Camel and bovine milk lactoferrins activate insulin receptor and its related AKT and ERK1/2 pathways
Mir Azam Khan, Irfa Anwar, Elrashdy M. Redwan, Abdulrasheed Palakkott, Arshida Ashraf, Jaleel Kizhakkayil +3 more
Journal of Dairy Science
Abstract
Lactoferrin (LF) is a milk protein that may be an interesting candidate for the antidiabetic properties of milk due to its well-documented bioactivity and implication in diabetes. Here, we investigated the functional action of LF purified from camel and bovine milk (cLF, bLF) on insulin receptors (IR) and their pharmacology and signaling in hepatocarcinoma (HepG2) and human embryonic kidney (HEK293) cells. For this, we examined IR activation by bioluminescence resonance energy transfer (BRET) technology and the phosphorylation of its key downstream signaling kinases by western blot. The purified cLF and bLF induced phosphorylation of IR, AKT, and ERK1/2 in HepG2 and HEK293 cells. The BRET assays in HEK293 cells confirm the pharmacological action of cLF and bLF on IR, with a possible allosteric mode of action. This reveals for the first time the bioactivity of LF toward IR function, indicating it as a potential bioactive protein behind the antidiabetic properties of camel milk.
Extracted Claims
3 claims extracted from this paper into the knowledge graph
lactoferrin (LF) from bovine milk (bLF) induced phosphorylation of insulin receptors (IR), AKT, and ERK1/2
“The purified cLF and bLF induced phosphorylation of IR, AKT, and ERK1/2 in HepG2 and HEK293 cells”
cLF and bLF confirmed pharmacological action on insulin receptors (IR)
“The BRET assays in HEK293 cells confirm the pharmacological action of cLF and bLF on IR, with a possible allosteric mode of action”
lactoferrin (LF) from camel milk (cLF) induced phosphorylation of insulin receptors (IR), AKT, and ERK1/2
“The purified cLF and bLF induced phosphorylation of IR, AKT, and ERK1/2 in HepG2 and HEK293 cells”