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amstocks82

04/28/17 1:48 AM

#103292 RE: OFP #103283

"Well I think your reference (among many others) make it clear that s1R unequivocally DOES chaperone proteins."



LOL.

1. S1R is a protein
2. Its chaperone function is mediated by protein-protein interaction and translocation (reference provided upon request).



The fact that you think those two points make your point is interesting. It shows you are unable to comprehend the links I provided.

Here is the same information posted another way: "the sigma-1 receptor chaperones the functional IP3 receptor at the endoplasmic reticulum and mitochondrion interface to ensure proper Ca2+ signaling from endoplasmic reticulum into mitochondrion. However, under pathological conditions whereby cells encounter enormous stress that results in the endoplasmic reticulum losing its global Ca2+ homeostasis, the sigma-1 receptor translocates and counteracts the arising apoptosis. Thus, the sigma-1 receptor is a receptor chaperone essential for the metabotropic receptor signaling and for the survival against cellular stress."

"I do find it a bit amusing that I'm the one taking the AVXL line on an issue. "



And I find it amusing that you THINK you are taking the AVXL line. You aren't.

I can see I'm wasting my time though with you.