2001 Fiscal Year Final Research Report Summary
Functinal characterization of human mannose-binding lectin-associated serine protease (MASP) -1/3 and MASP-2
| Project/Area Number |
12670119
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Fukushima Medical University School of Medicine |
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Principal Investigator |
ENDO Yuichi Fukushima Medical University School of medicine, Associate Professor, 医学部, 助教授 (20117427)
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| Project Period (FY) |
2000 – 2001
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| Keywords | complement / lectin pathway / MASP / CLs / Promoter / serine prtease |
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| Research Abstract |
In the lectin pathway, mannose-binding lectin (MBL)-associated serine proteases (MASPs) form complexes with polymeric lectin molecules which are involved in pattern recognition. Upon binding of the recognition molecules to carbohydrates on the surface of microorganisms, MASPs are converted to their active forms and initiate complement activation.
In this study, the 5'-flanking regions of the genes encoding human MASP-1 and MASP-2,Mkey enzymes in the lectin complement pathway, were isolated and characterized. The features of their promoters were compared with those of the human gene for Cls, an effector component of the classical pathway. The sequences upstream from the transcription start sites of the three genes contained the elements essential for transcription and liver-specific expression. Transient expression of constructs of these genes fused to the luciferase reporter gene confirmed their liver-specific expression and showed that the MASP promoters were slightly up-regulated by IL-1β. The stimulatory effects of IL-lβ on MASPl and 2 gene expression were abolished by the simultaneous presence of IL-6. MASPl promoter activity was also down-regulated by IFN-γ. In contrast, Cls promoter activity was strongly up-regulated by BL-6, IL-1β and IFN-1γ. These results suggest that EL-6 and IFN-γ may have a role in switching the host defense system from the lectin pathway to the classical pathway.
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[Publications] Yabuta N, Fujii T, Copeland N G, Gilbert D J, Jenkins N A, Nishiguchi H, Endo Y, Toji S, Tanaka H, Nishimune Y, Nojima H.: "Structure expression and chromosomal mapping of LATS2 a mammalian homologue of the Drosophila tumor suppressor gene lats/wart"Genomics. 63. 263-270 (2000)
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[Publications] Shibuya A, Sawamoto N, Shimizu Y, Shibuya K, Osawa M, Hiroyama T, Eyre HJ, Sutherland GR, Endo Y, Fujita T, Miyabashi T, Sakano S, Tsuji T, Nakayama E, Phillips JH, Lanier LL, Nakauchi H.: "Fca/m receptor mediates endocytosis of TgM-coated microbes"Nature Immunology. 1. 441-446 (2000)
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[Publications] Watabe K, Asada H, Endo Y. Kobayashi T, Kawamoto K, Itami S, Takao S, Shinomura Y, Aikou T, Yoshikawa K, Matsuzawa Y, Kitamura Y, Nojima H.: "Structure expression and chromosome mapping of MLZE a novel gene which is preferentially expressed in metastatic melanoma cells"Jpn J Cancer Res. 92. 140-151 (2001)
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[Publications] Stover C, Endo Y, Takahashi M, Lvnch N, Vorup-Jensen T, Thiel S, Jensenius J, Friedl H, Gregory S, Hankeln T, Fujita T, Schwaeble W.: "The human gene for mannan binding lectin-associated serine protease-2 (MASP-2) the effector componenet of the lectin route of complement activation is part of a tightly linked gene cluster on chromosome lp36.2-3."Genes Immun. 2. 119-127 (2001)
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[Publications] Sekine H, Kenjo A, Azumi K, Ohi G, Takahashi M, Kasukawa R, Ichihara N, Nakata M, Mizuochi T, Matsushita M, Endo Y, Fuiita T.: "An ancient lectin-dependent complement system in an ascidian novel lectin isolated from the plasm of the solitary ascidian Halocynthia roretzi"J Immunol. 167. 4504-4510 (2001)
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