Src homology 2 domain–containing inositol 5' phosphatase is negatively associated with histamine release to human recombinant histamine-releasing factor in human basophils

Vonakis, Becky M.; Gibbons, Scott P.; Sora, Rebecca; Langdon, Jacqueline M.; MacDonald, Susan

doi:10.1067/mai.2001.119159

Cited by 72 publications

(71 citation statements)

References 52 publications

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“…They found that the activity of the inositol 5 0 phosphatase SHIP-1, which inhibits the PI3-kinase signalling pathway, is inversely correlated with the HRF-dependent histamine release in basophils from IgE(+) donors. This finding was corroborated by the demonstration that the PI3-kinase inhibitor Ly294002 also prevented the HRF-dependent histamine release in these cells (Vonakis et al 2001). In another study, they showed that, in TCTP/HRF-responsive basophils (but not in non-responsive ones), HRF-treatment resulted in phosphorylation of the protein kinase Akt (Vonakis et al 2008), further confirming that the PI3-kinase pathway is involved in mediating the intracellular events in these type of cells.…”

Section: Tctp As Extracellular 'Signaling Molecule' In Immune Reactionsmentioning

confidence: 66%

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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The Translational Controlled Tumour Protein TCTP (gene symbol TPT1, also called P21, P23, Q23, fortilin or histamine-releasing factor, HRF) is a highly conserved protein present in essentially all eukaryotic organisms and involved in many fundamental cell biological and disease processes. It was first discovered about 35 years ago, and it took an extended period of time for its multiple functions to be revealed, and even today we do not yet fully understand all the details. Having witnessed most of this history, in this chapter, I give a brief overview and review the current knowledge on the structure, biological functions, disease involvements and cellular regulation of this protein. TCTP is able to interact with a large number of other proteins and is therefore involved in many core cell biological processes, predominantly in the response to cellular stresses, such as oxidative stress, heat shock, genotoxic stress, imbalance of ion metabolism as well as other conditions. Mechanistically, TCTP acts as an anti-apoptotic protein, and it is involved in DNA-damage repair and in cellular autophagy. Thus, broadly speaking, TCTP can be considered a cytoprotective protein. In addition, TCTP facilitates cell division through stabilising the mitotic spindle and cell growth through modulating growth signalling pathways and through its interaction with the proteosynthetic machinery of the cell. Due to its activities, both as an anti-apoptotic protein and in promoting cell growth and division, TCTP is also essential in the early development of both animals and plants. Apart from its involvement in various biological processes at the cellular level, TCTP can also act as an extracellular protein and as such has been involved in modulating whole-body defence processes, namely in the mammalian immune system. Extracellular TCTP, typically in its dimerised form, is able to induce the release of cytokines and other signalling molecules from various types of immune cells. There are also several examples, where TCTP was shown to be involved in antiviral/antibacterial defence in lower animals. In plants, the protein appears to have a protective effect against phytotoxic stresses, such as flooding, draught, too high or low temperature, salt stress or exposure to heavy metals. The finding for the latter stress condition is corroborated by earlier reports that TCTP levels are considerably up-regulated upon exposure of earthworms to high levels of heavy metals. Given the involvement of TCTP in many biological processes aimed at maintaining cellular or whole-body homeostasis, it is not surprising that dysregulation of TCTP levels may promote a range of disease processes, foremost cancer. Indeed a large body of evidence now supports a role of TCTP in at least the most predominant types of human cancers. Typically, this can be ascribed to both the anti-apoptotic activity of the protein and to its function in promoting cell growth and division. However, TCTP also appears to be involved in the later stages of cancer progression, such ...

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Section: Tctp As Extracellular 'Signaling Molecule' In Immune Reactionsmentioning

confidence: 66%

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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“…Agents that inhibit cytoskeletal formation markedly enhance secretion in RBL cells and have the same functional effect in basophils (11). Recent studies in murine mast cells suggest that Src homology 2-containing 5Ј-inositol phosphatase (SHIP) is a critical down-regulator of ongoing secretion whose absence leads to hypersecretion (12), and a similar finding may apply to human basophils (13,14).…”

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confidence: 76%

Two Regions of Down-Regulation in the IgE-Mediated Signaling Pathway in Human Basophils

MacGlashan¹

2003

The Journal of Immunology

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Previous studies demonstrated that after stimulation of human basophils with a polyclonal anti-IgE Ab, early signaling elements showed sustained phosphorylation, whereas later elements were transient, suggesting that a region of down-regulation involved inhibition of phosphatidylinositol (PI) 3 kinase or its products. However, the current studies show that under some conditions, syk phosphorylation is transient. Generally, stimulation with a variety of Ags makes this early form of down-regulation more apparent. An exploration of the conditions needed to induce early down-regulation indicates that both the nature of aggregation and the cell surface density of IgE play roles. It was also found that the previously described late form of down-regulation (PI3 kinase product transience) can occur in cells displaying early down-regulation (transient syk phosphorylation), but this phenomenon is revealed by testing for subsequent down-regulation of the response to non-cross-reacting stimuli, altering their ability to induce phosphorylation of Akt or extracellular signal-regulated kinase. In contrast, phosphorylation of syk kinase, in response to a non-cross-reacting stimulus, was relatively unaffected by prior stimulation. The magnitude of cross-desensitization of the Akt or extracellular signal-regulated kinase response was a function of the strength of the first stimulus. Mediator release showed a similar cross-desensitization effect. Therefore, stimulation induces two forms of down-regulation, one operating before or at the level of syk phosphorylation, possibly characterizing the process formerly known as specific desensitization, and one that operates in the region of PI3 kinase, accounting for the process formerly known as nonspecific desensitization, which is dependent on the strength of stimulus.

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“…In vitro studies have shown that SHIP-1 functioned as a negative regulator in mast cell degranulation in mouse cells 19 and human cells. 20 IL-4 stimulation of 32D cells resulted in phosphorylation of SHIP-1, 13 suggesting its involvement in the T H 2 signaling. Dendritic cells from Lyndeficient mice had decreased phosphorylation of SHIP-1, suggesting that SHIP-1 might participate in regulating dendritic cell (DC) activation in response to allergen.…”

Section: Discussionmentioning

confidence: 96%

Src homology 2 domain–containing inositol 5-phosphatase 1 deficiency leads to a spontaneous allergic inflammation in the murine lung

Zheng

Bailey

et al. 2007

Journal of Allergy and Clinical Immunology

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Background-Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP-1) controls the intracellular level of the phosphoinositide 3-kinase product phosphotidylinositol-3,4,5-trisphosphate and functions as a negative regulator of cytokine and immune receptor signaling. Emerging evidence suggests that the phosphoinositide 3-kinase pathway might be involved in allergic inflammation in the lung. However, the functional relevance of SHIP-1 in the T H 2 activation pathway has not been established. SHIP-1 −/− mice have spontaneous myeloproliferative inflammation in the lung, the nature of which has not been elucidated. We hypothesized that SHIP-1 plays an important role as a regulator in pulmonary allergic inflammation and in maintaining lung homeostasis.

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Src homology 2 domain–containing inositol 5' phosphatase is negatively associated with histamine release to human recombinant histamine-releasing factor in human basophils

Cited by 72 publications

References 52 publications

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Two Regions of Down-Regulation in the IgE-Mediated Signaling Pathway in Human Basophils

Src homology 2 domain–containing inositol 5-phosphatase 1 deficiency leads to a spontaneous allergic inflammation in the murine lung

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