Apoptotic killing of fibroblasts by matrix-bound advanced glycation endproducts.
The extracellular matrix accumulates biologically active advanced glycation endproducts such as carboxymethyl-lysine (CML). Alikhani et al. recently reported that CML-rich collagen, representing an artifically aged matrix protein, induces apoptosis in vivo and in fibroblasts. This observation may have profound implications for the biology of cell-matrix interactions during aging.
Obrenovich
Mark E
ME
Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.
Monnier
Vincent M
VM
D000375:Aging / Q000473:pathology; D000818:Animals; D017209:Apoptosis; D002453:Cell Cycle / Q000502:physiology; D005109:Extracellular Matrix / Q000502:physiology*; D005347:Fibroblasts / Q000166:cytology*; D017127:Glycation End Products, Advanced / Q000502:physiology*; D008239:Lysine / Q000031:analogs & derivatives* / Q000502:physiology; D015416:Maillard Reaction; D008954:Models, Biological; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000502:physiology; D015398:Signal Transduction
D017127:Glycation End Products, Advanced; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; C048496:N(6)-carboxymethyllysine; D008239:Lysine