST)

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Schematic diagram of a typical antibody showing two Ig heavy chains (blue) linked by disulfide bonds to two Ig light chains (green). The constant (C) and variable (V) domains are shown.

An antibody molecule. The two heavy chains are colored red and blue and the two light chains green and yellow.^[1]

The immunoglobulin heavy chain (IgH) is the large polypeptide subunit of an antibody (immunoglobulin).

A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains. Several different types of heavy chain exist that define the class or isotype of an antibody. These heavy chain types vary between different animals. All heavy chains contain a series of immunoglobulin domains, usually with one variable domain (V_H) that is important for binding antigen and several constant domains (C_H1, C_H2, etc.).

The heavy chain doesn't always have to bind to a light chain. Pre-B lymphocytes can synthesize heavy chain in the absence of light chain, which then can allow the heavy chain to bind to a heavy-chain binding protein.^[2]

In mammals

Classes

There are five types of mammalian immunoglobulin heavy chain: γ, δ, α, μ and ε.^[3] They define classes of immunoglobulins: IgG, IgD, IgA, IgM and IgE, respectively.

Heavy chains α and γ have approximately 450 amino acids.
Heavy chains μ and ε have approximately 550 amino acids.^[3]

Regions

Each heavy chain has two regions:

a constant region (which is the same for all immunoglobulins of the same class but differs between classes).
- Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.^[4]
- Heavy chains μ and ε have a constant region composed of four domains.^[3]
a variable region that differs between different B cells, but is the same for all immunoglobulins produced by the same B cell or B cell clone. The variable domain of any heavy chain is composed of a single immunoglobulin domain. These domains are about 110 amino acids long.^{[citation needed]}

Cows

Cows, specifically Bos Taurus, show a variation on the general mammalian theme in which the heavy chain CDR H3 region has adapted to produce a divergent repertoire of antibodies which present a "stalk and knob" antigen interaction surface instead of the more familiar bivalent tip surface.^[5] The bovine CDR is unusually long and contains unique sequence attributes which support the production of paired cysteine residues during somatic hypermutation.^[5] Thus, where in humans the somatic hypermutation step targets the V(D)J recombination process, the target in cows is on the creation of diverse disulfide bonds and the generation of unique sets of loops which interact with antigen.^[5] A speculated evolutionary driver for this variation is the presence of a vastly more diverse microbial environment in the digestive system of the cow as a consequence of their being ruminants.^[5]

In fish

Jawed fish appear to be the most primitive animals that are able to make antibodies like those described for mammals.^[6] However, fish do not have the same repertoire of antibodies that mammals possess.^[7] Three distinct Ig heavy chains have so far been identified in bony fish.

The first identified was the μ (or mu) heavy chain that is present in all jawed fish and is the heavy chain for what is thought to be the primordial immunoglobulin. The resulting antibody, IgM, is secreted as a tetramer in teleost fish instead of the typical pentamer found in mammals and sharks.^{[citation needed]}
The heavy chain (δ) for IgD was identified initially from the channel catfish and Atlantic salmon and is now well documented for many teleost fish.^[8]
The third teleost Ig heavy chain gene was identified very recently and does not resemble any of the heavy chains so far described for mammals. This heavy chain, identified in both rainbow trout (τ)^[9] and zebrafish (ζ),^[10] could potentially form a distinct antibody isotype (IgT or IgZ) that may precede IgM in evolutionary terms.

Similar to the situation observed for bony fish, three distinct Ig heavy chain isotypes have been identified in cartilaginous fish. With the exception of μ, these Ig heavy chain isotypes appear to be unique to cartilaginous fish. The resulting antibodies are designated IgW (also called IgX or IgNARC) and IgNAR ('immunoglobulin new antigen receptor').^[11]^[12] The latter type is a heavy-chain antibody, an antibody lacking light chains, and can be used to produce single-domain antibodies, which are essentially the variable domain of an IgNAR.^[13]

IgW has now also been found in the group of lobe finned fishes including the coelacanth and lungfish. The IgW1 and IgW2 in coelacanth has a usual (VD)n-Jn-C structure as well has having a large number of constant domains.^[14]^[15]

