The Millhauser Lab    Prions, Alzheimer's Disease, EPR, NMR
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Prion Protein
      Alzheimer's Disease

PrP-Cu
  PrP-Aβ


Misfolding of PrPC causes prion diseases, which include kuru, CJD and mad cow disease.  PrP's normal function is related to copper and zinc regulation in the central nervous system. Cu2+ promotes an interaction between the protein's domains that suppresses inherent neurotoxicity. (J. Mol. Biol. 432:4408-25 2020, Meth. Enzymol. 666:297-314 2022)
PrPC is a primary receptor for the Aβ peptide and its aggregates, which form senile plaques that initiate Alzheimer's disease. Confocal microscopy shows that Aβ with a fluorescent tag (green) is imported into PrP expressing cells. (PNAS 117:28625-31 2020).

Research Funded by the National Institute of General Medical Sciences, NIH R35 GM131781                       
                            

    UCSC Chemistry           PBSE             qb3          

                         

                      


Professor Glenn L. Millhauser
Department of Chemistry & Biochemistry
University of California, Santa Cruz
Santa Cruz, CA 95064

glennm at ucsc.edu

office phone  831 459 2176
lab phone  831 459 3390
fax  831 459 2935

Web design by Chloe S. Millhauser