6 research outputs found
Temporal Quantitative Phosphoproteomics Profiling of Interleukin-33 Signaling Network Reveals Unique Modulators of Monocyte Activation
Interleukin-33 (IL-33), a member of the IL-1 superfamily cytokines, is an endogenous danger signal and a nuclear-associated cytokine. It is one of the essential mediators of both innate and adaptive immune responses. Aberrant IL-33 signaling has been demonstrated to play a defensive role against various infectious and inflammatory diseases. Although the signaling responses mediated by IL-33 have been previously reported, the temporal signaling dynamics are yet to be explored. To this end, we applied quantitative temporal phosphoproteomics analysis to elucidate pathways and proteins induced by IL-33 in THP-1 monocytes. Employing a TMT labeling-based quantitation and titanium dioxide (TiO2)-based phosphopeptide enrichment strategy followed by mass spectrometry analysis, we identified and quantified 9448 unique phosphopeptides corresponding to 3392 proteins that showed differential regulation. Of these, 171 protein kinases, 60 phosphatases and 178 transcription factors were regulated at different phases of IL-33 signaling. In addition to the confirmed activation of canonical signaling modules including MAPK, NFκB, PI3K/AKT modules, pathway analysis of the time-dependent phosphorylation dynamics revealed enrichment of several cellular processes, including leukocyte adhesion, response to reactive oxygen species, cell cycle checkpoints, DNA damage and repair pathways. The detailed quantitative phosphoproteomic map of IL-33 signaling will serve as a potentially useful resource to study its function in the context of inflammatory and pathological conditions
Characterization of human pineal gland proteome
We employed a high-resolution mass spectrometry-based approach to characterize the proteome of the human pineal gland.</p
Proteomic Analysis of Adult Human Hippocampal Subfields Demonstrates Regional Heterogeneity in the Protein Expression
Background: Distinct hippocampal subfields are known
to get affected during aging, psychiatric disorders, and various neurological
and neurodegenerative conditions. To understand the biological processes
associated with each subfield, it is important to understand its heterogeneity
at the molecular level. To address this lacuna, we investigated the
proteomic analysis of hippocampal subfieldsthe cornu ammonis
sectors (CA1, CA2, CA3, CA4) and dentate gyrus (DG) from healthy adult
human cohorts. Findings: Microdissection of hippocampal
subfields from archived formalin-fixed paraffin-embedded tissue sections
followed by TMT-based multiplexed proteomic analysis resulted in the
identification of 5,593 proteins. Out of these, 890 proteins were
found to be differentially abundant among the subfields. Further bioinformatics
analysis suggested proteins related to gene splicing, transportation,
myelination, structural activity, and learning processes to be differentially
abundant in DG, CA4, CA3, CA2, and CA1, respectively. A subset of
proteins was selected for immunohistochemistry-based validation in
an independent set of hippocampal samples. Conclusions: We believe that our findings will effectively pave the way for further
analysis of the hippocampal subdivisions and provide awareness of
its subfield-specific association to various neurofunctional anomalies
in the future. The current mass spectrometry data is deposited and
publicly made available through ProteomeXchange Consortium via the
PRIDE partner repository with the data set identifier PXD029697
Proteomic Analysis of Adult Human Hippocampal Subfields Demonstrates Regional Heterogeneity in the Protein Expression
Background: Distinct hippocampal subfields are known
to get affected during aging, psychiatric disorders, and various neurological
and neurodegenerative conditions. To understand the biological processes
associated with each subfield, it is important to understand its heterogeneity
at the molecular level. To address this lacuna, we investigated the
proteomic analysis of hippocampal subfieldsthe cornu ammonis
sectors (CA1, CA2, CA3, CA4) and dentate gyrus (DG) from healthy adult
human cohorts. Findings: Microdissection of hippocampal
subfields from archived formalin-fixed paraffin-embedded tissue sections
followed by TMT-based multiplexed proteomic analysis resulted in the
identification of 5,593 proteins. Out of these, 890 proteins were
found to be differentially abundant among the subfields. Further bioinformatics
analysis suggested proteins related to gene splicing, transportation,
myelination, structural activity, and learning processes to be differentially
abundant in DG, CA4, CA3, CA2, and CA1, respectively. A subset of
proteins was selected for immunohistochemistry-based validation in
an independent set of hippocampal samples. Conclusions: We believe that our findings will effectively pave the way for further
analysis of the hippocampal subdivisions and provide awareness of
its subfield-specific association to various neurofunctional anomalies
in the future. The current mass spectrometry data is deposited and
publicly made available through ProteomeXchange Consortium via the
PRIDE partner repository with the data set identifier PXD029697