Effect of aging on macrophage adherence to extracellular matrix proteins.
Fibronectin, type I, type IV and type V collagens were compared for their abilities to promote mouse peritoneal resident macrophage adherence and the effect of aging on macrophage adhesion to these matrix proteins was examined. Adherence of macrophages to fibronectin was remarkable and more than 5-fold compared to type I, type IV or type V collagens. Adherence of macrophages to fibronectin and type I collagen increased during aging. However, no age-related changes were observed in macrophage adherence to type IV and type V collagens. The percent of inhibition of macrophage adherence to fibronectin by arginine-glycine-aspartic acid-serine (RGDS) peptide (58.1 +/- 2.7%) was significantly (P < 0.01) higher than that in cells from young mice (23.1 +/- 5.7%). These data suggest that macrophage attach preferentially to fibronectin and that the ability of macrophage to attach to fibronectin increases during aging. The age-related increase in macrophage attachment to fibronectin is related to the concentration of cell surface receptors of macrophage which recognize RGDS sequence within fibronectin during aging. Adherence of macrophage to fibronectin implies retention of macrophages in subendothelial space. Age-related increase in macrophage ability to attach to fibronectin may be related to atherogenesis during aging.
Iiyama
M
M
Department of Geriatric Medicine, Kyoto University, Japan.
Shimada
Y
Y
Kita
T
T
Ito
H
H
D000375:Aging / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D001161:Arteriosclerosis / Q000209:etiology; D001665:Binding Sites; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D003094:Collagen / Q000145:classification / Q000502:physiology; D016326:Extracellular Matrix Proteins / Q000502:physiology*; D005353:Fibronectins / Q000737:chemistry / Q000502:physiology; D066298:In Vitro Techniques; D007700:Kinetics; D017737:Macrophages, Peritoneal / Q000187:drug effects / Q000502:physiology*; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology
D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D009842:Oligopeptides; D003094:Collagen; C046617:arginyl-glycyl-aspartyl-serine