Team:UC Davis/Treatments

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(New page: =Current treatments= Currently, no cure has been found for this illness. The only way to avoid some of celiac disease’s symptoms is by adopting a gluten free diet (14, 12, and 11). Howe...)
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=Current treatments=
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=Current Treatments=
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Currently, no cure has been found for this illness. The only way to avoid some of celiac disease’s symptoms is by adopting a gluten free diet (14, 12, and 11). However, you are more likely to find gluten in your everyday diet. Therefore, avoiding gluten is not easy or pleasant from a gastronomical standpoint.
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Currently, there is no cure for this genetic condition. Prevention of the symptoms associated with celiac disease is accomplished through adopting a gluten-free diet (14, 12, 11). However, gluten is present in most everyday diets, making it difficult to have a gluten-free diet.
   
   
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"Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8). However, enzymes studied earlier were not able to degrade gluten (inside stomach before it reaches small intestine because they were "irreversibly inactivated by pepsin and acidic pH, both present in the stomach."(8)
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"Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8) However, enzymes studied earlier were not able to degrade gluten inside stomach before it reaches small intestine because they were "irreversibly inactivated by pepsin and acidic pH, both present in the stomach."(8)
              
              
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Nevertheless, over the past years, researchers have discovered an enzyme from ''Aspergillus niger'', a newly identified prolyl endoprotease, that was observed to "work optimally at 4-5pH and remains stable at 2pH"(8) and maybe this enzyme will lead us to an alternative treatment for this disorder (8). Studies have shown that prolyl-endoprotease from ''Aspergillus niger'' is able to "degrade gluten in vitro and under conditions similar to the ones present in the gastrointestinal tract." (8) ; but due to licensing restrictions we have opted not to work with this protein.
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Over the past years, researchers discovered an enzyme from the bacterium ''Aspergillus niger''. This recently identified prolyl endoprotease was observed to "work optimally at 4-5 pH and [remain] stable at 2 pH".(8) It is possible that this enzyme may provide an alternative treatment for celiac disease. (8) Studies have shown that prolyl endoprotease is able to "degrade gluten ''in vitro'' and under conditions similar to the ones present in the gastrointestinal tract." (8) However, due to licensing restrictions we have opted not to work with this protein.
              
              
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Recently (year 2007), a study has suggested an alternative approach by combining a glutamine-specific endoprotease (EP-B2 from barley) and a prolyl endopeptidase (SC PEP from Sphingomonas capsulata); with gastric activity and complementary substrate specificity there is a possibility of increasing the safe threshold of ingested gluten (12). One of the advantages of this “combination product is that both enzymes are active and stable in stomach and can therefore be administered as lyophilized powders or simple capsules or tablets” (12).
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In 2007, a study suggested an alternative approach by combining a glutamine-specific endoprotease (EP-B2 from barley) and a prolyl endopeptidase (SC PEP from ''Sphingomonas capsulata''); with gastric activity and complementary substrate specificity there is a possibility of increasing the safe threshold of ingested gluten (12). An advantage of this “combination product is that both enzymes are active and stable in stomach and can therefore be administered as lyophilized powders or simple capsules or tablets” (12).
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''Note: Moreover, this study was first “evaluated via in vitro digestion of whole-wheat beard and then confirmed by in vivo studies in rats (12), unlike other earlier studies which were performed on synthetic gluten oligopeptides, recombinant gliadin proteins, or uncooked gluten” (12).''
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''Note: This study was first “evaluated via in vitro digestion of whole-wheat bread and then confirmed by in vivo studies in rats (12), unlike other earlier studies which were performed on synthetic gluten oligopeptides, recombinant gliadin proteins, or uncooked gluten” (12).''
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Latest revision as of 22:08, 23 September 2009

Current Treatments

Currently, there is no cure for this genetic condition. Prevention of the symptoms associated with celiac disease is accomplished through adopting a gluten-free diet (14, 12, 11). However, gluten is present in most everyday diets, making it difficult to have a gluten-free diet.

"Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8) However, enzymes studied earlier were not able to degrade gluten inside stomach before it reaches small intestine because they were "irreversibly inactivated by pepsin and acidic pH, both present in the stomach."(8)

Over the past years, researchers discovered an enzyme from the bacterium Aspergillus niger. This recently identified prolyl endoprotease was observed to "work optimally at 4-5 pH and [remain] stable at 2 pH".(8) It is possible that this enzyme may provide an alternative treatment for celiac disease. (8) Studies have shown that prolyl endoprotease is able to "degrade gluten in vitro and under conditions similar to the ones present in the gastrointestinal tract." (8) However, due to licensing restrictions we have opted not to work with this protein.

In 2007, a study suggested an alternative approach by combining a glutamine-specific endoprotease (EP-B2 from barley) and a prolyl endopeptidase (SC PEP from Sphingomonas capsulata); with gastric activity and complementary substrate specificity there is a possibility of increasing the safe threshold of ingested gluten (12). An advantage of this “combination product is that both enzymes are active and stable in stomach and can therefore be administered as lyophilized powders or simple capsules or tablets” (12).

Note: This study was first “evaluated via in vitro digestion of whole-wheat bread and then confirmed by in vivo studies in rats (12), unlike other earlier studies which were performed on synthetic gluten oligopeptides, recombinant gliadin proteins, or uncooked gluten” (12).

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