Mobility of surface proteins on normal rat macrophages and on a "macrophagelike" rat tumor.
Peritoneal macrophages endocytosed their histocompatibility antigens (RT1), Fc receptors (FcR), and concanavalin A (Con A) receptors after cross-linking by ligands, but did not cap these membrane proteins. The 323N cell, a "macrophage like" tumor cell, under identical conditions capped its surface proteins. Experiments measuring fluorescence recovery after photobleaching showed that the mobile fraction of RT1 was significantly greater in 323N cells than in normal peritoneal macrophages. Presumably, the membrane proteins of 323N are not as tethered to the cytoskeleton, or, if so, are in a nexus that is not the same as that which occurs between membrane proteins of normal macrophages and the cytoskeleton. The mobility of RT1 on normal lymphocytes was also different from that of macrophages. These observations suggest that the movement of membrane molecules is determined by cell type and is regulated by the cytoskeleton which varies in structure and function from cell type to cell type.
D000818:Animals; D002471:Cell Transformation, Neoplastic; D003078:Colchicine / Q000494:pharmacology; D006649:Histocompatibility Antigens; D008214:Lymphocytes / Q000378:metabolism; D008264:Macrophages / Q000378:metabolism*; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D051381:Rats; D011917:Rats, Inbred Lew; D011952:Receptors, Concanavalin A / Q000378:metabolism; D011961:Receptors, Fc / Q000378:metabolism; D013160:Splenic Neoplasms / Q000473:pathology*
D006649:Histocompatibility Antigens; D008565:Membrane Proteins; D011952:Receptors, Concanavalin A; D011961:Receptors, Fc; D003078:Colchicine