neurotoxin1 (endogenous)

http://www.informatics.jax.org/allele/MGI:3716630

The LYNX1 gene encodes a protein that shares characteristics with toxins that bind and inhibit nicotinic acetylcholine receptors (nAChR; see, e.g., CHRNA1, 100690) (Miwa et al., 1999). Components of snake venoms often have structural and functional mammalian homologs. For example, hemolytic snake venom toxins are related to cellular phospholipases (e.g., PLA2G1B; 172410), and snake sarafotoxins may be related to vertebrate endothelins (e.g., EDN1; 131240). The elapid venom alpha-bungarotoxin also binds to and inhibits nAChR
 
https://www.frontiersin.org/articles/10.3389/fphar.2019.00343/full

Lynx Prototoxins: Roles of Endogenous Mammalian Neurotoxin-Like Proteins in Modulating Nicotinic Acetylcholine Receptor Function to Influence Complex Biological Processes

The cholinergic system modulates many biological functions, due to the widespread distribution of cholinergic neuronal terminals, and the diffuse release of its neurotransmitter, acetylcholine. Several layers of regulation help to refine and control the scope of this excitatory neurotransmitter system. One such regulatory mechanism is imparted through endogenous toxin-like proteins, prototoxins, which largely control the function of nicotinic receptors of the cholinergic system. Prototoxins and neurotoxins share the distinct three finger toxin fold, highly effective as a receptor binding protein, and the former are expressed in the mammalian brain, immune system, epithelium, etc. Prototoxins and elapid snake neurotoxins appear to be related through gene duplication and divergence from a common ancestral gene. Protein modulators can provide a graded response of the cholinergic system, and within the brain, stabilize neural circuitry through direct interaction with nicotinic receptors.
 
lansbergen said:
and within the brain, stabilize neural circuitry through direct interaction with nicotinic receptors.
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I've probably got the wrong end of the stick here but would this explain why my brain goes all 'slidey' (like driving on black ice) when I don't have nicotine?

Or why my eyesight goes in the same situation, remaining degraded for years, but instantly fixed by nicotine.

Or why a popular mouth ulcer pain killing gel (bonjela) which works using something to do with acetylcholine to kill pain, actually causes me to be in agony, until it wears off?
 
Wonko said:
I've probably got the wrong end of the stick here but would this explain why my brain goes all 'slidey' (like driving on black ice) when I don't have nicotine?

Or why my eyesight goes in the same situation, remaining degraded for years, but instantly fixed by nicotine.

Or why a popular mouth ulcer pain killing gel (bonjela) which works using something to do with acetylcholine to kill pain, actually causes me to be in agony, until it wears off?
Click to expand...

We need more information. Maybe @mariovitali can find what proteins the prototoxin lynx1 makes in humans.
 
Mithriel said:
I was part of a study that found that acetylcholine was cleared more slowly by people with ME. Because the test could not be influenced, the technician was happy to talk about my results. It is the only positive test I have had for ME :)
Click to expand...

Would that happen when the receptor is occupied by something else?
 
I'm not sure. It was done by measuring the width of blood vessels with a laser. They dropped some acetylcholine on my arm and it made the blood vessels dilate. In healthy controls the acetylcholine is mopped up in some way (like the usual feedback mechanisms that work in biology) but mine stayed open for much longer meaning the acetylcholine remained.

I've tried to find out more about what would be happening since it could explain more of my symptoms but I've not been able to find anything at a level I can understand.

The actual research was looking at what caused orthostatic intolerance.
 
Low complement c3 mimicks snake venom effect
I suspect I have inherited mine

In addition to studying C3 deficiency in diagnosed human patients, researchers have studied C3 deficiency in animals. C3 deficiency can be induced by injecting animals with cobra venom factor, which functions like an unregulated C3-convertase because factor I and factor H do not regulate it, cleaving most C3 molecules in the serum into C3a and C3b fragments, which depletes the amount of intact C3.[4]
https://en.m.wikipedia.org/wiki/Complement_3_deficiency
 
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