Movatterモバイル変換

[0]ホーム

Пређи на садржај

Glikoprotein 130

Уреди везе

С Википедије, слободне енциклопедије

Interleukin 6 signal transducer (gp130,onkostatin M receptor)

Kristalna struktura Gp130 ekstracelularnog domaina (1p9m).

Dostupne strukture

1bj8,1bqu,1i1r,1p9m,1pvh

Identifikatori

Simboli

IL6ST; CD130; CDw130; GP130; GP130-RAPS; IL6R-beta

Vanjski ID

OMIM: 600694MGI: 96560HomoloGene: 1645GeneCards:IL6ST Gene

Ontologija gena
Molekularna funkcija	•aktivnost receptora •aktivnost interleukin-6 receptora •aktivnost onkostatin-M receptora •vezivanje proteina
Celularna komponenta	•membrana plazme •integralno sa membranom plazme
Biološki proces	•imunski odgovor •transdukcija signala vezana za receptore na ćelijskoj površini •pozitivna regulacija ćelijske proliferacije •regulacija Notch signalinog puta

Ortolozi

Vrsta

Čovek

Miš

RefSeq (mRNA)

RefSeq (protein)

Lokacija (UCSC)

Chr 5:
55.23 - 55.29 Mb

Chr 13:
113.58 - 113.63 Mb

PubMed pretraga

[1]

[2]

Glikoprotein 130 (takođe poznat kaogp130,IL6ST,IL6-beta iliCD130) jetransmembranski protein. On je osnivački član klasecitokinskih receptora. On formira jednupodjedinicu tipa I citokinskih receptora uIL-6 receptorskoj familiji. On se često naziva zajedničkom gp130 podjedinicom, i važan je zasignal transdukciju nakon interakcije sacitokinom. Kao i drugi citokinski receptori tipa I, gp130 poseduje WSXWSaminokiselinski motiv koji osigurava korektnoproteinsko savijanje i vezivanjeliganda. On interaguje saJanus kinazom da bi izazvaointracelularni signal nakon interakcije receptora sa ligandom. Strukturno, gp130 se sastoji od petfibronektin tip-IIIdomena i jednogimunoglobulinu-sličnog C2-tipa domena na njegovom ekstracelularnom delu.^[1]^[2]

Karakteristike

[уреди |уреди извор]

Svi članoviIL-6 receptorske familije formiraju kompleks sa gp130 proteinom, i putem njega prenose signal. Na primer, IL-6 se veže za IL-6 receptor. Kompleks ova dva proteina se onda asocira sa gp130. Taj kompleks od 3 proteina sehomodimerizuje da formiraheksamerni kompleks koji može da proizvede nizvodne signale.^[3] Postoje mnogi drugi proteini koji se asociraju sagp130, kao što sukardiotrofin 1 (CT-1),inhibitorni faktor leukemije (LIF),cilijarni neurotrofni faktor (CNTF),onkostatin M (OSM), iIL-11.^[4] Postoji takođe nekoliko drugih proteina koji imaju strukturnu sličnost sa gp130, sadrže WSXWS motiv i očuvanecisteinske ostatke. Članovi ove grupe su:LIF-R,OSM-R, iG-CSF-R.

Gubitak gp130

[уреди |уреди извор]

gp130 je važan deo mnogih različitih tipova signalnih kompleksa. Inaktivacija gp130 proteina je letalna kodmiševa.^[5]Homozigotni miševi nakon rođenja ispoljavaju brojne defekte, jedan od kojih je poremećeni razvojventrikularnih miokardijuma.Hematopoetski efekti obuhvataju redukovanje brojevastem ćelija uslezini ijetri.

