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  1. Article ; Online: Measurement of orexin levels is currently an uncertain business.

    Kukkonen, Jyrki P

    Sleep medicine

    2023  Volume 107, Page(s) 308

    MeSH term(s) Humans ; Orexins ; Orexin Receptors
    Chemical Substances Orexins ; Orexin Receptors
    Language English
    Publishing date 2023-05-26
    Publishing country Netherlands
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2012041-2
    ISSN 1878-5506 ; 1389-9457
    ISSN (online) 1878-5506
    ISSN 1389-9457
    DOI 10.1016/j.sleep.2023.05.022
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    Zs.A 5315: Show issues Location:
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  2. Article ; Online: The G protein preference of orexin receptors is currently an unresolved issue.

    Kukkonen, Jyrki P

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 3162

    MeSH term(s) Orexin Receptors ; Orexins ; GTP-Binding Proteins ; Receptors, G-Protein-Coupled/genetics ; Receptors, Neuropeptide ; Benzoxazoles
    Chemical Substances Orexin Receptors ; Orexins ; GTP-Binding Proteins (EC 3.6.1.-) ; Receptors, G-Protein-Coupled ; Receptors, Neuropeptide ; Benzoxazoles
    Language English
    Publishing date 2023-06-01
    Publishing country England
    Document type Letter ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38764-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The G protein preference of orexin receptors is currently an unresolved issue

    Jyrki P. Kukkonen

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Volume 3

    Keywords Science ; Q
    Language English
    Publishing date 2023-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Allosteric interactions via the orthosteric ligand binding sites in a constitutive G-protein-coupled receptor homodimer.

    Kukkonen, Jyrki P

    Pharmacological research

    2020  Volume 166, Page(s) 105116

    Abstract: I interpret some recent data to indicate that co-operative effects take place between the (identical) orthosteric binding sites in a G-protein-coupled receptor dimer. In the current study, the reasonability of this concept was tested by creating a ... ...

    Abstract I interpret some recent data to indicate that co-operative effects take place between the (identical) orthosteric binding sites in a G-protein-coupled receptor dimer. In the current study, the reasonability of this concept was tested by creating a mathematical model. The model is composed of a symmetrical constitutive receptor dimer in which the protomers are able to affect each other allosterically, and it includes binding, receptor activation and signal amplification steps. The model was utilized for analyses of previous data as well as simulations of predicted behaviour. The model demonstrates the behaviour stated in the hypotheses, i.e. even an apparently neutral receptor ligand can allosterically affect agonist binding or receptor activation by binding to the normal orthosteric ligand binding site. Therewith the speculated allosteric action originating from the orthosteric binding site of the dimeric receptor is a realistic possibility. The results of the simulations and curve fitting constitute a reasonable starting point for further studies, and the model can be utilized to design meaningful experiments to investigate these questions.
    MeSH term(s) Allosteric Regulation ; Binding Sites ; Humans ; Ligands ; Orexin Receptors/chemistry ; Orexin Receptors/metabolism ; Protein Binding ; Protein Multimerization ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism
    Chemical Substances Ligands ; Orexin Receptors ; Receptors, G-Protein-Coupled
    Language English
    Publishing date 2020-08-09
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1003347-6
    ISSN 1096-1186 ; 0031-6989 ; 1043-6618
    ISSN (online) 1096-1186
    ISSN 0031-6989 ; 1043-6618
    DOI 10.1016/j.phrs.2020.105116
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 721: Show issues Location:
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  5. Article ; Online: Cellular Signaling Mechanisms of Hypocretin/Orexin.

    Kukkonen, Jyrki P / Turunen, Pauli M

    Frontiers of neurology and neuroscience

    2021  Volume 45, Page(s) 91–102

    Abstract: Orexin receptors (OXRs) are promiscuous G-protein-coupled receptors that signal via several G-proteins and, putatively, via other proteins. On which basis the signal pathways are selected and orchestrated is largely unknown. We also have an insufficient ... ...

