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Purification of macrophage deactivating factor.

S Srimal¹, C Nathan

¹Beatrice and Samuel A. Seaver Laboratory, Department of Medicine, Cornell University Medical College, New York, New York 10021.

The Journal of Experimental Medicine

|April 1, 1990

Summary

Macrophage deactivation factor (MDF) was purified from tumor cells and found to be a protein that suppresses macrophage activity. This factor tightly associates with albumin and may have a blocked N-terminus.

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Area of Science:

Immunology
Cell Biology
Biochemistry

Background:

Activated macrophages release hydrogen peroxide, a key component of immune response.
Tumor cells can modulate immune cell function, including macrophage activity.

Purpose of the Study:

To purify and characterize the Macrophage Deactivation Factor (MDF) from P815 tumor cell-conditioned medium.
To investigate the properties and molecular weight of MDF.
To assess the inhibitory capacity of purified MDF on activated macrophages.

Main Methods:

Assay of MDF by suppression of hydrogen peroxide release from activated mouse peritoneal macrophages.
Multi-step purification involving acid-ethanol extraction, ether precipitation, gel filtration, anion-exchange, and reversed-phase HPLC.
SDS-PAGE, radioiodination, and NH2-terminal amino acid sequencing for protein characterization.

Main Results:

MDF was purified 6,140-fold, exhibiting properties of a soluble protein(s) in low and high molecular weight fractions.
The final preparation contained a ~13,000 Mr species tightly associated with a 66,000 Mr albumin species.
Purified MDF inhibited macrophage hydrogen peroxide release by 50% at 1-10 nM, but was less potent than TGF-beta and not neutralized by TGF-beta antibodies.

Conclusions:

MDF is a ~13,000 Mr protein that associates with albumin and deactivates macrophages.
The N-terminus of the ~13,000 Mr MDF species may be blocked.
MDF represents a distinct mechanism of macrophage deactivation compared to TGF-beta.

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