Cutting Edge: Complement-Activating Complex of Ficolin and Mannose-Binding Lectin-Associated Serine Protease

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P 144: Sunflower Mannose binding Lectin-Associated Serine Protease Inhibitor-1 (SFMI-1) and -2: Significant Inhibitors of Mannose binding Lectin Pathway which Helps in Multiple Sclerosis Treatment

One of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. The four pattern recognition molecules that have been identified till now are Mannose binding lectin (MBL), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. MBL ...

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p 144: sunflower mannose binding lectin-associated serine protease inhibitor-1 (sfmi-1) and -2: significant inhibitors of mannose binding lectin pathway which helps in multiple sclerosis treatment

one of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. the four pattern recognition molecules that have been identified till now are mannose binding lectin (mbl), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. mbl ...

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Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci.

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Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway.

The complement system plays an important role in innate immunity. In the lectin complement pathway, mannose-binding lectin (MBL) and ficolins act as recognition molecules, and MBL-associated serine protease (MASP) is a key enzyme. It has been suggested that MASP-2 is responsible for the activation of C4. Other serine proteases (MASP-1 and MASP-3) are also associated with MBL or ficolins; howeve...

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ژورنال

عنوان ژورنال: The Journal of Immunology

سال: 2000

ISSN: 0022-1767,1550-6606

DOI: 10.4049/jimmunol.164.5.2281