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Cathepsins D and L reduce the toxicity of advanced glycation end products

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dc.contributor.authorYILMAZ, BETÜL
dc.contributor.authorsGrimm, Stefanie; Horlacher, Melanie; Catalgol, Betul; Hoehn, Annika; Reinheckel, Thomas; Grune, Tilman
dc.date.accessioned2022-03-12T18:07:15Z
dc.date.available2022-03-12T18:07:15Z
dc.date.issued2012
dc.description.abstractAdvanced glycation end product-modified proteins are known for accumulating during aging and in several pathological conditions such as diabetes, renal failure, and neurodegenerative disorders. There is little information about the intracellular fate of endocytosed advanced glycation end products (AGES) and their influence on proteolytic systems. However, it is known that the lysosomal system is impaired during aging. Therefore, undegraded material may accumulate and play a considerable role in the development of diverse diseases. To investigate if AGEs can be degraded and to test whether they accumulate because of impaired lysosomal proteases we studied the effects of advanced glycation end products on the endosomal lysosomal system. Five different types of AGEs were generated by bovine serum albumin incubation with glyoxal, methylglyoxal, glucose, fructose, and ribose. The first experiments revealed the uptake of AGEs by the macrophage cell line RAW 264.7. Further investigations demonstrated an increase in cathepsin D and L activity and an increase in mature cathepsins D and L Increased activities were accompanied by the presence of more lysosomes, measured by staining with LysoTracker blue. To specify the roles of cathepsins D and L we used knockout cells to test the roles of both cathepsins on the toxicity of advanced glycation end products. In summary we conclude that both cathepsins are required for a reduction in advanced glycation end product-induced cytotoxicity. (C) 2012 Elsevier Inc. All rights reserved.
dc.identifier.doi10.1016/j.freeradbiomed.2011.12.021
dc.identifier.eissn1873-4596
dc.identifier.issn0891-5849
dc.identifier.pubmed22245096
dc.identifier.urihttps://hdl.handle.net/11424/230999
dc.identifier.wosWOS:000300964000005
dc.language.isoeng
dc.publisherELSEVIER SCIENCE INC
dc.relation.ispartofFREE RADICAL BIOLOGY AND MEDICINE
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectLysosomes
dc.subjectAdvanced glycation end products
dc.subjectCathepsin D
dc.subjectCathepsin L
dc.subjectPepstatin A
dc.subjectFree radicals
dc.subjectLYSOSOMAL STORAGE DISEASES
dc.subjectBOVINE SERUM-ALBUMIN
dc.subjectCYSTEINE PROTEASES
dc.subjectNEURODEGENERATIVE DISEASES
dc.subjectPARKINSONS-DISEASE
dc.subjectCANCER PROGRESSION
dc.subjectALZHEIMERS-DISEASE
dc.subjectL DEFICIENCY
dc.subjectAMINO-ACID
dc.subjectRAT-BRAIN
dc.titleCathepsins D and L reduce the toxicity of advanced glycation end products
dc.typearticle
dspace.entity.typePublication
local.avesis.id937d4ace-990e-4fb3-8eb7-bc153574dd11
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.journal.numberofpages13
oaire.citation.endPage1023
oaire.citation.issue6
oaire.citation.startPage1011
oaire.citation.titleFREE RADICAL BIOLOGY AND MEDICINE
oaire.citation.volume52
relation.isAuthorOfPublication81633a07-e5fb-4760-b3ef-bf0878d87827
relation.isAuthorOfPublication.latestForDiscovery81633a07-e5fb-4760-b3ef-bf0878d87827

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