| Project/Area Number |
08670372
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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 |
Immunology
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| Research Institution | Fukushima Medical University |
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Principal Investigator |
MATSUSHITA Misao Fukushima Medical University, School of Medicine, Assistant Professor, 医学部, 講師 (00165812)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1997: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1996: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | complement / lectin pathway / MBL / MASP / sMAP / マンノース結合蛋白 / P22 |
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| Research Abstract |
Mannose-binding lectin (MBL, also called MBP) is associated with two types of serine protease, MASP-1 and MASP-2, which are structually homologous. Upon binding to carbohydrates such as mannose on pathogens, the MBL-MASP complex activates the lectin complement pathway. The aim of this research was to elucidate the activation mechamism of the lectin pathway. We obtained the following results.
1) A 22kDa protein (sMAP) is present in an MBL-MASP preparation and is associated with MASP-1. cDNA analysis of sMAP revealed that sMAP is derived from the MASP-2 gene by alternative polyadenylation.
2) We developed an ELISA for MASP-1 levels in human serum and found that MBL and MASP-1 levels in serum are not correlated in the individual, and that MASP-1 exists as MBL-bound and MBL-unbound forms, the latter of which is associated with sMAP in part.
3) MASP-1 and MASP-2 exhibit proteolytic activities towards C3 and C4, respectively.
4) MBL exists as a homopolymer with various sizes. Analysis of one of MBL homopolymers revealed that it copurified with MASP-1 and sMAP but not with MASP-2.
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