Evaluation of in vitro function by subcellular distribution of lysosomal and peroxisomal protein in Saccharomyces cerevisiae

Lysosomes and peroxisomes, contained in all eukaryote cells, are similar but have completely different function. Lysosomes have three dozen different kinds of hydrolytic enzymes and release lysosomal enzymes to digest intra/extracellular materials. The lysosomal enzymes degrade bacteria cell walls and proteins in cell, exhibiting an antimicrobial and anticancerous effect. Peroxisomes contain oxidative enzymes such as peroxidase, D-amino acid oxidase, and catalase allowing the ability to degrade melanin in hyperpigmentation disorders. Exposure of Saccharomyces cerevisiae and HeLa cells to chemical stress alters lysosomal and peroxisomal enzymes. Chemical stresses such as phenylhydrazine, sodium azide, rolipram, NH₄Cl, salicylic acid, H₂O₂ and 6-hydroxdopamine (6-OHDA) have been suggested to stimulate in vitro function of lysosome and peroxisome-like organelles (LPO) isolated from S. cerevisiae, and we demonstrate activity of LPO in HeLa cells through chemical analysis. The lysosomes of cells exposed to salicylic acid, 6-OHDA and H₂O₂ had increased antimicrobial and anticancerous activity, and the peroxisomes of cells exposed to phenylhydrazine and sodium azide had reduced effect of melanin degradation. Therefore, our results suggest that activity of lysosomes and peroxisomes can be regulated by several stimuli, therefore lysosomes may be used as antimicrobial agents, apoptosis-inducing materials, or peroxisomal enzymes to be useful agents for cosmeceutical skin lightening and treatment of hyperpigmentation disorders.