Inhibition of glycosaminoglycan synthesis and protein glycosylation with WAS-406 and azaserine result in reduced islet amyloid formation in vitro

Am J Physiol Cell Physiol. 2007 Nov;293(5):C1586-93. doi: 10.1152/ajpcell.00208.2007. Epub 2007 Sep 5.

Abstract

Deposition of islet amyloid polypeptide (IAPP) as amyloid in the pancreatic islet occurs in approximately 90% of individuals with Type 2 diabetes and is associated with decreased islet beta-cell mass and function. Human IAPP (hIAPP), but not rodent IAPP, is amyloidogenic and toxic to islet beta-cells. In addition to IAPP, islet amyloid deposits contain other components, including heparan sulfate proteoglycans (HSPGs). The small molecule 2-acetamido-1,3,6-tri-O-acetyl-2,4-dideoxy-alpha-D-xylo-hexopyranose (WAS-406) inhibits HSPG synthesis in hepatocytes and blocks systemic amyloid A deposition in vivo. To determine whether WAS-406 inhibits localized amyloid formation in the islet, we incubated hIAPP transgenic mouse islets for up to 7 days in 16.7 mM glucose (conditions that result in amyloid deposition) plus increasing concentrations of the inhibitor. WAS-406 at doses of 0, 10, 100, and 1,000 microM resulted in a dose-dependent decrease in amyloid deposition (% islet area occupied by amyloid: 0.66 +/- 0.14%, 0.10 +/- 0.06%, 0.09 +/- 0.07%, and 0.004 +/- 0.003%, P < 0.001) and an increase in beta-cell area in hIAPP transgenic islets (55.0 +/- 2.6 vs. 60.6 +/- 2.2% islet area for 0 vs. 100 microM inhibitor, P = 0.05). Glycosaminoglycan, including heparan sulfate, synthesis was inhibited in both hIAPP transgenic and nontransgenic islets (the latter is a control that does not develop amyloid), while O-linked protein glycosylation was also decreased, and WAS-406 treatment tended to decrease islet viability in nontransgenic islets. Azaserine, an inhibitor of the rate-limiting step of the hexosamine biosynthesis pathway, replicated the effects of WAS-406, resulting in reduction of O-linked protein glycosylation and glycosaminoglycan synthesis and inhibition of islet amyloid formation. In summary, interventions that decrease both glycosaminoglycan synthesis and O-linked protein glycosylation are effective in reducing islet amyloid formation, but their utility as pharmacological agents may be limited due to adverse effects on the islet.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Sugars / pharmacology*
  • Amyloid / genetics
  • Amyloid / metabolism*
  • Animals
  • Azaserine / pharmacology*
  • Cell Line
  • Cell Size
  • Cell Survival
  • Chondroitin Sulfates / metabolism
  • Deoxy Sugars / pharmacology*
  • Dermatan Sulfate / metabolism
  • Dose-Response Relationship, Drug
  • Enzyme Inhibitors / pharmacology*
  • Glucose / metabolism
  • Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / antagonists & inhibitors
  • Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / metabolism
  • Glycosaminoglycans / metabolism*
  • Glycosylation
  • Heparan Sulfate Proteoglycans / metabolism
  • Hexosamines / biosynthesis
  • Humans
  • Insulin / metabolism
  • Insulin-Secreting Cells / drug effects
  • Insulin-Secreting Cells / metabolism
  • Islet Amyloid Polypeptide
  • Islets of Langerhans / cytology
  • Islets of Langerhans / drug effects*
  • Islets of Langerhans / enzymology
  • Islets of Langerhans / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Mice, Inbred DBA
  • Mice, Transgenic
  • Organ Culture Techniques
  • Protein Processing, Post-Translational / drug effects*
  • Time Factors

Substances

  • 2-acetamido-1,3,6-tri-O-acetyl-2,4-dideoxyhexopyranose
  • Amino Sugars
  • Amyloid
  • Deoxy Sugars
  • Enzyme Inhibitors
  • Glycosaminoglycans
  • Heparan Sulfate Proteoglycans
  • Hexosamines
  • Insulin
  • Islet Amyloid Polypeptide
  • Dermatan Sulfate
  • Azaserine
  • Chondroitin Sulfates
  • Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
  • Glucose