Extracellular UDP-Glucose Activates P2Y14 Receptor and Induces Signal Transducer and Activator of Transcription 3 (STAT3) Tyr705 Phosphorylation and Binding to Hyaluronan Synthase 2 (HAS2) Promoter, Stimulating Hyaluronan Synthesis of Keratinocytes

Jokela, Tiina; Kärnä, Riikka; Makkonen, Katri M.; Laitinen, Jarmo T.; Tammi, Raija; Tammi, Markku

doi:10.1074/jbc.m114.551804

Cited by 43 publications

(49 citation statements)

References 61 publications

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“…Selective antagonist for P2Y 14 receptor has not yet been identified. PTX, known as an inhibitor of G i -coupled receptor (Jacobson et al, 2009;Jokela et al, 2014), was used to assess the activation of P2Y 14 receptor induced by OGD in this experiment.…”

Section: Groups and Drug Administrationmentioning

confidence: 99%

Geniposide attenuates inflammatory response by suppressing P2Y14 receptor and downstream ERK1/2 signaling pathway in oxygen and glucose deprivation-induced brain microvascular endothelial cells

et al. 2016

Journal of Ethnopharmacology

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Section: Groups and Drug Administrationmentioning

confidence: 99%

Geniposide attenuates inflammatory response by suppressing P2Y14 receptor and downstream ERK1/2 signaling pathway in oxygen and glucose deprivation-induced brain microvascular endothelial cells

et al. 2016

Journal of Ethnopharmacology

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“…So far eight subtypes of P2Y subfamily have been (Pelegrin et al, 2008;Qu et al, 2011). Like P2X, P2Y receptors also differ in their agonist binding profiles, with one group specific to adenine nucleotides (P2Y 1 , P2Y 12 , P2Y 13 ), another group (P2Y 2 and rodent P2Y 4 ) activated by both adenine and uridine nucleotides, a third group specific to uridine nucleotides (human P2Y 4 and P2Y 6 ) and P2Y 14 activated by UDP-glucose (Jokela et al, 2014). All known subtypes of P2Y receptors are expressed in the CNS with variable distribution among different cell types (i.e.…”

Section: The Role Of P2y Receptors In Neuroinflammationmentioning

confidence: 99%

Purinergic mechanisms in neuroinflammation: An update from molecules to behavior

et al. 2016

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a b s t r a c tThe principle functions of neuroinflammation are to limit tissue damage and promote tissue repair in response to pathogens or injury. While neuroinflammation has utility, pathophysiological inflammatory responses, to some extent, underlie almost all neuropathology. Understanding the mechanisms that control the three stages of inflammation (initiation, propagation and resolution) is therefore of critical importance for developing treatments for diseases of the central nervous system. The purinergic signaling system, involving adenosine, ATP and other purines, plus a host of P1 and P2 receptor subtypes, controls inflammatory responses in complex ways. Activation of the inflammasome, leading to release of pro-inflammatory cytokines, activation and migration of microglia and altered astroglial function are key regulators of the neuroinflammatory response. Here, we review the role of P1 and P2 receptors in mediating these processes and examine their contribution to disorders of the nervous system. Firstly, we give an overview of the concept of neuroinflammation. We then discuss the contribution of P2X, P2Y and P1 receptors to the underlying processes, including a discussion of cross-talk between these different pathways. Finally, we give an overview of the current understanding of purinergic contributions to neuroinflammation in the context of specific disorders of the central nervous system, with special emphasis on neuropsychiatric disorders, characterized by chronic low grade inflammation or maternal inflammation. An understanding of the important purinergic contribution to neuroinflammation underlying neuropathology is likely to be a necessary step towards the development of effective interventions.

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“…A recent study showed that HA does not contribute to the growth and differentiation of human epidermal keratinocyte (Malaisse et al, 2016). Nevertheless, UDP-glucose induces HA synthesis in keratinocytes via P2Y14 receptor, STAT3 signaling and activation of hyaluronan synthase (HAS) promoter (Jokela et al, 2014). The conformation of HA in solution is readily subjected to changes upon altering the compositions of solvents, and this affects the functional properties of HA in many biological processes such as interactions with complement proteins and their associated hemolytic function (Chang and Boackle, 1985; Chang et al, 1985; Hong et al, 2007b).…”

Section: Introductionmentioning

confidence: 99%

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

Hsu

Chiang

Sze

et al. 2016

Front. Cell Dev. Biol.

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Hyaluronidase HYAL-2 is a membrane-anchored protein and also localizes, in part, in the lysosome. Recent study from animal models revealed that both HYAL-1 and HYAL-2 are essential for the metabolism of hyaluronan (HA). Hyal-2 deficiency is associated with chronic thrombotic microangiopathy with hemolytic anemia in mice due to over accumulation of high molecular size HA. HYAL-2 is essential for platelet generation. Membrane HYAL-2 degrades HA bound by co-receptor CD44. Also, in a non-canonical signal pathway, HYAL-2 serves as a receptor for transforming growth factor beta (TGF-β) to signal with downstream tumor suppressors WWOX and SMAD4 to control gene transcription. When SMAD4 responsive element is overly driven by the HYAL-2–WWOX–SMAD4 signaling complex, cell death occurs. When rats are subjected to traumatic brain injury, over accumulation of a HYAL-2–WWOX complex occurs in the nucleus to cause neuronal death. HA induces the signaling of HYAL-2–WWOX–SMAD4 and relocation of the signaling complex to the nucleus. If the signaling complex is overexpressed, bubbling cell death occurs in WWOX-expressing cells. In addition, a small synthetic peptide Zfra (zinc finger-like protein that regulates apoptosis) binds membrane HYAL-2 of non-T/non-B spleen HYAL-2+ CD3− CD19− Z lymphocytes and activates the cells to generate memory anticancer response against many types of cancer cells in vivo. Whether the HYAL-2–WWOX–SMAD4 signaling complex is involved is discussed. In this review and opinion article, we have updated the current knowledge of HA, HYAL-2 and WWOX, HYAL-2–WWOX–SMAD4 signaling, bubbling cell death, and Z cell activation for memory anticancer response.

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Extracellular UDP-Glucose Activates P2Y14 Receptor and Induces Signal Transducer and Activator of Transcription 3 (STAT3) Tyr705 Phosphorylation and Binding to Hyaluronan Synthase 2 (HAS2) Promoter, Stimulating Hyaluronan Synthesis of Keratinocytes

Cited by 43 publications

References 61 publications

Geniposide attenuates inflammatory response by suppressing P2Y14 receptor and downstream ERK1/2 signaling pathway in oxygen and glucose deprivation-induced brain microvascular endothelial cells

Geniposide attenuates inflammatory response by suppressing P2Y14 receptor and downstream ERK1/2 signaling pathway in oxygen and glucose deprivation-induced brain microvascular endothelial cells

Purinergic mechanisms in neuroinflammation: An update from molecules to behavior

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

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