An interaction between leukocyte cell-derived chemotaxin 2 and transferrin of ayu, Plecoglossus altivelis

Increased serum leukocyte cell-derived chemotaxin 2 (LECT2) levels in obesity and fatty liver

“…These studies suggested that electrostatic interactions with other serum proteins may interfere with the LECT2 assay. One such candidate protein is transferrin, whose interaction with LECT2 has been reported in fish and mice (22). Another candidate protein is LECT2 itself, which can oligomerize in vitro under certain conditions as previously reported (23).…”

An interaction between a C-type lectin receptor and leukocyte cell-derived chemotaxin 2 of ayu, Plecoglossus altivelis

“…All fish used in this study were apparently healthy without any pathological signs. The construction of the bait plasmid pGBKT7-aLECT2 and ayu liver cDNA library for Y2H was done as previously described [9].…”

“…All fish used in this study were apparently healthy without any pathological signs. The construction of the bait plasmid pGBKT7-aLECT2 and ayu liver cDNA library for Y2H was done as previously described [9].Using expressed aLECT2 as bait in Y2H screens, 9 independent interacting clones were identified after two separate screenings of an ayu cDNA expression library (2.5 Â 10 6 independent clones). Each clone could induce the two reporter genes, allowing growth on quadruple dropout plates and expression of a-galactosidase activity.…”

“…Each clone could induce the two reporter genes, allowing growth on quadruple dropout plates and expression of a-galactosidase activity. Sequencing showed that 2 of 9 were partial sequences from a C-type lectin receptor gene, while the other 7 clones were partial sequences from a transferrin (Tf) gene [9]. Subsequently, the complete cDNA sequence of ayu C-type lectin receptor gene (EMBL accession number: FN396582) was determined.…”

The establishment of a library screening method based on yeast two-hybrid system and its use to determine the potential interactions of liver proteins in ayu, Plecoglossus altivelis

“…The spectrin cleavage is inhibited by the Ca 2þ -dependent binding of CaM to Spna2, which therefore represents potential regulator of the stability and the plasticity of the spectrin-based skeleton [14]. That LECT2 interacts with Tf, previously identified in ayu, large yellow croaker (Pseudosciaena crocea) and mouse (Mus musculus), suggests that the different mechanisms of serum LECT2 changes would result in cellular immune responses [15].…”