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#12
New
Protein Identified in Liver Might Lead to Type 2 Diabetes Cure?
Researchers
at the Medical College of Ohio have identified a protein in the
liver that helps clear insulin from blood.
This
discovery could eventually lead to a cure for type 2 diabetes. It
has been a common belief among scientists that type 2 diabetes is
initiated when the body's muscles, fat tissues, and liver stop
responding to insulin. Insulin brings sugar from blood into muscle
and fat tissues to be stored as fuel and stops the liver from
making its own sugar. Lack of response to insulin in type 2
diabetes leads to increased sugar levels in blood.
Sonia
M. Najjar Ph.D., associate professor of pharmacology and
therapeutics, contends that type 2 diabetes may actually begin a
step before the body starts resisting insulin. Using genetically
modified mice, Najjar
has found when there is increased fat in the body, the liver's
ability to clear insulin is impaired. This, in turn, can lead to
insulin resistance in the liver and other tissues, thus resulting
in type 2 diabetes.
This
discovery coupled with the identification of CEACAM1, a liver
protein that controls insulin clearance, may play a major role in
the battle against type 2 diabetes.
"I
can easily envision a drug that enhances the function of this
protein and leads to a cure for type 2 diabetes," said
Najjar.
A
paper from Najjar's laboratory about the function of the CEACAM1
protein in insulin clearance will be published in the prestigious
journal, Nature Genetics in March 2002 and can be read online now
on its Website. Najjar's
research is currently sponsored by the National Institute of
Diabetes, Digestive and Kidney Diseases and the American Diabetes
Association. The Medical College of Ohio Foundation sponsored the
initial phase of her studies
We
hypothesized that insulin stimulates phosphorylation of CEACAM1
which in turn leads to upregulation of receptor-mediated insulin
endocytosis and degradation in the hepatocyte. We have generated
transgenic mice over-expressing in liver a dominant-negative,
phosphorylation-defective S503A-CEACAM1 mutant. Supporting our
hypothesis, we found that S503A-CEACAM1 transgenic mice developed
hyperinsulinemia resulting from impaired insulin clearance. The
hyperinsulinemia caused secondary insulin resistance with impaired
glucose tolerance and random, but not fasting, hyperglycemia.
Transgenic mice developed visceral adiposity with increased
amounts of plasma free fatty acids and plasma and hepatic
triglycerides. These findings suggest a mechanism through which
insulin signaling regulates insulin sensitivity by modulating
hepatic insulin clearance.
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