Re: Cataract cure finally found, but just left to rot

Browbie
I don't know what sort of cataracts you have. Are they white, yellow or brown?
If they are white, there is a good chance you don't have AGE-related cataracts, because many AGEs are colored chromophores. If they are white, they could be just due to simple misfolding and aggregation of crystallin. In that case, I would expect Lanomax to work. In my case, I have yellow/reddish-brown fluorescent cataracts, almost certainly due to binding of crystallin to the yellow pigment "imidazolone", and with this causality, I cannot see how Lanomax would work.

And I don't have cataracts which fluoresce blue.
That is another common type due to combination of crystallin with tryptophan metabolism end-products, notably the blue fluorophores xanthurenic acid, its glycosides and its oxidation products. There is research under way on treating common tryptophan-related cataracts like this with certain light wavelengths, and clinical trials using this method are slated to happen in the next few years. It is noteworthy that although light transmission through the lens was greatly improved by this treatment, levels of all AGEs in the lens, including imidazolone, were completely unchanged. This points to the fact that the light therapy was breaking up something else apart from the AGEs, which I suppose was the tryptophan derivatives I mentioned.

I remember when I got my cataracts about 4 years ago. At that time, when I had nephrotic syndrome (proteinuria), I went on a "no-protein" diet in an effort to cure the proteinuria and improve kidney function (GFR). It did not cure the proteinuria or increase GFR, but it did give me cataracts. The presence of proteinuria itself suggests that AGEs like imidazolone are damaging kidney function by combining with kidney proteins.
I found a reference as to why cutting out protein could cause cataracts of the AGE-related type:

https://www.ncbi.nlm.nih.gov/pubmed/11477156

Here, it is shown that the enzyme trypsin inhibited the binding of the AGE imidazolone to BSA protein (bovine serum albumin) in the kidney. Since trypsin is produced by the pancreas only "on demand" when protein is consumed, it is clear that there would be a deficiency of trypsin in the system when no protein is consumed. And I believe that is exactly what happened in my case, since due to my proteinuria, I already had an excess of imidazolone in my blood. So, it was a terrible mistake to try to improve kidney function by cutting out protein altogether.

Tryptophan of course is an amino acid, while the AGE imidazolone is formed by combination of the amino acid arginine with methyl glyoxal via what is known as the Maillard reaction. Both tryptophan and arginine are amino acids, so it would appear they are separately responsible for two different types of cataracts, as I outlined above.
Now trypsin can only prevent accumulation of AGEs and AGE-protein addition products; it probably can't break AGEs once they are formed. Only an AGE-breaker like phenacyl thiazolium bromide can do that.
In the end, I think that if I were to try Lanomax again, it would have to be in combination with some kind of AGE-breaker therapy. So far, I have not found any company interested in taking this further.