Proteomic Profiling of Surface Proteins on Th1 and Th2 Cells

Loyet, Kelly M.; Ouyang, Wenjun; Eaton, Dan; Stults, John T.

doi:10.1021/pr049810q

Cited by 49 publications

(56 citation statements)

References 50 publications

(91 reference statements)

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“…Consistent with this observation, BST2 was found to be more abundant in Th1 T cells, which produce IFN-␥, than Th2 T cells (32). Although the expression on most cells remains low following stimulation, plasma cells and IPC cannot be distinguished on the basis of BST2 expression alone and many other cell types may be difficult to separate.…”

Section: Discussionsupporting

confidence: 64%

Bone Marrow Stromal Cell Antigen 2 Is a Specific Marker of Type I IFN-Producing Cells in the Naive Mouse, but a Promiscuous Cell Surface Antigen following IFN Stimulation

Blasius

Giurisato

Cella

et al. 2006

The Journal of Immunology

383

432

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Type I IFN-producing cells (IPC) are sentinels of viral infections. Identification and functional characterization of these cells have been difficult because of their small numbers in blood and tissues and their complex cell surface phenotype. To overcome this problem in mice, mAbs recognizing IPC-specific cell surface molecules have been generated. In this study, we report the identification of new Abs specific for mouse IPC, which recognize the bone marrow stromal cell Ag 2 (BST2). Interestingly, previously reported IPC-specific Abs 120G8 and plasmacytoid dendritic cell Ag-1 also recognize BST2. BST2 is predominantly specific for mouse IPC in naive mice, but is up-regulated on most cell types following stimulation with type I IFNs and IFN-γ. The activation-induced promiscuous expression of BST2 described in this study has important implications for the use of anti-BST2 Abs in identification and depletion of IPC. Finally, we show that BST2 resides within an intracellular compartment corresponding to the Golgi apparatus, and may be involved in trafficking secreted cytokines in IPC.

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Section: Discussionsupporting

confidence: 64%

Bone Marrow Stromal Cell Antigen 2 Is a Specific Marker of Type I IFN-Producing Cells in the Naive Mouse, but a Promiscuous Cell Surface Antigen following IFN Stimulation

Blasius

Giurisato

Cella

et al. 2006

The Journal of Immunology

383

432

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“…Tandem mass spectrometry was performed on a Q-STAR QTOF with a MALDI source (Applied Biosystems). For additional sequence confirmation, tryptic peptides were analyzed with capillary reverse phase high performance liquid chromatography in-line with an electrospray ionization LCQ Deca ion-trap mass spectrometer (Thermo Finnigan) using a guided single ion monitoring approach as previously described (25,26).…”

Section: Methodsmentioning

confidence: 99%

CAPS Activity in Priming Vesicle Exocytosis Requires CK2 Phosphorylation

Nojiri

Loyet²,

Klenchin

et al. 2009

Journal of Biological Chemistry

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CAPS (Ca 2؉ -dependent activator protein for secretion) functions in priming Ca 2؉ -dependent vesicle exocytosis, but the regulation of CAPS activity has not been characterized. Here we show that phosphorylation by protein kinase CK2 is required for CAPS activity. Dephosphorylation eliminated CAPS activity in reconstituting Ca 2؉ -dependent vesicle exocytosis in permeable and intact PC12 cells. Ser-5, -6, and -7 and Ser-1281 were identified by mass spectrometry as the major phosphorylation sites in the 1289 residue protein. Ser-5, -6, and -7 but not Ser-1281 to Ala substitutions abolished CAPS activity. Protein kinase CK2 phosphorylated CAPS in vitro at these sites and restored the activity of dephosphorylated CAPS. CK2 is the likely in vivo CAPS protein kinase based on inhibition of phosphorylation by tetrabromo-2-benzotriazole in PC12 cells and by the identity of in vivo and in vitro phosphorylation sites. CAPS phosphorylation by CK2 was constitutive, but the elevation of Ca 2؉ in synaptosomes increased CAPS Ser-5 and -6 dephosphorylation, which terminates CAPS activity. These results identify a functionally important N-terminal phosphorylation site that regulates CAPS activity in priming vesicle exocytosis.Regulated neurotransmitter secretion is central to intercellular communication in the nervous system. Two types of secretory vesicles mediate neurotransmitter release; that is, synaptic vesicles that release transmitters such as glutamate at synapses and dense-core vesicles that release modulatory transmitters and neuropeptides at non-synaptic sites. Both types of secretory vesicles are recruited to docking sites on the plasma membrane where they are primed to a ready release state to undergo fusion in response to Ca 2ϩ elevations. Many of the proteins that mediate the targeting, docking, priming, and Ca 2ϩ -dependent fusion of vesicles with the plasma membrane function in both synaptic vesicle and dense-core vesicle pathways (1). CAPS-1 2 (also known as Cadps1) is a 1289-residue protein that reconstitutes Ca 2ϩ -triggered dense-core vesicle exocytosis in permeable neuroendocrine cells at a priming step (2-4). CAPS is required for secretion of a subset of transmitters in Caenorhabditis elegans (5) and Drosophila melanogaster (6) and for priming dense-core vesicle exocytosis in neuroendocrine cells (7) and synaptic vesicle exocytosis in neurons (8). Vesicle priming reactions are extensively modulated during physiological demand (9), but mechanisms that regulate CAPS function remain to be identified.Reversible protein phosphorylation is a major mechanism for the regulation of cellular processes including vesicle exocytosis. Many proteins that function in evoked vesicle exocytosis are phosphoproteins (10, 11). The neuronal SNARE proteins syntaxin 1A, VAMP-2, and SNAP-25 are phosphorylated by several protein kinases in vitro (12)(13)(14). Protein kinase C and protein kinase A sites on SNAP-25 affect refilling rates and size, respectively, of the primed pool of vesicles in chromaffin cells (15,16). Several SNARE...

