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Yong Dai
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ORCiD: https://orcid.org/0000-0002-6840-9158
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Systemic lupus erythematosus (SLE) is a complex autoimmune disease that affects multiple organs, the pathogenic mechanism is related to many factors, but the specific pathogenic mechanism has not been clarified yet. Protein lysine modifications play important roles in gene regulation, transcription, metabolism and other biological processes. The lysine 2-hydroxyisobutyrylation(K hib ) histone mark has recently been discovered as a novel protein modification. In this study, patients in the active SLE group were examined (N=8), while the control group was healthy (N=20).Utilizing antibody-based affinity enrichment and nano-HPLC/MS/MS analyses of K hib peptides, we identified 156 upregulated proteins(fold change>1.5),124 downregulated proteins(fold change<1/1.5), including 220 K hib sites that were upregulated and 187 K hib sites that were downregulated. Our data demonstrate that proteins with K hib sites were localized in the cytoplasm. Functional enrichment analysis revealed that proteins with K hib sites are broadly involved in a wide range of biological processes, cellular components and molecular functions. The 03010 Ribosome pathways may exert important influence on the SLE pathogenic mechanism, according to a KEGG analysis. The functional analysis of K hib is of value for important future investigations of SLE pathogenesis.
Keywords
SLE, 2-hydroxyisobutyrylation, Mass spectrometry, Bioinformatics
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This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Research
Yong Dai
Corresponding Author
ORCiD: https://orcid.org/0000-0002-6840-9158
Badges
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Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
History
CURRENT STATUS: Posted
The most recent version of this article is available here.
No community comments so far
Version 1
Posted 23 Mar, 2020
No comments provided
Metrics
Comments: 0
PDF Downloads: ...
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Subject Areas
Bioinformatics
License:
This work is licensed under a CC BY 4.0 License. Read Full License
The most recent version of this article is available here.
Systemic lupus erythematosus (SLE) is a complex autoimmune disease that affects multiple organs, the pathogenic mechanism is related to many factors, but the specific pathogenic mechanism has not been clarified yet. Protein lysine modifications play important roles in gene regulation, transcription, metabolism and other biological processes. The lysine 2-hydroxyisobutyrylation(K hib ) histone mark has recently been discovered as a novel protein modification. In this study, patients in the active SLE group were examined (N=8), while the control group was healthy (N=20).Utilizing antibody-based affinity enrichment and nano-HPLC/MS/MS analyses of K hib peptides, we identified 156 upregulated proteins(fold change>1.5),124 downregulated proteins(fold change<1/1.5), including 220 K hib sites that were upregulated and 187 K hib sites that were downregulated. Our data demonstrate that proteins with K hib sites were localized in the cytoplasm. Functional enrichment analysis revealed that proteins with K hib sites are broadly involved in a wide range of biological processes, cellular components and molecular functions. The 03010 Ribosome pathways may exert important influence on the SLE pathogenic mechanism, according to a KEGG analysis. The functional analysis of K hib is of value for important future investigations of SLE pathogenesis.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
This is a list of supplementary files associated with this preprint. Click to download.
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