Interleuchina 3

Da Wikipedia, l'enciclopedia libera.
Interleuchina 3
Struttura chimica
Pattern di espressione genetica
Gene
HUGO MCGF
Entrez 3562
Locus Chr. 5 q31.1
Proteina
OMIM 147740
UniProt P08700

L'interleuchina 3, conosciuta anche come IL3, è una proteina codificata dal gene umano IL3[1][2].

Indice

Funzione [modifica]

La IL3 è una interleuchina, una molecola di segnale biologico (citochina) che può intervenire nella risposta naturale del corpo alle malattie, come parte del sistema immunitario. Agisce legandosi ai recettori per interleuchina-3.

La IL3 stimola la differenziazione delle cellule staminali emopoietiche multipotenti in cellule progenitrici mieloidi (a differenza delle cellule progenitrici linfoidi, dove la differenziazione è stimolata dalla interleuchina 7), e stimola la proliferazione di tutte le cellule della linea mieloide (globuli rossi, megacariociti, granulociti, monociti e cellule dendritiche). È secreto in seguito all'attivazione delle cellule T per sostenere la crescita e la differenziazione delle cellule T dal midollo osseo in una risposta immunitaria. Il gene umano IL3 codifica una proteina di 152 amminoacidi.

Il gene umano dell'IL3 si trova nel cromosoma 5, a sole 9 coppie di basi di distanza dal gene GM-CSF che codifica per un fattore di crescita dei granulociti e monociti, la cui funzione è molto simile a quella dell'IL3.

Scoperta [modifica]

L'interleuchina 3 fu scoperta da James N. Ihle nei topi. Egli trovò un fattore derivato dalla cellula T che induceva la sintesi di 20alpha-idrossisteroido-deidrogenasi in cellule ematopoietiche e lo definì interleuchina-3. [3][4].

Interazioni [modifica]

L'interleuchina 3 si lega mediante interazione proteina-proteina al suo recettore specifico, detto IL3RA (recettore alfa, a bassa affinità)[5][6].

Altre letture [modifica]

  • Wagemaker G, Burger H, van Gils FC, et al. (1991). Interleukin-3.. Biotherapy (Dordrecht, Netherlands) 2 (4): 337–45. PMID 2268499.
  • Martinez-Moczygemba M, Huston DP (2003). Biology of common beta receptor-signaling cytokines: IL-3, IL-5, and GM-CSF.. J. Allergy Clin. Immunol. 112 (4): 653–65; quiz 666. DOI:10.1016/S0091. PMID 14564341.
  • Mroczko B, Szmitkowski M (2005). Hematopoietic cytokines as tumor markers.. Clin. Chem. Lab. Med. 42 (12): 1347–54. DOI:10.1515/CCLM.2004.253. PMID 15576295.
  • Kitamura T, Sato N, Arai K, Miyajima A (1991). Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors.. Cell 66 (6): 1165–74. DOI:10.1016/0092-8674(91)90039-2. PMID 1833064.
  • Urdal DL, Price V, Sassenfeld HM, et al. (1989). Molecular characterization of colony-stimulating factors and their receptors: human interleukin-3.. Ann. N. Y. Acad. Sci. 554: 167–76. DOI:10.1111/j.1749-6632.1989.tb22418.x. PMID 2544122.
  • Otsuka T, Miyajima A, Brown N, et al. (1988). Isolation and characterization of an expressible cDNA encoding human IL-3. Induction of IL-3 mRNA in human T cell clones.. J. Immunol. 140 (7): 2288–95. PMID 3127463.
  • Yang YC, Ciarletta AB, Temple PA, et al. (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. DOI:10.1016/0092-8674(86)90360-0. PMID 3489530.
  • Le Beau MM, Epstein ND, O'Brien SJ, et al. (1987). The interleukin 3 gene is located on human chromosome 5 and is deleted in myeloid leukemias with a deletion of 5q.. Proc. Natl. Acad. Sci. U.S.A. 84 (16): 5913–7. DOI:10.1073/pnas.84.16.5913. PMID 3497400.
  • Dorssers L, Burger H, Bot F, et al. (1987). Characterization of a human multilineage-colony-stimulating factor cDNA clone identified by a conserved noncoding sequence in mouse interleukin-3.. Gene 55 (1): 115–24. DOI:10.1016/0378-1119(87)90254-X. PMID 3497843.
  • Chirmule N, Goonewardena H, Pahwa S, et al. (1995). HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells.. J. Biol. Chem. 270 (33): 19364–9. DOI:10.1074/jbc.270.33.19364. PMID 7642615.
  • Than S, Oyaizu N, Pahwa RN, et al. (1994). Effect of human immunodeficiency virus type-1 envelope glycoprotein gp160 on cytokine production from cord-blood T cells.. Blood 84 (1): 184–8. PMID 8018916.
  • Le Beau MM, Espinosa R, Neuman WL, et al. (1993). Cytogenetic and molecular delineation of the smallest commonly deleted region of chromosome 5 in malignant myeloid diseases.. Proc. Natl. Acad. Sci. U.S.A. 90 (12): 5484–8. DOI:10.1073/pnas.90.12.5484. PMID 8516290.
  • Stomski FC, Sun Q, Bagley CJ, et al. (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. PMID 8649415.
  • Feng Y, Klein BK, McWherter CA (1996). Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3.. J. Mol. Biol. 259 (3): 524–41. DOI:10.1006/jmbi.1996.0337. PMID 8676386.
  • Vanhaesebroeck B, Welham MJ, Kotani K, et al. (1997). P110delta, a novel phosphoinositide 3-kinase in leukocytes.. Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4330–5. DOI:10.1073/pnas.94.9.4330. PMID 9113989.
  • Klein BK, Feng Y, McWherter CA, et al. (1997). The receptor binding site of human interleukin-3 defined by mutagenesis and molecular modeling.. J. Biol. Chem. 272 (36): 22630–41. DOI:10.1074/jbc.272.36.22630. PMID 9278420.
  • Sanchez X, Suetomi K, Cousins-Hodges B, et al. (1998). CXC chemokines suppress proliferation of myeloid progenitor cells by activation of the CXC chemokine receptor 2.. J. Immunol. 160 (2): 906–10. PMID 9551928.
  • Tabira T, Chui DH, Fan JP, et al. (1998). Interleukin-3 and interleukin-3 receptors in the brain.. Ann. N. Y. Acad. Sci. 840: 107–16. DOI:10.1111/j.1749-6632.1998.tb09554.x. PMID 9629242.
  • Nilsen EM, Johansen FE, Jahnsen FL, et al. (1998). Cytokine profiles of cultured microvascular endothelial cells from the human intestine.. Gut 42 (5): 635–42. PMID 9659156.

Note [modifica]

  1. ^ Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)
  2. ^ Yang YC, Ciarletta AB, Temple PA, Chung MP, Kovacic S, Witek-Giannotti JS, Leary AC, Kriz R, Donahue RE, Wong GG (ottobre 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. DOI:10.1016/0092-8674(86)90360-0. PMID 3489530.
  3. ^ Ihle JN, Pepersack L, Rebar L (giugno 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.
  4. ^ Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). Interleukin 3. Meth. Enzymol. 116: 540–52. DOI:10.1016/S0076-6879(85)16042-8. PMID 3003517.
  5. ^ Stomski, F C, Sun Q, Bagley C J, Woodcock J, Goodall G, Andrews R K, Berndt M C, Lopez A F (Jun. 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.
  6. ^ Woodcock, J M, Zacharakis B, Plaetinck G, Bagley C J, Qiyu S, Hercus T R, Tavernier J, Lopez A F (Nov. 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.
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