Abstract: As the most common primary glomerular disease worldwide, IgA Nephropathy （IgAN） is a common cause of end-stage renal disease. So far, renal biopsy remains a gold standard for diagnosing and evaluating disease activity. Previous studies have demonstrated that a deposition of Galactose-deficient IgA1 （GD-IGA1） plays an important role in the pathogenesis of IgAN. The deposition of GD-IGA1 may activate the complement system, including alternative pathway （AP）, lectin pathway （LP） and classical pathway （CP）. Mannose binding lectin （MBL） is a key factor for activating lectin pathway. Activated mannose binding ectin-associated serine proteases （MASPs） are key enzymes in lectin pathway. There are three different subtypes of MASPs （MASP1, MASP2 、 MASP3）. As a new MASP protease, MASP3 has become a recent research hotspot. Many studies at home and abroad have shown that MASP3 could activate factor D, participate in alternative pathways and cause damage to glomerular mesangial cells. Therefore, there may be some relationship between a deposition of GD-IGA1 and an appearance of MASP3 in IgAN, which needs further experimental study. This review systematically examined the role of GD-IGA1 and MASP3 in the pathogenesis of IgAN and explored the correlation between GD-IGA1 and MASP3.