    Abstract Orexin receptors (OXRs) are promiscuous G-protein-coupled receptors that signal via several G-proteins and, putatively, via other proteins. On which basis the signal pathways are selected and orchestrated is largely unknown. We also have an insufficient understanding of the kind of signaling that is important for specific types of cellular responses. OXRs are able to form complexes with several other G-protein-coupled receptors in vitro, and one possibility is that the complexing partners regulate the use of certain signal transducers. In the central nervous system neurons, the main acute downstream responses of OXR activation are the inhibition of K+ channels and the activation of the Na+/Ca2+ exchanger and non-selective cation channels of unknown identity. The exact nature of the intracellular signal chain between the OXRs and these downstream targets is yet to be elucidated, but the Gq-phospholipase C (PLC) protein kinase C pathway - which is a significant signaling pathway for OXRs in recombinant cells - may be one of the players in neurons. The Gq-PLC pathway may also, under certain circumstances, take the route to diacylglycerol lipase, which leads to the production of the potent endocannabinoid (eCB), 2-arachidonoyl glycerol, and thereby connects orexins with eCB signaling. In addition, OXRs have been studied in the context of neurodegeneration and cancer cell death. Overall, OXR signaling is complex, and it can change depending on the cell type and environment.
    MeSH term(s) Humans ; Orexin Receptors/metabolism ; Orexins/metabolism ; Signal Transduction/physiology
    Chemical Substances Orexin Receptors ; Orexins
    Language English
    Publishing date 2021-05-28
    Publishing country Switzerland
    Document type Journal Article ; Review
    ISSN 1662-2804 ; 1660-4431
    ISSN (online) 1662-2804
    ISSN 1660-4431
    DOI 10.1159/000514962
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  6. Article ; Online: Characterization of a putative orexin receptor in Ciona intestinalis sheds light on the evolution of the orexin/hypocretin system in chordates.

    Rinne, Maiju K / Urvas, Lauri / Mandrika, Ilona / Fridmanis, Dāvids / Riddy, Darren M / Langmead, Christopher J / Kukkonen, Jyrki P / Xhaard, Henri

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 7690

    Abstract: Tunicates are evolutionary model organisms bridging the gap between vertebrates and invertebrates. A genomic sequence in Ciona intestinalis (CiOX) shows high similarity to vertebrate orexin receptors and protostome allatotropin receptors (ATR). Here, ... ...

    Abstract Tunicates are evolutionary model organisms bridging the gap between vertebrates and invertebrates. A genomic sequence in Ciona intestinalis (CiOX) shows high similarity to vertebrate orexin receptors and protostome allatotropin receptors (ATR). Here, molecular phylogeny suggested that CiOX is divergent from ATRs and human orexin receptors (hOX
    MeSH term(s) Animals ; Humans ; Orexin Receptors/genetics ; Orexin Receptors/metabolism ; Orexins/genetics ; Orexins/metabolism ; Ciona intestinalis/genetics ; Ciona intestinalis/metabolism ; HEK293 Cells ; Signal Transduction ; Vertebrates/metabolism ; Carrier Proteins/metabolism
    Chemical Substances Orexin Receptors ; Orexins ; Carrier Proteins
    Language English
    Publishing date 2024-04-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-024-56508-1
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  7. Article ; Online: G-protein inhibition profile of the reported Gq/11 inhibitor UBO-QIC.

    Kukkonen, Jyrki P

    Biochemical and biophysical research communications

    2016  Volume 469, Issue 1, Page(s) 101–107

    Abstract: UBO-QIC (FR900359) is the only currently available Gq/11 protein inhibitor. However, its characterization has not been published, and we thus set out to do this. Gi, Gs and Gq protein-mediated responses were assessed utilizing endogenous or ... ...