In amphibians

Frogs can synthesize IgX and IgY. ^[16]

References

^ http://www.emc.maricopa.edu/faculty/farabee/BIOBK/ANTIBODY.gif^{[full citation needed]}
^ Haas, Ingrid G.; Wabl, Matthias (1983). "Immunoglobulin heavy chain binding protein". Nature 306 (5941): 387–9. Bibcode:1983Natur.306..387H. doi:10.1038/306387a0. PMID 6417546.
^ ^a ^b ^c Janeway CA, Jr.; et al. (2001). Immunobiology (5th ed.). Garland Publishing. ISBN 0-8153-3642-X. (electronic full text via NCBI Bookshelf). ^{[page needed]}
^ Woof, Jenny M.; Burton, Dennis R. (2004). "Human antibody–Fc receptor interactions illuminated by crystal structures". Nature Reviews Immunology 4 (2): 89–99. doi:10.1038/nri1266. PMID 15040582.
^ ^a ^b ^c ^d Wang, Feng; Ekiert, Damian C.; Ahmad, Insha; Yu, Wenli; Zhang, Yong; Bazirgan, Omar; Torkamani, Ali; Raudsepp, Terje; Mwangi, Waithaka; Criscitiello, Michael F.; Wilson, Ian A.; Schultz, Peter G.; Smider, Vaughn V. (2013). "Reshaping Antibody Diversity". Cell 153 (6): 1379–93. doi:10.1016/j.cell.2013.04.049. PMID 23746848.
^ Fish heavy chain and light chain genes
^ Bengtén, Eva; Clem, L. William; Miller, Norman W.; Warr, Gregory W.; Wilson, Melanie (2006). "Channel catfish immunoglobulins: Repertoire and expression". Developmental & Comparative Immunology 30: 77. doi:10.1016/j.dci.2005.06.016.
^ Solem, Stein Tore; Stenvik, Jørgen (2006). "Antibody repertoire development in teleosts—a review with emphasis on salmonids and Gadus morhua L". Developmental & Comparative Immunology 30: 57. doi:10.1016/j.dci.2005.06.007.
^ Hansen, J. D.; Landis, E. D.; Phillips, R. B. (2005). "Discovery of a unique Ig heavy-chain isotype (IgT) in rainbow trout: Implications for a distinctive B cell developmental pathway in teleost fish". Proceedings of the National Academy of Sciences 102 (19): 6919–6924. Bibcode:2005PNAS..102.6919H. doi:10.1073/pnas.0500027102. JSTOR 3375456. PMC 1100771. PMID 15863615.
^ Danilova, Nadia; Bussmann, Jeroen; Jekosch, Kerstin; Steiner, Lisa A (2005). "The immunoglobulin heavy-chain locus in zebrafish: Identification and expression of a previously unknown isotype, immunoglobulin Z". Nature Immunology 6 (3): 295–302. doi:10.1038/ni1166. PMID 15685175.
^ Dooley, H.; Flajnik, M.F. (2006). "Antibody repertoire development in cartilaginous fish". Developmental & Comparative Immunology 30: 43. doi:10.1016/j.dci.2005.06.022.
^ Simmons, David P.; Abregu, Fiona A.; Krishnan, Usha V.; Proll, David F.; Streltsov, Victor A.; Doughty, Larissa; Hattarki, Meghan K.; Nuttall, Stewart D. (2006). "Dimerisation strategies for shark IgNAR single domain antibody fragments". Journal of Immunological Methods 315 (1–2): 171–84. doi:10.1016/j.jim.2006.07.019. PMID 16962608.
^ Wesolowski, Janusz; Alzogaray, Vanina; Reyelt, Jan; Unger, Mandy; Juarez, Karla; Urrutia, Mariela; Cauerhff, Ana; Danquah, Welbeck; Rissiek, Björn; Scheuplein, Felix; Schwarz, Nicole; Adriouch, Sahil; Boyer, Olivier; Seman, Michel; Licea, Alexei; Serreze, David V.; Goldbaum, Fernando A.; Haag, Friedrich; Koch-Nolte, Friedrich (2009). "Single domain antibodies: Promising experimental and therapeutic tools in infection and immunity". Medical Microbiology and Immunology 198 (3): 157–74. doi:10.1007/s00430-009-0116-7. PMC 2714450. PMID 19529959.
^ http://www.ncbi.nlm.nih.gov/nuccore/407080573^{[full citation needed]}
^ http://www.ncbi.nlm.nih.gov/pubmed/?term=IgW+Protopterus^{[full citation needed]}
^ Du, Christina C.; Mashoof, Sara M.; Criscitiello, Michael F. (2012). "Oral immunization of the African clawed frog (Xenopus laevis) upregulates the mucosal immunoglobulin IgX". Veterinary Immunology and Immunopathology 145 (1–2): 493–8. doi:10.1016/j.vetimm.2011.10.019. PMC 3273591. PMID 22100190.

