Mannose-binding lectin and associate serine protease complex modulates neutrophil respiratory burst and gene expression in Capra hircus

Patel, Pankaj Kumar; Choudhary, Komal; Patidar, Preeti; Sharma, S. N.; Hajela, Krishnan

doi:10.1016/j.imbio.2020.151972

Cited by 3 publications

(1 citation statement)

References 30 publications

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“…In HUVECs, MASP-1 induces the secretion of IL-8, predominantly through the p38-MAPK pathway, and increases E-selectin expression, facilitating neutrophil chemotaxis and enhanced adhesion to the endothelium [118,119]. Moreover, MASP-1 has been found to directly stimulate neutrophils through neutrophil surface receptors, leading to an increased oxidative burst and enhanced phagocytosis in goat [120]. The cleavage of zymogen MASP-1 into the active form is a prerequisite for its direct cell-activating effect [121].…”

Section: Cellular Effects Of Maspsmentioning

confidence: 99%

The Lectin Pathway of the Complement System—Activation, Regulation, Disease Connections and Interplay with Other (Proteolytic) Systems

Dobó,

Kocsis,

Farkas

et al. 2024

IJMS

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The complement system is the other major proteolytic cascade in the blood of vertebrates besides the coagulation–fibrinolytic system. Among the three main activation routes of complement, the lectin pathway (LP) has been discovered the latest, and it is still the subject of intense research. Mannose-binding lectin (MBL), other collectins, and ficolins are collectively termed as the pattern recognition molecules (PRMs) of the LP, and they are responsible for targeting LP activation to molecular patterns, e.g., on bacteria. MBL-associated serine proteases (MASPs) are the effectors, while MBL-associated proteins (MAps) have regulatory functions. Two serine protease components, MASP-1 and MASP-2, trigger the LP activation, while the third component, MASP-3, is involved in the function of the alternative pathway (AP) of complement. Besides their functions within the complement system, certain LP components have secondary (“moonlighting”) functions, e.g., in embryonic development. They also contribute to blood coagulation, and some might have tumor suppressing roles. Uncontrolled complement activation can contribute to the progression of many diseases (e.g., stroke, kidney diseases, thrombotic complications, and COVID-19). In most cases, the lectin pathway has also been implicated. In this review, we summarize the history of the lectin pathway, introduce their components, describe its activation and regulation, its roles within the complement cascade, its connections to blood coagulation, and its direct cellular effects. Special emphasis is placed on disease connections and the non-canonical functions of LP components.

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