Camel and bovine milk lactoferrins activate insulin receptor and its related AKT and ERK1/2 pathways.

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.

Synergistic activation of thrombin and angiotensin II receptors revealed by bioluminescence resonance energy transfer.

We recently reported a physical interaction between the angiotensin II (AngII) receptor (AT1R) and thrombin receptor (PAR1) in HEK293 cells using bioluminescence resonance energy transfer (BRET) technology. This was characterized by thrombin trans-activating AT1R and the synergistic responses of the AT1R-PAR1 complex. Here, we investigated the other face of the coin by examining the effect of AT1R on PAR1 activity using BRET.

Molecular basis of the anti-diabetic properties of camel milk through profiling of its bioactive peptides on dipeptidyl peptidase IV (DPP-IV) and insulin receptor activity.

The molecular basis of the anti-diabetic properties of camel milk reported in many studies and the exact active agent are still elusive. Recent studies have reported effects of camel whey proteins (CWP) and their hydrolysates (CWPH) on the activities of dipeptidyl peptidase IV (DPP-IV) and the human insulin receptor (hIR). In this study, CWPH were generated, screened for DPP-IV binding in silico and inhibitory activity in vitro, and processed for peptide identification.

Interplay Between Angiotensin II Type 1 Receptor and Thrombin Receptor Revealed by Bioluminescence Resonance Energy Transfer Assay.

The key hormone of the renin-angiotensin system (RAS), angiotensin II (AngII), and thrombin are known to play major roles in the vascular system and its related disorders. Previous studies reported connections between AngII and thrombin in both physiological and pathophysiological models. However, the molecular mechanisms controlling such interplay at the level of their receptors belonging to the family of G protein-coupled receptors (GPCRs) are not fully understood.

Anti-Insulin Receptor Antibodies in the Pathology and Therapy of Diabetes Mellitus.

Diabetes mellitus (DM) is recognized as the most common and the world's fastest-growing chronic disease with severe complications leading to increased mortality. Many strategies exist for the management of DM and its control, including treatment with insulin and insulin analogs, oral hypoglycemic therapy such as insulin secretion stimulators and insulin sensitizers, and diet and physical training. Over the years, many types of drugs and molecules with an interesting pharmacological diversity have been developed and proposed for their anti-diabetic potential.

Positive Modulation of Angiotensin II Type 1 Receptor-Mediated Signaling by LVV-Hemorphin-7.

Hemorphins are hemoglobin β-chain-derived peptides initially known for their analgesic effects binding to the opioid receptors belonging to the family of G protein-coupled receptor (GPCR), as well as their physiological action on blood pressure. However, their molecular mechanisms in the regulation of blood pressure are not fully understood. Studies have reported an antihypertensive action the inhibition of the angiotensin-converting enzyme, a key enzyme in the renin-angiotensin system.