WordNet

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
the 8th letter of the Roman alphabet (同)h
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
bound with chains; "enchained demons strained in anger to gnaw on his bones"; "prisoners in chains" (同)enchained

PrepTutorEJDIC

『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』)》
hydrogenの化学記号
鉛筆の硬度 / 《俗》heroin

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/11/28 21:28:58」(JST)

wiki en

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

^ "Archived copy". Archived from the original on April 19, 2007. Retrieved April 20, 2007. ^{[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^{[full citation needed]} Archived March 23, 2007, at the Wayback Machine.
^ 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.
^ Zhang, Tianyi; Tacchi, Luca; Wei, Zhiguo; Zhao, Yaofeng; Salinas, Irene (2014). "Intraclass diversification of immunoglobulin heavy chain genes in the African lungfish". Immunogenetics. 66 (5): 335–51. doi:10.1007/s00251-014-0769-2. PMC 4348116. PMID 24676685.
^ Ota, T.; Rast, J. P.; Litman, G. W.; Amemiya, C. T. (2003). "Lineage-restricted retention of a primitive immunoglobulin heavy chain isotype within the Dipnoi reveals an evolutionary paradox". Proceedings of the National Academy of Sciences. 100 (5): 2501–6. doi:10.1073/pnas.0538029100. PMC 151370. PMID 12606718.
^ 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（原発性アミロイドーシス）の臨床像、検査所見、および診断 clinical presentation laboratory manifestations and diagnosis of immunoglobulin light chain al amyloidosis primary amyloidosis
2. 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
3. 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
4. 意義未確定の単クローン性免疫グロブリン血症（MGUS）の診断 diagnosis of monoclonal gammopathy of undetermined significance
5. 重度複合型免疫不全（SCID）：特定の欠損 severe combined immunodeficiency scid specific defects

English Journal

VprBP Is Required for Efficient Editing and Selection of Igκ+ B Cells, but Is Dispensable for Igλ+ and Marginal Zone B Cell Maturation and Selection.

Palmer VL1, Aziz-Seible R1, Kassmeier MD1, Rothermund M1, Perry GA1, Swanson PC2.
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2015 Jul 6. pii: 1500952. [Epub ahead of print]
B cell development past the pro-B cell stage in mice requires the Cul4-Roc1-DDB1 E3 ubiquitin ligase substrate recognition subunit VprBP. Enforced Bcl2 expression overcomes defects in distal VH-DJH and secondary Vκ-Jκ rearrangement associated with VprBP insufficiency in B cells and substantially r
PMID 26150531

TLR-9 and IL-15 Synergy Promotes the In Vitro Clonal Expansion of Chronic Lymphocytic Leukemia B Cells.

Mongini PK1, Gupta R2, Boyle E2, Nieto J2, Lee H2, Stein J2, Bandovic J3, Stankovic T4, Barrientos J5, Kolitz JE6, Allen SL6, Rai K6, Chu CC7, Chiorazzi N8.
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2015 Jul 1. pii: 1403189. [Epub ahead of print]
Clinical progression of B cell chronic lymphocytic leukemia (B-CLL) reflects the clone's Ag receptor (BCR) and involves stroma-dependent B-CLL growth within lymphoid tissue. Uniformly elevated expression of TLR-9, occasional MYD88 mutations, and BCR specificity for DNA or Ags physically linked to DN
PMID 26136429

Bruton's Tyrosine Kinase Synergizes with Notch2 To Govern Marginal Zone B Cells in Nonobese Diabetic Mice.