    Abstract UBO-QIC (FR900359) is the only currently available Gq/11 protein inhibitor. However, its characterization has not been published, and we thus set out to do this. Gi, Gs and Gq protein-mediated responses were assessed utilizing endogenous or heterologously expressed receptors in Chinese hamster ovary cells. UBO-QIC, at 1 μM, was an effective inhibitor of the Gq-mediated responses, but was inactive at Gi- and Gs-mediated responses. Gq/11 and G16 responses were additionally compared in HEL92.1.7 cells, showing inhibition of Gq/11 responses. However, UBO-QIC also appeared to inhibit G16. Further studies are required to establish its profile with respect to the different Gq-family proteins.
    MeSH term(s) Animals ; CHO Cells ; Cricetulus ; Depsipeptides/administration & dosage ; Depsipeptides/chemistry ; Dose-Response Relationship, Drug ; GTP-Binding Protein alpha Subunits, Gq-G11/antagonists & inhibitors ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism
    Chemical Substances Depsipeptides ; FR900359 ; GTP-Binding Protein alpha Subunits, Gq-G11 (EC 3.6.5.1)
    Language English
    Publishing date 2016-01-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2015.11.078
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  8. Article ; Online: OX2 orexin/hypocretin receptor signal transduction in recombinant Chinese hamster ovary cells.

    Kukkonen, Jyrki P

    Cellular signalling

    2016  Volume 28, Issue 2, Page(s) 51–60

    Abstract: There are two subtypes of orexin receptors, OX1 and OX2. Signalling pathways have been mapped in much higher detail for OX1 receptors than OX2 receptors. Almost all the detailed studies have been performed in Chinese hamster ovary cells, and we thus ... ...

    Abstract There are two subtypes of orexin receptors, OX1 and OX2. Signalling pathways have been mapped in much higher detail for OX1 receptors than OX2 receptors. Almost all the detailed studies have been performed in Chinese hamster ovary cells, and we thus chose the same cell background for the studies on human OX2 receptors to allow comparison to human OX1 receptors. Adenylyl cyclase, phospholipase A2, C and D and diacylglycerol lipase activities were assessed by precursor radiolabelling and chromatographic separation (ion exchange, affinity or thin layer), calcium by a fluorescent method, and receptor binding with [(125)I]-orexin-A. Upon activation with orexin-A, OX2 receptors stimulated phospholipase A2, C and D, diacylglycerol lipase and calcium elevation, and both inhibited and stimulated adenylyl cyclase; i.e., the responses to OX2 activation by orexin-A were principally like those of OX1, in contrast to some previous suggestions. The responses occurred mostly in the same concentration range as those for OX1 activation and via the same signal cascades. However, some responses were weaker, suggesting a partially differential coupling to some cascades. In summary, OX2 receptor signalling is principally similar to OX1 receptor signalling suggesting also a physiologically similar coupling, though this needs to be verified in physiological contexts. Some (relatively weak) differences between the receptors may be investigated in further studies.
    MeSH term(s) Adenylyl Cyclases/metabolism ; Animals ; CHO Cells ; Calcium/metabolism ; Cricetinae ; Cricetulus ; HEK293 Cells ; Humans ; Lipoprotein Lipase/metabolism ; Orexin Receptors/genetics ; Orexin Receptors/metabolism ; Orexins/metabolism ; Phospholipase D/metabolism ; Phospholipases A2/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; Type C Phospholipases/metabolism
    Chemical Substances Orexin Receptors ; Orexins ; Recombinant Proteins ; Lipoprotein Lipase (EC 3.1.1.34) ; Phospholipases A2 (EC 3.1.1.4) ; Type C Phospholipases (EC 3.1.4.-) ; Phospholipase D (EC 3.1.4.4) ; Adenylyl Cyclases (EC 4.6.1.1) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2016-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1002702-6
    ISSN 1873-3913 ; 0898-6568
    ISSN (online) 1873-3913
    ISSN 0898-6568
    DOI 10.1016/j.cellsig.2015.11.009
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    Zs.A 2579: Show issues Location:
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  9. Article ; Online: G-protein-dependency of orexin/hypocretin receptor signalling in recombinant Chinese hamster ovary cells.

    Kukkonen, Jyrki P

    Biochemical and biophysical research communications

    2016  Volume 476, Issue 4, Page(s) 379–385

    Abstract: Multiple signalling pathways for orexin receptors have been discovered, and most thoroughly mapped in Chinese hamster ovary K1 (CHO-K1) cells. It is also known that orexin receptors can couple to the G-protein families Gi, Gs and Gq. However, the ... ...