Prenos signala

[уреди |уреди извор]

gp130 nema unutrašnjutirozin kinaznu aktivnost. Umesto toga, on jefosforilisan natirozin ostacima nakonkompleksiranja sa drugimproteinima. Fosforilacija dovodi do asocijacije saJAK/Tyktirozin kinazama iSTAT proteinskim transkripcionim faktorima^[6] Specifično,STAT-3 se aktivira, što dovodi do aktivacije mnogih nizvodnih gena. Drugi putevi aktivacije suRAS iMAPK signalizacija.

Interakcije

[уреди |уреди извор]

Za glikoprotein 130 je bilo pokazanointeraguje saTLE1,^[7]SOCS3,^[8]HER2/neu,^[9]PTPN11,^[8]^[10]^[11]Leukemijski inhibitorni faktor receptorom,^[12]^[13]Grb2,^[14]Janus kinaza 1^[11]^[15]^[16] iSHC1.^[17]

Reference

[уреди |уреди извор]

^Hibi; Murakami, M; Saito, M; Hirano, T; Taga, T; Kishimoto, T; et al. (1990). „Molecular cloning and expression of an IL-6 signal transducer, gp130”.Cell.63 (6): 1149—1157.PMID 2261637.doi:10.1016/0092-8674(90)90411-7.
^Bravo; Staunton, D; Heath, JK; Jones, EY; et al. (1998).„Crystal structure of a cytokine-binding region of gp130”.EMBO J.17 (6): 1665—1674.PMC 1170514 .PMID 9501088.doi:10.1093/emboj/17.6.1665.
^Murakami M, Hibi M, Nakagawa N, Nakagawa T, Yasukawa K, Yamanishi K, Taga T, Kishimoto T (1993).„IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase”.Science.260 (5115): 1808—1810.PMID 8511589.doi:10.1126/science.8511589.
^Kishimoto T, Akira S, Narazaki M, Taga T (1995).„Interleukin-6 family of cytokines and gp130”.Blood.86 (4): 1243—1254.PMID 7632928.
^Yoshida K, Taga T, Saito M, Suematsu S, Kumanogoh A, Tanaka T, Fujiwara H, Hirata M, Yamagami T, Nakahata T, Hirabayashi T, Yoneda Y, Tanaka K, Wang WZ, Mori C, Shiota K, Yoshida N, Kishimoto T (1996).„Targeted disruption of gp130, a common signal transducer for IL-6-family of cytokines, leads to myocardial and hematological disorders”.Proc Natl Acad Sci.93 (1): 407—411.PMC 40247 .PMID 8552649.doi:10.1073/pnas.93.1.407.
^Kishimoto T, Taga T, Akira S (1994). „Cytokine signal transduction”.Cell.76 (2): 253—262.PMID 8293462.doi:10.1016/0092-8674(94)90333-6.
^Liu, Fei; Liu Yin; Li Demin; Zhu Yong; Ouyang Weiming; Xie Xin; Jin Boquan (2002).„The transcription co-repressor TLE1 interacted with the intracellular region of gpl30 through its Q domain”.Mol. Cell. Biochem. Netherlands.232 (1-2): 163—7.ISSN 0300-8177.PMID 12030375.doi:10.1023/A:1014880813692.
^^а ^бLehmann, Ute; Schmitz Jochen; Weissenbach Manuela; Sobota Radoslaw M; Hortner Michael; Friederichs Kerstin; Behrmann Iris; Tsiaris William; Sasaki Atsuo; Schneider-Mergener Jens; Yoshimura Akihiko; Neel Benjamin G; Heinrich Peter C; Schaper Fred (2003).„SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130”.J. Biol. Chem. United States.278 (1): 661—71.ISSN 0021-9258.PMID 12403768.doi:10.1074/jbc.M210552200.
