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Mannose-binding Lectin (MBL)-associated Serine Protease (MASP)-1 Contributes to Activation of the Lectin Complement Pathway

Mannose-binding Lectin (MBL)-associated Serine Protease (MASP)-1 Contributes to Activation of the Lectin Complement Pathway

Minoru Takahashi, Daisuke Iwaki, Kazuko Kanno, Yumi Ishida, Jie Xiong, Misao Matsushita, Yuichi Endo, Shigeto Miura, Naoto Ishii, Kazuo Sugamura, Teizo Fujita

J Immunol. 2008 May 1;180(9):6132-8.

PMID: 18424734

Abstract:

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; however, their functions are still controversial. In this study, a MASP-1- and MASP-3-deficient mouse model (MASP1/3(-/-)) was generated by a gene targeting strategy to investigate the roles of MASP-1 and MASP-3 in the lectin pathway. Serum derived from MASP1/3(-/-) mice showed significantly lower activity of both C4 and C3 deposition on mannan-agarose, and this low activity was restored by the addition of recombinant MASP-1. MASP-1/3-deficient serum showed a significant delay for activation of MASP-2 compared with normal serum. Reconstitution of recombinant MASP-1 in MASP-1/3-deficient serum was able to promote the activation of MASP-2. From these results, we propose that MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42410968	Mannan−Agarose			Price

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