Interleucina 3

Interleucina 3
Identificadores
Símbolo	IL3
Símbolos alt.	IL-3; MCGF; MULTI-CSF
Entrez	3562
OMIM	147740
PDB	1JLI
RefSeq	NP_000579
UniProt	P08700
Outros datos
Locus	Cr. 5 :(131.4 – 131.4 Mb)

A interleucina 3, abreviada como IL-3 (ou IL3), é unha proteína reguladora inmunitaria do tipo das interleucinas, que nos humanos está codificada no xene IL3 do cromosoma 5.^[1]^[2] O xene humano da IL-3 codifica unha proteína de 152 aminoácidos, e a IL-3 natural está glicosilada. O xene humano da IL-3, está situado a só 9 kb do xene do GM-CSF, e a súa función é bastante similar á deste.

Función

A interleucina 3 (IL-3) é unha interleucina, un tipo de sinal químico biolóxico (citocina) que pode mellorar a resposta natural do corpo ás doenzas como parte do sistema inmunitario. Actúa uníndose ao receptor da interleucina 3.

A IL-3 estimula a diferenciación das células nai hematopoéticas multipotentes en células proxenitoras mieloides ou, coa adición de IL-7, en células proxenitoras linfoides. Ademais, a IL-3 estimula a proliferación de todas as células da liñaxe mieloide (granulocitos, monocitos, e células dendríticas), en conxunción con outras citocinas, por exemplo, a eritropoetina (EPO), factor estimulante das colonias de granulocitos-macrófagos (GM-CSF), e IL-6. É segregada polos basófilos e por células T activadas para apoiar o crecemento e diferenciación das células T nas respostas imunitarias. As células T activadas poden inducir a súa propia proliferación e diferenciación por sinalización autócrinsa ou poden inducilas noutras células T por sinalización parácrina, e en ambos os casos está implicada a unión de IL-2 ao receptor de IL-2 das células T (regulado á alza cando se activa a célula, baixo a indución feita pola IL-1 segregada por macrófagos).

Descubrimento

A interleucina 3 descubriuna JN Ihle orixinariamente nos ratos. Atopou un factor derivado das células T que inducía a síntese de 20alfa-hidroxiesteroide deshidroxenase en células hematopoéticas e denominouno interleucina 3.^[3]^[4]

Interactions

A interleucina 3 presenta interaccións con IL3RA.^[5]^[6]

Notas

↑ "Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)".
↑ Yang YC, Ciarletta AB, Temple PA, Chung MP, Kovacic S, Witek-Giannotti JS, Leary AC, Kriz R, Donahue RE, Wong GG (October 1986). "Human IL-3 (multi-CSF): identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3". Cell 47 (1): 3–10. PMID 3489530. doi:10.1016/0092-8674(86)90360-0.
↑ Ihle JN, Pepersack L, Rebar L (June 1981). "Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid dehydrogenase in splenic lymphocytes from athymic mice by a unique lymphokine". J. Immunol. 126 (6): 2184–9. PMID 6971890.
↑ Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). "Interleukin 3". Meth. Enzymol. Methods in Enzymology 116: 540–52. ISBN 978-0-12-182016-9. PMID 3003517. doi:10.1016/S0076-6879(85)16042-8.
↑ Stomski FC, Sun Q, Bagley CJ, Woodcock J, Goodall G, Andrews RK, Berndt MC, Lopez AF (June 1996). "Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding". Mol. Cell. Biol. 16 (6): 3035–46. PMC 231298. PMID 8649415.
↑ Woodcock JM, Zacharakis B, Plaetinck G, Bagley CJ, Qiyu S, Hercus TR, Tavernier J, Lopez AF (November 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. 13 (21): 5176–85. PMC 395466. PMID 7957082.

Véxase tamén

Bibliografía

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[entrez-1] "Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)".

[pmid3489530-2] Yang YC, Ciarletta AB, Temple PA, Chung MP, Kovacic S, Witek-Giannotti JS, Leary AC, Kriz R, Donahue RE, Wong GG (October 1986). "Human IL-3 (multi-CSF): identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3". Cell 47 (1): 3–10. PMID 3489530. doi:10.1016/0092-8674(86)90360-0.

[pmid6971890-3] Ihle JN, Pepersack L, Rebar L (June 1981). "Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid dehydrogenase in splenic lymphocytes from athymic mice by a unique lymphokine". J. Immunol. 126 (6): 2184–9. PMID 6971890.

[pmid3003517-4] Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). "Interleukin 3". Meth. Enzymol. Methods in Enzymology 116: 540–52. ISBN 978-0-12-182016-9. PMID 3003517. doi:10.1016/S0076-6879(85)16042-8.

[pmid8649415-5] Stomski FC, Sun Q, Bagley CJ, Woodcock J, Goodall G, Andrews RK, Berndt MC, Lopez AF (June 1996). "Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding". Mol. Cell. Biol. 16 (6): 3035–46. PMC 231298. PMID 8649415.

[pmid7957082-6] Woodcock JM, Zacharakis B, Plaetinck G, Bagley CJ, Qiyu S, Hercus TR, Tavernier J, Lopez AF (November 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. 13 (21): 5176–85. PMC 395466. PMID 7957082.

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