^Grant, Susan L; Hammacher Annet; Douglas Andrea M; Goss Geraldine A; Mansfield Rachel K; Heath John K; Begley C Glenn (2002). „An unexpected biochemical and functional interaction between gp130 and the EGF receptor family in breast cancer cells”.Oncogene. England.21 (3): 460—74.ISSN 0950-9232.PMID 11821958.doi:10.1038/sj.onc.1205100.
^Anhuf D, Weissenbach M, Schmitz J, Sobota R, Hermanns HM, Radtke S, Linnemann S, Behrmann I, Heinrich PC, Schaper F (2000).„Signal transduction of IL-6, leukemia-inhibitory factor, and oncostatin M: structural receptor requirements for signal attenuation”.J. Immunol. UNITED STATES.165 (5): 2535—43.ISSN 0022-1767.PMID 10946280.
^^а ^бKim, H; Baumann H (1997).„Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells”.J. Biol. Chem. UNITED STATES.272 (49): 30741—7.ISSN 0021-9258.PMID 9388212.doi:10.1074/jbc.272.49.30741.
^Timmermann, Andreas; Küster Andrea; Kurth Ingo; Heinrich Peter C; Müller-Newen Gerhard (2002). „A functional role of the membrane-proximal extracellular domains of the signal transducer gp130 in heterodimerization with the leukemia inhibitory factor receptor”.Eur. J. Biochem. Germany.269 (11): 2716—26.ISSN 0014-2956.PMID 12047380.doi:10.1046/j.1432-1033.2002.02941.x.
^Mosley B, De Imus C, Friend D, Boiani N, Thoma B, Park LS, Cosman D (1996).„Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation”.J. Biol. Chem. UNITED STATES.271 (51): 32635—43.ISSN 0021-9258.PMID 8999038.doi:10.1074/jbc.271.51.32635.
^Lee IS, Liu Y, Narazaki M, Hibi M, Kishimoto T, Taga T (1997).„Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”.FEBS Lett. NETHERLANDS.401 (2-3): 133—7.ISSN 0014-5793.PMID 9013873.doi:10.1016/S0014-5793(96)01456-1.
^Haan C, Is'harc H, Hermanns HM, Schmitz-Van De Leur H, Kerr IM, Heinrich PC, Grötzinger J, Behrmann I (2001). „Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction”.J. Biol. Chem. United States.276 (40): 37451—8.ISSN 0021-9258.PMID 11468294.doi:10.1074/jbc.M106135200.
^Haan, Claude; Heinrich Peter C; Behrmann Iris (2002).„Structural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: the receptor is crucial for kinase activation”.Biochem. J. England.361 (Pt 1): 105—11.ISSN 0264-6021.PMC 1222284 .PMID 11742534.doi:10.1042/0264-6021:3610105.
^Giordano V, De Falco G, Chiari R, Quinto I, Pelicci PG, Bartholomew L, Delmastro P, Gadina M, Scala G (1997).„Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase”.J. Immunol. UNITED STATES.158 (9): 4097—103.ISSN 0022-1767.PMID 9126968.