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“…Other studies focused on T-cell subproteomes within the early stages of T-cell differentiation and investigated proteomic changes in the nucleus of activated human cord blood CD4 ϩ T cells after interleukin-4 stimulation (15) or focused on changes of the global phosphoproteome of human primary T cells in response to 5 min of TCR activation with ␣CD3 (16). In vitro manipulated T cells were previously analyzed such as 7-day cultures of in vitro differentiated T helper 1 and T helper 2 cells (17), however, the surface proteome of human naive CD4 ϩ T cells and how these proteins change during the early time window of ␣CD3/␣CD28 activation has not been investigated so far. Interestingly, knowledge of the surface proteins of naive CD4 ϩ T cells would provide a molecular fingerprint to classify naive CD4 ϩ T cells and especially their cellular state during activation.…”

Section: Naive Cd4mentioning

confidence: 99%

A Combined Omics Approach to Generate the Surface Atlas of Human Naive CD4+ T Cells during Early T-Cell Receptor Activation

Graessel

Hauck

Toerne

et al. 2015

Molecular & Cellular Proteomics

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Naive CD4؉ T cells are the common precursors of multiple effector and memory T-cell subsets and possess a high plasticity in terms of differentiation potential. This stemcell-like character is important for cell therapies aiming at regeneration of specific immunity. Naive CD4ϩ T cells are the common precursors for all other T-helper cell subsets and it is of fundamental importance for specific immunity that their differentiation process is well directed. A complex signaling network is engaged upon antigen recognition that triggers the differentiation process of stemcell-like, plastic, antigen-unexperienced naive T cells into antigen-specific, functional distinct T-cell subphenotypes (1). The differentiation process of naive T cells is tightly regulated in healthy individuals. Pathology develops under dysregulated effector responses such as overshooting responses leading to impaired tolerance (2) or ineffective control of infections (3). Naive T cells are defined by CD45RA expression and they are early cellular targets of immune modulation regarding the differentiation process and the development of long lasting, sustainable therapeutic strategies. In contrast, memory T cells express CD45RO and cover already committed cells such as T helper 1 and T helper 2 cells. Therefore, we chose to investigate the naive CD4 ϩ T cell (CD45RA) and its phenotype during T-cell receptor (TCR) 1 activation. The differentiation From the ‡Center of Allergy and Environment (ZAUM), Technische

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Proteomic Profiling of Surface Proteins on Th1 and Th2 Cells

Cited by 49 publications

References 50 publications

Bone Marrow Stromal Cell Antigen 2 Is a Specific Marker of Type I IFN-Producing Cells in the Naive Mouse, but a Promiscuous Cell Surface Antigen following IFN Stimulation

Bone Marrow Stromal Cell Antigen 2 Is a Specific Marker of Type I IFN-Producing Cells in the Naive Mouse, but a Promiscuous Cell Surface Antigen following IFN Stimulation

CAPS Activity in Priming Vesicle Exocytosis Requires CK2 Phosphorylation

A Combined Omics Approach to Generate the Surface Atlas of Human Naive CD4+ T Cells during Early T-Cell Receptor Activation

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