Expression of 67,000 MW calcimedin and its binding protein in resident and thioglycolate-elicited macrophages.
Calcimedins are newly recognized calcium-dependent hydrophobic-binding proteins. The 67,000 MW calcimedin exhibits calcium-dependent specific binding to a 60,000 MW intracellular acceptor protein (60,000 MW). Macrophages possessed 30,000 MW and 67,000 MW calcimedins and 60,000 MW acceptor protein, identified by immunofluorescence and confirmed by SDS-PAGE and Western immunoblots. Compared with low levels in resident macrophages, thioglycolate-elicited inflammatory macrophages showed large increases in the levels of 67,000 MW calcimedin and 60,000 MW acceptor protein, especially at cell-limiting membranes. Levels of calmodulin and 30,000 MW calcimedin appeared similar in both populations. Trypsinization removed most 67,000 MW calcimedin and some 60,000 MW acceptor-protein staining. The calcimedins appear to represent novel macrophage-differentiation antigens. Their modulation suggests that they may play a role in the inflammatory response.
Morse
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Rockefeller University, Laboratory Animal Research Center, New York, New York 10021.
Moore
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PB
D000818:Animals; D017302:Annexins; D001202:Ascitic Fluid / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000032:analysis*; D002352:Carrier Proteins / Q000032:analysis; D005455:Fluorescent Antibody Technique; D008264:Macrophages / Q000032:analysis*; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D010533:Peritoneal Lavage; D013864:Thioglycolates; D014357:Trypsin / Q000494:pharmacology
D017302:Annexins; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D013864:Thioglycolates; D014357:Trypsin