Literatura

[уреди |уреди извор]

Ip NY; Nye SH; Boulton TG; et al. (1992). „CNTF and LIF act on neuronal cells via shared signaling pathways that involve the IL-6 signal transducing receptor component gp130.”.Cell.69 (7): 1121—32.PMID 1617725.doi:10.1016/0092-8674(92)90634-O.
Hibi M; Murakami M; Saito M; et al. (1991). „Molecular cloning and expression of an IL-6 signal transducer, gp130.”.Cell.63 (6): 1149—57.PMID 2261637.doi:10.1016/0092-8674(90)90411-7.
Taga T; Hibi M; Hirata Y; et al. (1989). „Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130.”.Cell.58 (3): 573—81.PMID 2788034.doi:10.1016/0092-8674(89)90438-8.
Rodriguez C; Grosgeorge J; Nguyen VC; et al. (1995). „Human gp130 transducer chain gene (IL6ST) is localized to chromosome band 5q11 and possesses a pseudogene on chromosome band 17p11.”.Cytogenet. Cell Genet.70 (1-2): 64—7.PMID 7736792.doi:10.1159/000133993.
Narazaki M; Yasukawa K; Saito T; et al. (1993).„Soluble forms of the interleukin-6 signal-transducing receptor component gp130 in human serum possessing a potential to inhibit signals through membrane-anchored gp130.”.Blood.82 (4): 1120—6.PMID 8353278.
Davis S; Aldrich TH; Stahl N; et al. (1993).„LIFR beta and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor.”.Science.260 (5115): 1805—8.PMID 8390097.doi:10.1126/science.8390097.
Murakami M; Hibi M; Nakagawa N; et al. (1993).„IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase.”.Science.260 (5115): 1808—10.PMID 8511589.doi:10.1126/science.8511589.
Sharkey AM; Dellow K; Blayney M; et al. (1996). „Stage-specific expression of cytokine and receptor messenger ribonucleic acids in human preimplantation embryos.”.Biol. Reprod.53 (4): 974—81.PMID 8547494.doi:10.1095/biolreprod53.4.974.
Mosley B; De Imus C; Friend D; et al. (1997). „Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation.”.J. Biol. Chem.271 (51): 32635—43.PMID 8999038.doi:10.1074/jbc.271.51.32635.
Lee IS; Liu Y; Narazaki M; et al. (1997).„Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6.”.FEBS Lett.401 (2-3): 133—7.PMID 9013873.doi:10.1016/S0014-5793(96)01456-1.
Auguste P; Guillet C; Fourcin M; et al. (1997).„Signaling of type II oncostatin M receptor.”.J. Biol. Chem.272 (25): 15760—4.PMID 9188471.doi:10.1074/jbc.272.25.15760.
Schiemann WP, Bartoe JL, Nathanson NM (1997).„Box 3-independent signaling mechanisms are involved in leukemia inhibitory factor receptor alpha- and gp130-mediated stimulation of mitogen-activated protein kinase. Evidence for participation of multiple signaling pathways which converge at Ras.”.J. Biol. Chem.272 (26): 16631—6.PMID 9195977.doi:10.1074/jbc.272.26.16631.
Diamant M; Rieneck K; Mechti N; et al. (1997).„Cloning and expression of an alternatively spliced mRNA encoding a soluble form of the human interleukin-6 signal transducer gp130.”.FEBS Lett.412 (2): 379—84.PMID 9256256.doi:10.1016/S0014-5793(97)00750-3.
Koshelnick Y; Ehart M; Hufnagl P; et al. (1997).„Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumor cell line TCL-598.”.J. Biol. Chem.272 (45): 28563—7.PMID 9353320.doi:10.1074/jbc.272.45.28563.
Kim H, Baumann H (1998). „Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells.”.J. Biol. Chem.272 (49): 30741—7.PMID 9388212.doi:10.1074/jbc.272.49.30741.
Bravo J, Staunton D, Heath JK, Jones EY (1998).„Crystal structure of a cytokine-binding region of gp130.”.EMBO J.17 (6): 1665—74.PMC 1170514 .PMID 9501088.doi:10.1093/emboj/17.6.1665.
Barton VA, Hudson KR, Heath JK (1999).„Identification of three distinct receptor binding sites of murine interleukin-11.”.J. Biol. Chem.274 (9): 5755—61.PMID 10026196.doi:10.1074/jbc.274.9.5755.
Hirota H; Chen J; Betz UA; et al. (1999). „Loss of a gp130 cardiac muscle cell survival pathway is a critical event in the onset of heart failure during biomechanical stress.”.Cell.97 (2): 189—98.PMID 10219240.doi:10.1016/S0092-8674(00)80729-1.
Tacken I; Dahmen H; Boisteau O; et al. (1999). „Definition of receptor binding sites on human interleukin-11 by molecular modeling-guided mutagenesis.”.Eur. J. Biochem.265 (2): 645—55.PMID 10504396.doi:10.1046/j.1432-1327.1999.00755.x.
Chung TD; Yu JJ; Kong TA; et al. (2000). „Interleukin-6 activates phosphatidylinositol-3 kinase, which inhibits apoptosis in human prostate cancer cell lines.”.Prostate.42 (1): 1—7.PMID 10579793.doi:10.1002/(SICI)1097-0045(20000101)42:1<1::AID-PROS1>3.0.CO;2-Y.

