Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

Kathryn J. Potter(University of British Columbia), Andisheh Abedini(Columbia University), Peter Marek(State University of New York), Agnieszka Klimek‐Abercrombie(University of British Columbia), Sonia A. Butterworth(University of British Columbia), Miles Driscoll(State University of New York), Rocky L. Baker(University of British Columbia), Melanie R. Nilsson(McDaniel College), Garth L. Warnock(University of British Columbia), José Oberholzer(University of Illinois Chicago), Suzanne Bertera(University of Pittsburgh), Massimo Trucco(University of Pittsburgh), Gregory S. Korbutt(University of Alberta), Paul E. Fraser(University of Toronto), Daniel P. Raleigh(State University of New York), C. Bruce Verchere(University of British Columbia)
Proceedings of the National Academy of Sciences
February 16, 2010
Cited by 171Open Access
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Abstract

Islet transplantation is a promising treatment for diabetes but long-term success is limited by progressive graft loss. Aggregates of the beta cell peptide islet amyloid polypeptide (IAPP) promote beta cell apoptosis and rapid amyloid formation occurs in transplanted islets. Porcine islets are an attractive alternative islet source as they demonstrate long-term graft survival. We compared the capacity of transplanted human and porcine islets to form amyloid as an explanation for differences in graft survival. Human islets were transplanted into streptozotocin-diabetic immune-deficient mice. Amyloid deposition was detectable at 4 weeks posttransplantation and was associated with islet graft failure. More extensive amyloid deposition was observed after 8 weeks. By contrast, no amyloid was detected in transplanted neonatal or adult porcine islets that had maintained normoglycemia for up to 195 days. To determine whether differences in IAPP sequence between humans and pigs could explain differences in amyloid formation and transplant viability, we sequenced porcine IAPP. Porcine IAPP differs from the human sequence at 10 positions and includes substitutions predicted to reduce its amyloidogenicity. Synthetic porcine IAPP was considerably less amyloidogenic than human IAPP as determined by transmission electron microscopy, circular dichroism, and thioflavin T binding. Viability assays indicated that porcine IAPP is significantly less toxic to INS-1 beta cells than human IAPP. Our findings demonstrate that species differences in IAPP sequence can explain the lack of amyloid formation and improved survival of transplanted porcine islets. These data highlight the potential of porcine islet transplantation as a therapeutic approach for human diabetes.


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