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Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
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Factor D.

Hideharu Sekine1, Takeshi Machida1, Teizo Fujita2

  • 1Department of Immunology, Fukushima Medical University School of Medicine, Fukushima, Japan.

Immunological Reviews
|November 1, 2022
PubMed
Summary
This summary is machine-generated.

Complement factor D (FD) activation, crucial for the alternative pathway (AP), requires MASP-3. This discovery clarifies how FD is physiologically activated, impacting complement system research.

Keywords:
MASP-1MASP-3alternative pathwayfactor Dlectin pathway

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Area of Science:

  • Immunology
  • Biochemistry
  • Complement System Biology

Background:

  • Complement factor D (FD) is a serine protease essential for alternative pathway (AP) activation.
  • FD, primarily from adipose tissue, circulates in an activated form, unlike most liver-synthesized complement proteases.
  • The mechanism of FD activation remained largely unknown until recent discoveries.

Purpose of the Study:

  • To elucidate the mechanism of complement factor D (FD) activation.
  • To investigate the role of MASP-1 and MASP-3 in FD activation.
  • To clarify the physiological activation of the AP via FD.

Main Methods:

  • Utilized MASP-1/3-deficient mice and MASP-1 or MASP-3 monospecific knockout mice.
  • Analyzed sera from these knockout mice for lectin pathway (LP) and AP activity.
  • Examined sera from 3MC syndrome patients with MASP1 gene mutations.

Main Results:

  • MASP-1/3-deficient mice sera showed minimal LP and AP activity with pro-FD.
  • MASP-1-deficient mice sera lacked LP activity.
  • MASP-3-deficient mice sera lacked AP activity with pro-FD, indicating MASP-3's crucial role.

Conclusions:

  • MASP-1 and/or MASP-3 are involved in the activation of FD.
  • MASP-3 plays a pivotal role in the physiological activation of the AP through FD activation.
  • This research clarifies a key step in complement system regulation.