Spoljašnje veze

[уреди |уреди извор]

Cytokine+Receptor+gp130 наUS National Library of Medicine Medical Subject Headings (MeSH)

п р у PDB Galerija
1bj8: Treći N-terminalni domen (GP130),NMR, minimizovana srednja struktura 1bqu:Citokin-vezujući region (GP130) 1i1r: Kristalna strukturacitokin-receptor kompleksa 1p9m: Kristalna struktura heksamernog ljudskogIL-6/IL-6 alfa receptor/gp130 kompleksa 1pvh: Kristalna struktura inhibitornog faktora leukemije u kompleksu sa gp130

п р у Proteini:klasteri diferencijacije (vidi istospisak ljudskih klastera diferencijacije)
1-50	CD1 (a-c,1A,1D,1E) • CD2 • CD3 (γ,δ,ε) • CD4 • CD5 • CD6 • CD7 • CD8 (a) • CD9 • CD10 • CD11 (a,b,c) • CD13 • CD14 • CD15 • CD16 (A,B) • CD18 • CD19 • CD20 • CD21 • CD22 • CD23 • CD24 • CD25 • CD26 • CD27 • CD28 • CD29 • CD30 • CD31 • CD32 (A,B) • CD33 • CD34 • CD35 • CD36 • CD37 • CD38 • CD39 • CD40 • CD41 • CD42 (a,b,c,d) • CD43 • CD44 • CD45 • CD46 • CD47 • CD48 • CD49 (a,b,c,d,e,f) • CD50
51-100	CD51 • CD52 • CD53 • CD54 • CD55 • CD56 • CD57 • CD58 • CD59 • CD61 • CD62 (E,L,P) • CD63 • CD64 (A,B,C) • CD66 (a,b,c,d,e,f) • CD68 • CD69 • CD70 • CD71 • CD72 • CD73 • CD74 • CD78 • CD79 (a,b) • CD80 • CD81 • CD82 • CD83 • CD84 • CD85 (a,d,e,h,j,k) • CD86 • CD87 • CD88 • CD89 • CD90 • CD91-CD92 • CD93 • CD94 • CD95 • CD96 • CD97 • CD98 • CD99 • CD100
101-150	CD101 • CD102 • CD103 • CD104 • CD105 • CD106 • CD107 (a,b) • CD108 • CD109 • CD110 • CD111 • CD112 • CD113 • CD114 • CD115 • CD116 • CD117 • CD118 • CD119 • CD120 (a,b) • CD121 (a,b) • CD122 • CD123 • CD124 • CD125 • CD126 • CD127 • CD129 • CD130 • CD131 • CD132 • CD133 • CD134 • CD135 • CD136 • CD137 • CD138 • CD140b • CD141 • CD142 • CD143 • CD144 • CD146 • CD147 • CD148 • CD150
151-200	CD151 • CD152 • CD153 • CD154 • CD155 • CD156 (a,b,c) • CD157 • CD158 (a,d,e,i,k) • CD159 (a,c) • CD160 • CD161 • CD162 • CD163 • CD164 • CD166 • CD167 (a,b) • CD168 • CD169 • CD170 • CD171 • CD172 (a,b,g) • CD174 • CD177 • CD178 • CD179 (a,b) • CD181 • CD182 • CD183 • CD184 • CD185 • CD186 • CD191 • CD192 • CD193 • CD194 • CD195 • CD196 • CD197 • CDw198 • CDw199 • CD200
201-250	CD201 • CD202b • CD204 • CD205 • CD206 • CD207 • CD208 • CD209 • CDw210 (a,b) • CD212 • CD213a (1,2) • CD217 • CD218 (a,b) • CD220 • CD221 • CD222 • CD223 • CD224 • CD225 • CD226 • CD227 • CD228 • CD229 • CD230 • CD233 • CD234 • CD235 (a,b) • CD236 • CD238 • CD239 • CD240CE • CD241 • CD243 • CD244 • CD246 • CD247-CD248 • CD249
251-300	CD252 • CD253 • CD254 • CD256 • CD257 • CD258 • CD261 • CD262 • CD264 • CD265 • CD266 • CD267 • CD268 • CD269 • CD271 • CD272 • CD273 • CD274 • CD275 • CD276 • CD278 • CD279 • CD280 • CD281 • CD282 • CD283 • CD284 • CD286 • CD288 • CD289 • CD290 • CD292 • CDw293 • CD294 • CD295 • CD297 • CD298 • CD299
301-350	CD300A • CD301 • CD302 • CD303 • CD304 • CD305 • CD306 • CD307 • CD309 • CD312 • CD314 • CD315 • CD316 • CD317 • CD318 • CD320 • CD321 • CD322 • CD324 • CD325 • CD326 • CD328 • CD329 • CD331 • CD332 • CD333 • CD334 • CD335 • CD336 • CD337 • CD338 • CD339 • CD340 • CD344 • CD349 • CD350