    Abstract Multiple signalling pathways for orexin receptors have been discovered, and most thoroughly mapped in Chinese hamster ovary K1 (CHO-K1) cells. It is also known that orexin receptors can couple to the G-protein families Gi, Gs and Gq. However, the connection between the G-proteins and the downstream signals is only vaguely established, and we now set out to resolve this for human orexin receptors expressed in CHO-K1 cells. Adenylyl cyclase (AC), phospholipase A2, C and D, and diacylglycerol lipase activities were assessed by precursor radiolabelling and chromatographic separation, and calcium by fluorescent methods. Pertussis toxin, cholera toxin and the cyclic depsipeptide, UBO-QIC a.k.a. FR900359, were used to assess the involvement of Gi-, Gs- and Gq-family G-proteins, respectively. Calcium elevations as well as activation of the phospholipases and diacylglycerol lipase were dependent on Gq, as they were fully blocked by UBO-QIC. The low-potency AC activation fully depended on Gs. Surprisingly, the assumed Gi-dependent inhibition of AC was (fully or partially) inhibited by UBO-QIC, in opposition to the previous findings of no sensitivity of Gi proteins to UBO-QIC. Orexin receptor signalling is indeed mostly Gq-driven in CHO-K1 cells, even with respect to the less clearly mapped cascades such as phospholipase A2 and C and calcium influx, underlining the importance of Gq even under physiological conditions. AC regulation warrants more studies.
    MeSH term(s) Adenylyl Cyclases/metabolism ; Animals ; CHO Cells/drug effects ; CHO Cells/metabolism ; Calcium/metabolism ; Cholera Toxin/pharmacology ; Cricetulus ; Depsipeptides/pharmacology ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism ; GTP-Binding Proteins/metabolism ; Lipoprotein Lipase/metabolism ; Orexin Receptors/genetics ; Orexin Receptors/metabolism ; Pertussis Toxin/pharmacology ; Phospholipases/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Signal Transduction
    Chemical Substances Depsipeptides ; FR900359 ; HCRTR1 protein, human ; HCRTR2 protein, human ; Orexin Receptors ; Recombinant Proteins ; Cholera Toxin (9012-63-9) ; Pertussis Toxin (EC 2.4.2.31) ; Phospholipases (EC 3.1.-) ; Lipoprotein Lipase (EC 3.1.1.34) ; GTP-Binding Proteins (EC 3.6.1.-) ; GTP-Binding Protein alpha Subunits, Gq-G11 (EC 3.6.5.1) ; Adenylyl Cyclases (EC 4.6.1.1) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2016--05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2016.05.130
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
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  10. Article ; Online: Lipid signaling cascades of orexin/hypocretin receptors.

    Kukkonen, Jyrki P

    Biochimie

    2014  Volume 96, Page(s) 158–165

    Abstract: Orexins - orexin-A and orexin-B - are neuropeptides with significant role in regulation of fundamental physiological processes such as sleep-wakefulness cycle. Orexins act via G-protein-coupled OX1 and OX2 receptors, which are found, in addition to the ... ...

    Abstract Orexins - orexin-A and orexin-B - are neuropeptides with significant role in regulation of fundamental physiological processes such as sleep-wakefulness cycle. Orexins act via G-protein-coupled OX1 and OX2 receptors, which are found, in addition to the central nervous system, also in a number of peripheral organs. Orexin receptors show high degree of signaling promiscuity. One particularly prominent way of signaling for these receptors is via phospholipase cascades, including the phospholipase C, phospholipase D and phospholipase A2 cascades, and also diacylglycerol lipase and phosphoinositide-3-kinase pathways. Most analyses have been performed in recombinant cells; there are indications of some of these cascades in native cells while the significance of other cascades remains to be shown. In this review, I present these pathways, their activation mechanisms and their physiological significance.
    MeSH term(s) Animals ; Calcium Signaling ; Endocannabinoids/physiology ; Humans ; Lipid Metabolism ; Orexin Receptors/physiology ; Phosphatidylinositol 3-Kinases/metabolism ; Phospholipases/metabolism
    Chemical Substances Endocannabinoids ; Orexin Receptors ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Phospholipases (EC 3.1.-)
    Language English
    Publishing date 2014-01
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 120345-9
    ISSN 1638-6183 ; 0300-9084
    ISSN (online) 1638-6183
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2013.06.015
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