GlycoFi and Exti, differences, opinion of a poster
From: "canaani" xxxxxxxxxxxxxxx
Date: Thu Nov 13, 2003 8:32 am
'''I hope to shed some light on the difference (IMO) between the therapeutic proteins derived from EXTI cells and proteins generated by the yeast cells of GlycoFi.
Liver cells are complex "protein factories". They produce a plethora of enzymes and factors critical to normal metabolism. These proteins are highly complex and are very often species specific. That is a protein derived from a pig for example, may not be recognized or effective in the human body.
As I understand it, glycosylation the key to the GlycoFi technology. Glycosylation is one metabolic process by which a specific protein is "tagged" for its appropriate site of activity- sort of a key if you will. This would be a final step in creating a functional protein therapeutic from yeast cells. The first step, because yeast cells do not inherently produce these human proteins of interest, would require the insertion of the genetic blueprint for their manufacture. Assuming this geneticly engineered cell functions precisely as designed, studies of that "designer protein" to determine its integrity, safety, and efficacy as a therapeutic would be decidedly complex. The engineering process would be unique to each protein of interest and require validation of each yeast cell line and proein as it is established.
Alternatively, the EXTI human liver cells are potentially capable of generating native human proteins! These cell lines may be modified or optimized for specific protein production, but the "manufacture process" is inherently available. The minimal manipulation of the human liver cell lines should reduce the pathway to FDA approval relative to yeast derived proteins, which translates to reduced cost and timelier product to market.
This is my understanding of the technology- in any case. I hope it helps.
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AI
