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Serum lectin with known structure activates complement through the classical pathway
The Journal of Biological Chemistry
|June 5, 1987
Summary
Serum mannan-binding protein (MBP) activates the complement system via sugar binding, initiating the classical pathway. Rat liver MBP, however, does not activate complement, suggesting structural differences influence function in immune response.
Area of Science:
- Immunology
- Biochemistry
Background:
- Mannan-binding protein (MBP) is a lectin that binds mannose and N-acetylglucosamine.
- MBP plays a role in the innate immune system by activating complement.
- Differences in MBP function between serum and liver forms require investigation.
Purpose of the Study:
- To investigate the complement-activating properties of rat serum MBP.
- To compare the functional activity of serum MBP with rat liver MBP.
- To elucidate the mechanism of complement activation by serum MBP.
Main Methods:
- Passive hemolysis assay using mannan-coated sheep erythrocytes.
- Inhibition studies with haptenic sugars.
- Analysis of the N-terminal amino acid sequence of rat serum MBP.
Main Results:
- Rat serum MBP activated the complement system, while rat liver MBP did not.
- Complement activation by serum MBP was sugar-dependent and required C4, indicating classical pathway involvement.
- The N-terminal sequence of rat serum MBP matched MBP-A, confirming their identity.
Conclusions:
- Serum MBP initiates complement activation through its sugar-binding domain via the classical pathway.
- Structural similarities between serum MBP and C1q may inform the mechanism of complement activation.
- Distinct functional properties of serum and liver MBP highlight tissue-specific roles in immunity.