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What is really ‘killing” beta cells in type 2 diabetes ?
Everyone knows, the beta cells in the Islet’s of Langerhans, produce insulin.
But this is not all they produce…..
They also produce, a protein called amylin, also known as human islet amyloid polypeptide (hiAPP).
The antics of amylin
Now relatively speaking, the amount of amylin produced, is small – under “normal” circumstances, there are 20 molecules of insulin produced, for every molecule of amylin.
But this is enough to get the job done.
Amylin’s chief job, is to STOP HUNGER. And this helps insulin do HIS job i.e. move the glucose out of the blood, into cells.
By stopping you from round 2 – amylin buys insulin the time he needs, to clear the blood of glucose.
When it comes to body chemicals, amylin is a bit of an odd ball.
Amylin shape shifter
Unlike most proteins, amylin is an intrinsically disordered protein – this means amylin shape shifts, i.e. it “adapts” it’s shape, to interact with different targets.
This is, by it’s very nature, a “super power”.
But “super powers” come with vulnerabilities, in the case of amylin, the vulnerability is amylin molecules can interact with themselves.
The result………………… IS NOT PRETTY.
Amylins come together
They form aggregates that bung up the works.
Now, to be fair. Under normal circumstances, amylin molecules are dispatched from the pancreas to go about their business.
Under normal circumstances !
But, when you’re INSULIN RESISTANCE, things are NOT normal. The reason, the pancreas has shifted into overdrive…………
Insulin is being churned out in BUCKET loads.
Morning, noon and night.
The ramped up production, is a desperate attempt to meet the body’s excessive demand for insulin.
Insulin is what is NEEDED. Amylin comes along for the ride…………….. because insulin and amylin are secreted together.
So…………. lots of insulin, also means lots of amylin.
The amylin molecules INTERACT.
Bunging up the works
Now the details of exactly how they BUNG UP THE WORKS, are still a bit sketchy.
The point is, they do, bung up the works.
We know this, because when we look at the pancreas of people who have died with type 2 diabetes, there is marked accumulation of amylin.
This doesn’t happen in the non-diabetics.
Actually, it doesn’t happen in diabetic rodents either.
Turns out, rat amylin doesn’t have the same “super powers” as human amylin. It doesn’t aggregate. This is good for rats, but a problem for scientists studying type 2 diabetes.
It means, the role of amylin is not always appreciated.
Deposits are trouble
The presence of the amylin deposits, create additional stress, on the already pretty stressed out beta cells. Attempts are made to clean up the mess.
But…………… it is a numbers game.
The more amylin floating about, the dire the situation becomes. Especially in the light of the fact, that amylin aggregates are difficult to clean up.
Beta cells in trouble
Stressed out beta cells become
MORE STRESSED OUT.
For many, the accumulation of amylin is the final straw. They give up the ghost.
There are now fewer beta cells…………..
Sugar levels rise
The pancreas’ capacity to produce INSULIN is compromised.
It’s a vicious cycle.
More insulin is needed. More insulin is produced, along with MORE amylin. The MORE amylin molecules interact and aggregate. The amylin aggregates bung up the works. So less insulin is actually produced and sugar levels rise. Eish !
So what can you do ?
Give your beta cells some time off
REIN IN INSULIN and AMYLIN !
By decreasing THE NEED for insulin, you also decrease the production of amylin.
With less amylin moving through the pipes, the odds that the amylin molecules aggregate is significantly reduced.
And if a little aggregation does happen. And it will……… shape shifters are UNSTABLE.
Clean up inside the ER
The clean up crew, can get busy – no harm, no fowl.
Click here for tips and strategies that will help you rein in insulin, using lifestyle.
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