2018•Experimental DermatologyRequires access

Gelatin as a convenient surrogate protein to model the in vitro effects of advanced glycation end‐product formation

Nadine A. Pringle, Maryna van de Venter, Trevor Koekemoer

Open publisher page 7 citations

Abstract

Protein glycation has been implicated in skin ageing and several other disease states; however, the slow rate of glycation end-product formation makes in vitro studies challenging and often impractical. Gelatin, a denatured form of collagen, was identified as a convenient glycation surrogate amenable to cell culture conditions. The suitability of glycated gelatin to model the effects of AGE formation was verified using RAW 264.7 macrophages which revealed a remarkable correlation to previously documented effects. Effects of glycated gelatin on the central role of NF-ĸB and its downstream consequences (COX-2 and CD86) confirmed the pro-inflammatory nature of advanced glycation end-products. Together, these findings provide confidence that this model could prove a valuable tool to study the poorly understood mechanisms characterizing cellular dysfunction in response to AGE accumulation.

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What this paper is about

Protein glycation has been implicated in skin ageing and several other disease states; however, the slow rate of glycation end-product formation makes in vitro studies challenging and often impractical. Gelatin, a denatured form of collagen, was identified as a convenient glycation surrogate amenable to cell culture conditions. The suitability of glycated gelatin to model the effects of AGE formation was verified using RAW 264.7 macrophages which revealed a remarkable correlation to previously documented effects. Effects of glycated gelatin on the central role of NF-ĸB and its downstream consequences (COX-2 and CD86) confirmed the pro-inflammatory nature of advanced glycation end-products. Together, these findings provide confidence that this model could prove a valuable tool to study the poorly understood mechanisms characterizing cellular dysfunction in response to AGE accumulation.

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Available abstract

Protein glycation has been implicated in skin ageing and several other disease states; however, the slow rate of glycation end-product formation makes in vitro studies challenging and often impractical. Gelatin, a denatured form of collagen, was identified as a convenient glycation surrogate amenable to cell culture conditions. The suitability of glycated gelatin to model the effects of AGE formation was verified using RAW 264.7 macrophages which revealed a remarkable correlation to previously documented effects. Effects of glycated gelatin on the central role of NF-ĸB and its downstream consequences (COX-2 and CD86) confirmed the pro-inflammatory nature of advanced glycation end-products. Together, these findings provide confidence that this model could prove a valuable tool to study the poorly understood mechanisms characterizing cellular dysfunction in response to AGE accumulation.

Key concepts: Advanced glycation end-product, Glycation, Gelatin, In vitro, Chemistry, Biochemistry, Receptor

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