Case JB1, Bonami RH2, Nyhoff LE3, Steinberg HE2, Sullivan AM2, Kendall PL4.
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2015 Jul 1;195(1):61-70. doi: 10.4049/jimmunol.1400803. Epub 2015 Jun 1.
Expansion of autoimmune-prone marginal zone (MZ) B cells has been implicated in type 1 diabetes. To test disease contributions of MZ B cells in NOD mice, Notch2 haploinsufficiency (Notch2(+/-)) was introduced but failed to eliminate the MZ, as it does in C57BL/6 mice. Notch2(+/-)/NOD have MZ B cell
PMID 26034172

Japanese Journal

Maximizing Antibody Production in Suspension-Cultured Mammalian Cells by the Customized Transient Gene Expression Method

YOU Min,LIU Yanning,CHEN Yingwei [他],GUO Jiyuan,WU Jun,FU Yajuan,SHEN Rong,QI Rui,LUO Wenxin,XIA Ningshao
Bioscience, Biotechnology, and Biochemistry 77(6), 1207-1213, 2013
… For 8C11 cAb, coexpressing L-chain and H-chain on different plasmids led to higher yields. …
NAID 130003361090

Clostridium botulinum Type E Toxins Bind to Caco-2 Cells by a Different Mechanism from That of Type A Toxins

Zhang Kai,Yamamoto Yumiko,Suzuki Tomonori,Yokota Kenji,Ma Shaobo,Nengah Dwi Fatmawati Ni,Oguma Keiji
Acta Medica Okayama 66(3), 253-261, 2012-06
… The 7S toxin is cleaved into heavy (H) and light (L) chains by a protease(s) in some strains, and the H chain has 2 domains, the N-terminus (Hn) and C-terminus (Hc). …
NAID 120004247101

N-terminal vacuolar sorting signal at the mouse antibody alters the N-linked glycosylation pattern in suspension-cultured tobacco BY2 cells(PLANT BIOTECHNOLOGY)

Misaki Ryo,Sakai Yohei,Omasa Takeshi [他],Fujiyama Kazuhito,Seki Tatsuji
Journal of bioscience and bioengineering 112(5), 476-484, 2011-11
… In this study, the vacuolar sorting signal (VSS) of sporamin was fused to the heavy (H) and light (L) chains of a mouse monoclonal antibody (mAb), and the mAb was produced in suspension-cultured tobacco BY2 cells. … The sugar chain structures were determined by high-performance liquid chromatography, exoglycosidase digestion, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. …
NAID 110008761512

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★リンクテーブル★

リンク元	「H鎖」
関連記事	「chain」「H」

「H鎖」

　　[★]

英: H chain, H-chain
同: 重鎖 heavy chain
関: 免疫グロブリン、、B細胞、軽鎖 light chain

[show details]

H鎖 : 約 29,200 件
重鎖 : 約 166,000 件

H鎖 免疫グロブリン : 約 27,500 件
重鎖 免疫グロブリン : 約 55,900 件

「chain」

　　[★]

n.

鎖、チェーン

adj.

鎖状の、鎖式の

関: open-chain、strand

「H」

　　[★]

[1] "Archived copy". Archived from the original on April 19, 2007. Retrieved April 20, 2007. ^{[full citation needed]}

[Haas-2] 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.

[Janeway5-3] 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-4] 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.

[wang2013-5] 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.

[6] Fish heavy chain and light chain genes^{[full citation needed]} Archived March 23, 2007, at the Wayback Machine.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.

[12] 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.

[13] 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.

[14] Zhang, Tianyi; Tacchi, Luca; Wei, Zhiguo; Zhao, Yaofeng; Salinas, Irene (2014). "Intraclass diversification of immunoglobulin heavy chain genes in the African lungfish". Immunogenetics. 66 (5): 335–51. doi:10.1007/s00251-014-0769-2. PMC 4348116. PMID 24676685.

[15] Ota, T.; Rast, J. P.; Litman, G. W.; Amemiya, C. T. (2003). "Lineage-restricted retention of a primitive immunoglobulin heavy chain isotype within the Dipnoi reveals an evolutionary paradox". Proceedings of the National Academy of Sciences. 100 (5): 2501–6. doi:10.1073/pnas.0538029100. PMC 151370. PMID 12606718.

[16] 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.

v t e Antibodies

Antibodies	Light chain IGK@ IGL@ surrogate IGLL1 Heavy chain IGH@ IGHM IgA IgD IgE IgG IgM IgY Heavy-chain antibody/IgNAR

see also disorders of globin and globulin proteins

匿名

検索

案内

案内

H-chain