(Glyco)Protein Folding Disorders
The term “protein folding disorders” (PFD) was introduced for a small group of proteins that misfold after biosynthesis producing pathological symptoms, for example, by depositing in inappropriate places. Of these proteins, three can be normally or sometimes N-glycosylated hence the term “(glyco)protein folding disorders” (GFD). However one of these, the Aβ precursor glycoprotein providing the 40, 41, or 42 amino acid residue fragments called amyloid-β-protein (Aβ) that are found in the plaques of patients with Alzheimer’s disease (AD), is also O-GlcNAcylated and many other proteins can also be, which results in misfolding and tissue deposition.
The term “PFD” can also now be applied to many more proteins, as we find out more about their complicated life stories. For example, in Huntington’s Disease (HD), the addition at gene level of repeat CAG means that the protein can be biosynthesized with a long Gln tail. This is somewhat...
- Brooks SA, Dwek MV, Schumacher U (2002) Functional and molecular glycobiology. BIOS Scientific, OxfordGoogle Scholar
- Hounsell EF (2010) NMR spectroscopy of carbohydrates, lipids and membranes. In: Webb G (ed) Specialist reports in NMR spectroscopy. Royal Society of Chemistry, CambridgeGoogle Scholar
- Miyata T, Inagi R, Iida Y, Sato M, Yamada N, Oda O, Maeda K, Seo H (1994) Involvement of β-2 microglobulin modified with advanced glycation end products in the pathogenesis of haemodialysis-associated amyloidosis. Induction of human monocyte chemotaxis and macrophage secretion of tumour necrosis factor-α and interleukin-1. J Clin Invest 93:521–528CrossRefPubMedPubMedCentralGoogle Scholar
- Omtvedt LA, Bailey D, Renouf DV, Davies MJ, Paramonov NA, Haavik S, Husby G, Sletter K, Hounsell EF (2000) Glycosylation of immunoglobulin light chains associated with amyloidosis. Amyloid Int J Clin Invest 7:227–244Google Scholar
- Routier FH, Hounsell EF, Rudd PM, Takahashi N, Bond A, Hay FC, Alavi A, Axford JS, Jeffris R (1998) Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: a critical evaluation of different methods. J Immunol Methods 213(2):113–130CrossRefPubMedGoogle Scholar
- Voet D, Voet JD, Pratt CW (2008) Principles of biochemistry. Wiley, HobokenGoogle Scholar