Transmembranski:Imunoglobulinska superfamilija imunskih receptora

Receptori za antitela:
Fc receptor

Epsilon (ε)	FcεRI · (FcεRII jeC-tip lektin)
Gama (γ)	FcγRI • FcγRII • FcγRIII • Neonatalni
Alfa (α)/mu (μ)	FcαRI · Fcα/μR
Sekretorni	Polimerni imunoglobulinski receptor

Receptori za antigene

B ćelije

Antigenski receptor	BCR
Koreceptori	stimuliše:CD21/CD19/CD81 inhibira:CD22
Pomoćni molekuli	Ig-α/Ig-β (CD79)

T ćelije

Ligandi	MHC (MHC klasa I iMHC klasa II)
Antigenski receptor	TCR:TRA@ · TRB@ · TRD@ · TRG@
Koreceptori	CD8 (sa dva glikoproteinska lancaCD8α iCD8β) · CD4
Pomoćni molekuli	CD3 · CD3γ · CD3δ · CD3ε · ζ-lanac (CD3ζ iTCRζ)

Citokinski receptor

Pogledajtecitokinski receptori

Receptori ćelija ubica slični IG

KIR2DL1,KIR2DL2,KIR2DL3,KIR2DL4,KIR2DL5A,KIR2DL5B,KIR2DS1,KIR2DS2,KIR2DS3,KIR2DS4,KIR2DS5,KIR3DL1,KIR3DL2,KIR3DL3,KIR3DS1

Leukocitni receptori slični IG

LILRA1 · LILRA2 · LILRA3 · LILRA4 · LILRA5 · LILRA6 · LILRB1 · LILRB2 · LILRB3 · LILRB4 · LILRB5 · LILRA6 · LILRA5

Citokinski receptori

Hemokinski receptor
(GPCR)

CC hemokinski receptori	CCR1 CCRL1 CCR2 CCRL2 CCR3 CCR4 CCR5 CCR6 CCR7 CCR8 CCR9 CCR10
CXC hemokinski receptori	IL-8 CXCR1 CXCR2 CXCR3 CXCR4 CXCR5 CXCR6 CXCR7
Drugi	CCBP2 CMKLR1 CX3CR1 XCR1

