1. Transcriptional regulation of chicken leukocyte cell-derived chemotaxin 2 in response to toll-like receptor 3 stimulation
- Author
-
Sung-Jo Kim, Chong-Sam Na, Ra Ham Lee, Hak-Kyo Lee, Seokhyun Lee, and Ki-Duk Song
- Subjects
Toll-like receptor ,Chemistry ,lcsh:Animal biochemistry ,0402 animal and dairy science ,Leukocyte Cell-derived Chemotaxin 2 (LECT2) ,Gene Expression ,04 agricultural and veterinary sciences ,Chicken ,040201 dairy & animal science ,Article ,Animal Biotechnology ,Cell biology ,TLR3 ,Gene expression ,Transcriptional regulation ,Innate Immune Receptor Signaling ,Animal Science and Zoology ,lcsh:Animal culture ,Receptor ,lcsh:QP501-801 ,Peptide sequence ,Transcription factor ,Gene ,lcsh:SF1-1100 ,Food Science - Abstract
Objective Leukocyte cell-derived chemotaxin 2 (LECT2) is associated with several physiological processes including inflammation, tumorigenesis, and natural killer T cell generation. Chicken LECT2 (chLECT2) gene was originally identified as one of the differentially expressed genes in chicken kidney tissue, where the chickens were fed with different calcium doses. In this study, the molecular characteristics and gene expression of chLECT2 were analyzed under the stimulation of toll-like receptor 3 (TLR3) ligand to understand the involvement of chLECT2 expression in chicken metabolic disorders. Methods Amino acid sequence of LECT2 proteins from various species including fowl, fish, and mammal were retrieved from the Ensembl database and subjected to Insilco analyses. In addition, the time- and dose-dependent expression of chLECT2 was examined in DF-1 cells which were stimulated with polyinosinic:polycytidylic acid (poly [I:C]), a TLR3 ligand. Further, to explore the transcription factors required for the transcription of chLECT2, DF-1 cells were treated with poly (I:C) in the presence or absence of the nuclear factor κB (NFκB) and activated protein 1 (AP-1) inhibitors. Results The amino acid sequence prediction of chLECT2 protein revealed that along with duck LECT2 (duLECT2), it has unique signal peptide different from other vertebrate orthologs, and only chLECT2 and duLECT2 have an additional 157 and 161 amino acids on their carboxyl terminus, respectively. Phylogenetic analysis suggested that chLECT2 is evolved from a common ancestor along with the actinopterygii hence, more closely related than to the mammals. Our quantitative polymerase chain reaction results showed that, the expression of chLECT2 was up-regulated significantly in DF-1 cells under the stimulation of poly (I:C) (p
- Published
- 2019
- Full Text
- View/download PDF