ABSTRACT
Edible bird's nest (EBN), an Asian health food, contains insoluble proteins and conjugated N-acetylneuraminic acid (NANA) that are difficult to be absorbed by humans. In order to increase the nutritional value of EBN, we developed methods to digest EBN targeting the release of proteins and NANA. By using simulated gastric fluid under acidic conditions, the complex proteins were fully digested into smaller peptides, and in parallel, NANA was fully released from the conjugated form. The completely digested EBN showed better nutraceutical properties. In a skin whitening test, the EBN digest showed stronger inhibition of melanogenesis of cultured B16 cells and enzymatic activity of tyrosinase, as compared to that of undigested EBN. In addition, the EBN digest exhibited stronger osteogenic activity in cultured osteoblasts. Thus, the complete digestion of EBN could be applied to the development of a new generation of EBN health food products, including EBN drinks and skincare products.
Subject(s)
N-Acetylneuraminic Acid/chemistry , Peptides/chemistry , Saliva/chemistry , Animals , Birds , Cell Line , Digestion , Humans , Melanins/metabolism , Mice , N-Acetylneuraminic Acid/pharmacology , Nutritive Value , Osteoblasts/cytology , Osteogenesis/drug effects , Peptides/pharmacology , Proteins/chemistry , Skin/drug effects , Skin/metabolism , Skin Lightening Preparations/chemistry , Skin Lightening Preparations/pharmacologyABSTRACT
Acetylcholinesterase (AChE; EC 3.1.1.7) is known to hydrolyze acetylcholine at cholinergic synapses. In mammalian erythrocyte, AChE exists as a dimer (G2 ) and is proposed to play role in erythropoiesis. To reveal the regulation of AChE during differentiation of erythroblast, erythroblast-like cells (TF-1) were induced to differentiate by application of erythropoietin (EPO). The expression of AChE was increased in parallel to the stages of differentiation. Application of EPO in cultured TF-1 cells induced transcriptional activity of ACHE gene, as well as its protein product. This EPO-induced event was in parallel with erythrocytic proteins, for example, α- and ß-globins. The EPO-induced AChE expression was mediated by phosphorylations of Akt and GATA-1; because the application of Akt kinase inhibitor blocked the gene activation. Erythroid transcription factor also known as GATA-1, a downstream transcription factor of EPO signaling, was proposed here to account for regulation of AChE in TF-1 cell. A binding sequence of GATA-1 was identified in ACHE gene promoter, which was further confirmed by chromatin immunoprecipitation (ChIP) assay. Over-expression of GATA-1 in TF-1 cultures induced AChE expression, as well as activity of ACHE promoter tagged with luciferase gene (pAChE-Luc). The deletion of GATA-1 sequence on the ACHE promoter, pAChEΔGATA-1 -Luc, reduced the promoter activity during erythroblastic differentiation. On the contrary, the knock-down of AChE in TF-1 cultures could lead to a reduction in EPO-induced expression of erythrocytic proteins. These findings indicated specific regulation of AChE during maturation of erythroblast, which provided an insight into elucidating possible mechanisms in regulating erythropoiesis.
