Dataset Information

Hs_PanLibrary_Purified_platelets

ABSTRACT: Hs_PanLibrary_Purified_platelets

REANALYSIS of: PXD000953

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Rosenberger G, et al.

PROVIDER: PAe005347 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

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Publications

A repository of assays to quantify 10,000 human proteins by SWATH-MS.

Rosenberger George G Koh Ching Chiek CC Guo Tiannan T Röst Hannes L HL Kouvonen Petri P Collins Ben C BC Heusel Moritz M Liu Yansheng Y Caron Etienne E Vichalkovski Anton A Faini Marco M Schubert Olga T OT Faridi Pouya P Ebhardt H Alexander HA Matondo Mariette M Lam Henry H Bader Samuel L SL Campbell David S DS Deutsch Eric W EW Moritz Robert L RL Tate Stephen S Aebersold Ruedi R

Scientific data 20140916

Mass spectrometry is the method of choice for deep and reliable exploration of the (human) proteome. Targeted mass spectrometry reliably detects and quantifies pre-determined sets of proteins in a complex biological matrix and is used in studies that rely on the quantitatively accurate and reproducible measurement of proteins across multiple samples. It requires the one-time, a priori generation of a specific measurement assay for each targeted protein. SWATH-MS is a mass spectrometric method th ...[more]

PMID: 25977788

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Project description:Systemic lupus erythematosus is a chronic autoimmune disease with multifactorial ethiopathogenesis. The complement system is involved in both the early and late stages of disease development and organ damage. To better understand autoantibody mediated complement consumption the GAPAID consortium examined ex vivo immune complex formation on autoantigen arrays. We recruited patients with SLE (n=211), with other systemic autoimmune diseases (n=65) and non-autoimmune control subjects (n=149) in two rheumatology tertiary care centers. Standard clinical and laboratory data were collected from all subjects and serum complement levels were determined in SLE patients. The genotype of SNP rs1143679 in the ITGAM gene was also determined. On-chip formation of immune complexes was examined using a functional immunoassay on autoantigen microarray. The amount of antigen-bound IgM, IgG and complement C4 and C3 was quantified on autoantigens comprising nucleic acids, proteins and lipids. Our results show that the relatively high complement consumption of nucleic acids is further increased upon binding of IgM and IgG. This is true even when serum complement levels are decreased due to complement consumption in SLE patients. A negative correlation between serum complement levels and ex vivo complement deposition on nucleic acid autoantigens is demonstrated. On the contrary, most protein and lipid autoantigens show positive correlation with C4 and C3 levels. Genetic analysis reveals that the non-synonymous variant rs1143679 in complement receptor type 3 is associated with an increased production of anti-dsDNA IgG antibodies. Notwithstanding, homozygous carriers of the previously reported susceptible allele (AA) have lower levels of dsDNA specific IgM among SLE patients. Regarding organ involvement we find that besides anti-C1q IgG, low levels of dsDNA specific IgM and low complement C4 binding to C1q are also associated with renal injury. In summary, nucleic acids maintain a skewed complement deposition balance when bound by IgG and IgM, depleting the early classical complement pathway from other physiological processes. Dysfunction of the receptor responsible for complement-mediated apoptotic debris removal promotes the development of autoantibodies targeting nucleic acids. These observations provide serological and genetic evidence for complement-mediated clearance deficiency of apoptotic debris in lupus.

Dataset Information

Hs_PanLibrary_Purified_platelets

Publications

A repository of assays to quantify 10,000 human proteins by SWATH-MS.

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