Purinsubstanzen (Bd. IV, S. 1014)

Fodor, A.

doi:10.1007/978-3-642-51371-8_14

Cited by 1 publication

(1 citation statement)

References 79 publications

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“…The use of proteases in bottom-up proteomics introduces the possibility of generating hybrid peptides during sample preparation. 35,36 When a peptide bond is attacked by the catalytic site of a protease such as GluC or trypsin, two products are generated: the free C-terminal peptide fragment and an acyl-enzyme intermediate consisting of the enzyme bound via an ester bond to the C-terminus of the N-terminal peptide fragment. Usually, a water molecule hydrolyzes this ester bond, liberating the N-terminal peptide fragment from the enzyme.…”

Section: Discussionmentioning

confidence: 99%

Identification of Hybrid Insulin Peptides (HIPs) in Mouse and Human Islets by Mass Spectrometry

et al. 2018

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We recently discovered hybrid insulin peptides (HIPs) as a novel class of post-translationally modified peptides in murine-derived beta cell tumors, and we demonstrated that these molecules are autoantigens in type 1 diabetes (T1D). A HIP consists of an insulin fragment linked to another secretory granule peptide via a peptide bond. We verified that autoreactive CD4 T cells in both mouse and human autoimmune diabetes recognize these modified peptides. Here, we use mass spectrometric analyses to confirm the presence of HIPs in both mouse and human pancreatic islets. We also present criteria for the confident identification of these peptides. This work supports the hypothesis that HIPs are autoantigens in human T1D and provides a foundation for future efforts to interrogate this previously unknown component of the beta cell proteome.

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Section: Discussionmentioning

confidence: 99%