Digested wheat gluten inhibits binding between leptin and
its receptor
Tommy Jönsson1*, Ashfaque A Memon1, Kristina Sundquist1, Jan Sundquist1, Stefan Olsson2, Amarnadh Nalla34, Mikael Bauer5 and Sara Linse5
- *Corresponding
author: Tommy Jönsson Tommy.Jonsson@med.lu.se
BMC Biochemistry 2015, 16:3 doi:10.1186/s12858-015-0032-y
Published: 20 January 2015
BackgroundLeptin resistance is considered a primary risk
factor for obesity. It has been hypothesized that dietary cereal grain protein
could cause leptin resistance by preventing leptin from binding to its receptor.
Non-degraded dietary wheat protein has been found in human serum at a mean
level of 41?ng/mL. Here, we report our findings from testing whether
enzymatically digested gluten from wheat prevents leptin from binding to the
leptin receptor in vitro.Gluten from wheat was digested with pepsin and trypsin
under physiological conditions. Pepsin and trypsin activity was removed from
the gluten digest with a 10?kDa spin-filter or by heat treatment at 100?C for
30?min. Binding to the leptin receptor of leptin mixed with gluten digest at a
series of concentrations was measured using surface plasmon resonance
technology.ResultsBinding of the gluten digest to the leptin receptor was not
detected. Spin-filtered gluten digest inhibited binding of leptin to the leptin
receptor, with 50% inhibition at a gluten digest concentration of ~10?ng/mL.
Heat-treated gluten digest did not inhibit leptin binding.ConclusionsDigested
wheat gluten inhibits binding of leptin to the leptin receptor, with
half-maximal inhibition at 10?ng/mL. The inhibition is significant at
clinically relevant concentrations and could therefore serve as a novel pathway
to investigate to understand the molecular basis of leptin resistance, obesity
and associated disorders.
The complete article is available as a provisional
PDF. The fully formatted PDF and HTML versions are in production. Tomado de
envio de bcm
|
No hay comentarios:
Publicar un comentario