15 research outputs found
Management of Food Protein-Induced Enterocolitis Syndrome (FPIES): Current Approach and Future Needs
International consensus guidelines for the diagnosis and management of food proteinâinduced enterocolitis syndrome: Executive summaryâWorkgroup Report of the Adverse Reactions to Foods Committee, American Academy of Allergy, Asthma & Immunology
Food protein-induced enterocolitis (FPIES) is a non-IgE cell- mediated food allergy that can be severe and lead to shock. Despite the potential seriousness of reactions, awareness of FPIES is low; high-quality studies providing insight into the pathophysiology, diagnosis, and management are lacking; and clinical outcomes are poorly established. This consensus document is the result of work done by an international workgroup convened through the Adverse Reactions to Foods Committee of the American Academy of Allergy, Asthma & Immunology and the International FPIES Association advocacy group. These are the first international evidence-based guidelines to improve the diagnosis and management of patients with FPIES. Research on prevalence, pathophysiology, diagnostic markers, and future treatments is necessary to improve the care of patients with FPIES. These guidelines will be updated periodically as more evidence becomes available
Identification and Characterization of Proteins Encoded by Chromosome 12 as Part of Chromosome-centric Human Proteome Project
Chromosome-centric human proteome
project (C-HPP) is a global initiative
to comprehensively characterize proteins encoded by genes across all
human chromosomes by teams focusing on individual chromosomes. Here,
we report mass spectrometry-based identification and characterization
of proteins encoded by genes on chromosome 12. Our study is based
on proteomic profiling of 30 different histologically normal human
tissues and cell types using high-resolution mass spectrometry. In
our analysis, we identified 1,535 proteins encoded by 836 genes on
human chromosome 12. This includes 89 genes that are designated as
âmissing proteinsâ by âneXtProtâ as they
did not have any prior evidence either by mass spectrometry or by
antibody-based detection methods. We identified several variant peptides
that reflected coding SNPs annotated in dbSNP database. We also confirmed
the start sites of âŒ200 proteins by identifying protein N-terminal
acetylated peptides. We also identified alternative start sites for
11 proteins that were not annotated in public databases until now.
Most importantly, we identified 12 novel protein coding regions on
chromosome 12 using our proteogenomics strategy. All of the 12 regions
have been annotated as pseudogenes in public databases. This study
demonstrates that there is scope for significantly improving annotation
of protein coding genes in the human genome using mass-spectrometry-derived
data. Individual efforts as part of C-HPP initiative should significantly
contribute toward enriching human protein annotation. The data have
been deposited to ProteomeXchange with identifier PXD000561