External links

Immunoglobulin Heavy Chains at the US National Library of Medicine Medical Subject Headings (MeSH)
Educational Resource for Heavy Chain Analysis

UpToDate Contents

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1. 免疫グロブリン軽鎖（AL）アミロイドーシスおよび軽鎖重鎖沈着症の病因 pathogenesis of immunoglobulin light chain al amyloidosis and light and heavy chain deposition diseases
2. 免疫遺伝学 immunoglobulin genetics
3. 免疫グロブリンの構造 structure of immunoglobulins
4. 多発性骨髄腫の病理生物学 pathobiology of multiple myeloma
5. 免疫グロブリン軽鎖（AL）アミロイドーシスおよび軽鎖重鎖沈着症の予後および治療 prognosis and treatment of immunoglobulin light chain al amyloidosis and light and heavy chain deposition diseases

English Journal

The urodele amphibian Pleurodeles waltl has a diverse repertoire of immunoglobulin heavy chains with polyreactive and species-specific features.

Fonte C1, Gruez A2, Ghislin S1, Frippiat JP3.
Developmental and comparative immunology.Dev Comp Immunol.2015 Dec;53(2):371-84. doi: 10.1016/j.dci.2015.08.006. Epub 2015 Aug 13.
Urodele amphibians are an interesting model because although they possess the cardinal elements of the vertebrate immune system, their immune response is apparently subdued. This phenomenon, sometimes regarded as a state of immunodeficiency, has been attributed by some authors to limited antibody di
PMID 26277106

Equine immunoglobulins and organization of immunoglobulin genes.

Walther S1, Rusitzka TV2, Diesterbeck US3, Czerny CP4.
Developmental and comparative immunology.Dev Comp Immunol.2015 Dec;53(2):303-19. doi: 10.1016/j.dci.2015.07.017. Epub 2015 Jul 26.
Our understanding of how equine immunoglobulin genes are organized has increased significantly in recent years. For equine heavy chains, 52 IGHV, 40 IGHD, 8 IGHJ and 11 IGHC are present. Seven of these IGHCs are gamma chain genes. Sequence diversity is increasing between fetal, neonatal, foal and ad
PMID 26219564

A novel variable antibody fragment dimerized by leucine zippers with enhanced neutralizing potency against rabies virus G protein compared to its corresponding single-chain variable antibody fragment.

Li Z1, Cheng Y1, Xi H1, Gu T2, Yuan R1, Chen X1, Jiang C2, Kong W3, Wu Y4.
Molecular immunology.Mol Immunol.2015 Dec;68(2 Pt A):168-75. doi: 10.1016/j.molimm.2015.06.027. Epub 2015 Aug 29.
Fatal rabies can be prevented effectively by post-exposure prophylactic (PEP) with rabies immunoglobulin (RIG). Single-chain variable fragments (scFv), which are composed of a variable heavy chain (VH) and a variable light chain (VL) connected by a peptide linker, can potentially be used to replace
PMID 26325475

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リンク元	「免疫グロブリン重鎖」
拡張検索	「immunoglobulin heavy chain gene」「immunoglobulin heavy chain deletion」
関連記事	「heaving」「heavy」「chain」