TNF receptor

1-10	TNFRSF1(CD120) TNFRSF1A(CD120a) TNFRSF1B(CD120b) TNFRSF3(Limfotoksin beta receptor) TNFRSF4(CD134) TNFRSF5(CD40) TNFRSF6(FAS) TNFRSF6B TNFRSF7(CD27) TNFRSF8(CD30) TNFRSF9(CD137)
11-20	TNFRSF10A(CD261) TNFRSF10B(CD262) TNFRSF10C(CD263) TNFRSF10D(CD264) TNFRSF11A(CD265/RANK) TNFRSF11B(Osteoprotegerin) TNFRSF12A(CD266) TNFRSF13B(CD267) TNFRSF13C TNFRSF14 (CD268) TNFRSF16(Receptor nervnog faktora rasta) TNFRSF17(CD269) TNFRSF18 TNFRSF19
21-25	TNFRSF21 TNFRSF25 TNFRSF27

JAK-STAT

Tip I	zajednički beta lanac:Interleukinski receptori 3 5 GM-CSF zajednički gama lanac:Interleukinski receptori 2 4 7 9 13/A1/A2 15 21 gp130 koristeći:Interleukinski receptori 6 27) Onkostatin M Leukemija inhibitorni faktor drugiInterleukinski receptori 11/A 12/B1/B2 23 drugiCSF receptori (EPO G-CSF Trombopoietin Hormonski receptor:GH prolaktin
Tip II	Interleukini 10 20 22 28 interferon -α/β -γ

Ig superfamilija

S/T

TGF-beta (1
2)

Drugi

Ćelijska komunikacija:Citokini

Po familiji

Interleukin

IL-1 superfamilija	1 (1Ra) 18 33
poputIL-6/gp130 koristeći	6 11 27 30 31 (+ne ILOnkostatin M Inhibitorni faktor leukemije Cilijarni neurotrofni faktor Kardiotrofin 1)
IL-10 familija	10 19 20 22 24 26
Interferon tip III	28 29
Zajednički γ-lanac familija	2/15 3 4 7 9 13 21
IL-12 familija	12 (B) 23 27 35
Drugi	5 8 14 16 17/25 (A) 32 34

Hemokini

CCL	1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28
CXCL	1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17
CX3CL	1
XCL	1 2

TNF

Glavni	TNF-alfa
TNF (ligand) superfamilija	4-1BB ligand Faktor aktivacije B-ćelija FAS ligand Limfotoksin OX40L RANKL TRAIL
Klaster diferencijacije	CD70 CD153 CD154

Interferon

I	alfa ( Pegilirani 2a Pegilirani 2b), beta (1a 1b)
II	Gama
III	IL-28 IL-29

Drugi

Po funkciji

Protein,glikokonjugat:glikoproteini iglikopeptidi

Mukoproteini

Mucin	CD43 -CD164 -MUC1 -MUC2 -MUC3A -MUC3B -MUC4 -MUC5AC -MUC5B -MUC6 -MUC7 -MUC8 -MUC12 -MUC13 -MUC15 -MUC16 -MUC17 -MUC19 -MUC20
Drugi	Haptoglobin -Unutrašnji faktor -Orosomukoid -Peptidoglikan -Fitohemaglutinin -Ovomucin

Drugi

Aktivin i inhibin • ADAM • Alfa 1-antihimotripsin • Apolipoprotein H • CD70 • Asijaloglikoprotein • Avidin • B-ćelijski aktivacioni faktor • 4-1BB ligand • Kolesterilester transfer protein • Klasterin • Faktor stimulacije kolonije • Hemopeksin • Laktoferin • Membranski glikoproteini • Mijelin protein nula • Osteonektin • Protein C • Protein S • Proteoglikan • Serum amiloid P komponenta • Sialoglikoprotein (CD43,Glikoforin,Glikoforin C) • Trombopoetin • Tiroglobulin • Tiroksin-vezujući proteini • Transkortin • Faktor nekroze tumora-alfa • Uteroglobin • Vitronektin

Преузето из „https://sr.wikipedia.org/w/index.php?title=Glikoprotein_130&oldid=30643511”

Категорије:

Сакривене категорије:

[8]ページ先頭