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Proteolytic Activities of Two Types of Mannose-Binding Lectin-Associated Serine Protease
Open accessAbstract
Mannose (or mannan)-binding lectin (MBL) is an oligomeric serum lectin that plays a role in innate immunity by activating the complement system. In human, two types of MBL-associated serine protease (MASP-1 and MASP-2) and a truncated protein of MASP-2 (small MBL-associated protein; sMAP or MAp19) are complexed with MBL. To clarify the proteolytic activities of MASP-1 and MASP-2 against C4, C2, and C3, we isolated these two types of MASP in activated forms from human serum by sequential affinity chromatography. On an anti-MASP-1 column, MASP-2 passed through the column in the presence of EDTA and high salt concentration, whereas MASP-1 was retained. Isolated MASP-1 and MASP-2 exhibited proteolytic activities against C3 and C4, respectively. C2 was activated by both MASPs. C1 inhibitor (C1 INH), an inhibitor for C1r and C1s, formed equimolar complexes with MASP-1 and MASP-2 and inhibited their proteolytic activities.
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Cited by
Ehrnthaller, C., Ignatius, A., Gebhard, F., & Huber-Lang, M. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00149 · Cited by 226
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Swierzko, A. S., Cedzynski, M., Domzalska-Popadiuk, I., MacDonald, S. L., Borkowska-Klos, M., Atkinson, A. P. M., Szala, A., Jopek, A., Jensenius, J. C., Kawakami, M., et al. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.02.022 · Cited by 35
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Metadata
- Authors
- Matsushita, M., Thiel, S., Jensenius, J. C., Terai, I., & Fujita, T.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2000-09-01
- Volume
- 165
- Issue
- 5
- Pages
- 2637-2642
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2119423436
- Cited by
- 318
- References
- 0
- FWCI
- 6.86
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Matsushita, M., Thiel, S., Jensenius, J. C., Terai, I., & Fujita, T. (2000). Proteolytic Activities of Two Types of Mannose-Binding Lectin-Associated Serine Protease. The Journal of Immunology. https://doi.org/10.4049/jimmunol.165.5.2637
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