We used chromatographic separation to purify to homogeneity a monomeri
c monocyte chemotactic protein of 150 kDa contained in mesothelioma pl
eural effusions. It was identified by N-terminal amino acid sequencing
and immunoblotting as complement factor H, an inhibitor of the altern
ative complement pathway. Specific antibodies against factor H inhibit
ed the monocyte chemotactic activity of the purified protein, which wa
s most active at 10 nM. Factor H is a restrictive factor of alternativ
e complement pathway activation. The new chemotactic function assigned
to factor H in recruiting monocytes to the mesothelioma site might co
ntribute to malignant cell phagocytosis via the iC3b/complement recept
or type 3 pathway. These functions link the humoral and cellular immun
e systems.