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Related Experiment Video

Updated: May 14, 2026

Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity

Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity

Published on: January 7, 2019

The role of MASP-1/3 in complement activation.

Hideharu Sekine¹, Minoru Takahashi, Daisuke Iwaki

¹Department of Immunology, Fukushima Medical University School of Medicine, 1-Hikariga-oka, Fukushima 960-1295, Japan.

Advances in Experimental Medicine and Biology

|February 14, 2013

Summary

Mannose-binding lectin-associated serine proteases (MASPs) MASP-1 and MASP-3 are crucial for activating the complement system's alternative pathway. These proteases also appear to play a role in the lectin pathway's activation.

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Published on: August 10, 2021

Area of Science:

Immunology
Complement System Biology

Background:

The complement system comprises over 30 proteins, activating via classical, lectin, or alternative pathways for pathogen destruction.
Mannose-binding lectin (MBL) and ficolins initiate the lectin pathway, activating MBL-associated serine proteases (MASPs).
MASP-2 is essential for C3 convertase assembly, but the roles of MASP-1 and MASP-3 are largely unknown.

Purpose of the Study:

To elucidate the physiological functions of MASP-1 and MASP-3 within the complement system.
To investigate the involvement of MASP-1 and MASP-3 in the lectin and alternative pathways.

Main Methods:

Generation of a MASP-1 and MASP-3 deficient (M1/3 KO) mouse model.
In vitro enzymatic assays to assess the activity of MASP-1 and MASP-3 on Factor D and other MASPs.

Main Results:

M1/3 KO mice exhibited a complete lack of alternative pathway activation due to inactive Factor D.
MASP-1 and MASP-3 demonstrated the ability to activate Factor D proenzyme in vitro.
MASP-1 was shown to activate MASP-2 and MASP-3, analogous to C1r's activation of C1s.

Conclusions:

MASP-1 and MASP-3 are essential for the activation of the alternative complement pathway.
These proteases are implicated in the activation mechanisms of both the lectin and alternative pathways.