161 research outputs found
Kohdekuvaus: MOR-Y13-120: Torvinen (Sodankylä). Liite julkaisuun Valtakunnallisesti arvokkaat moreenimuodostumat. Suomen ympäristö 14/2007
No full textTorvinen Sodankylä
Tietokantatunnus: MOR-Y13-120
Muodostumatyyppi: Drumliini
Arvoluokka: 3
Karttalehti: 3624.09
Alueen pinta-ala: 47,5 ha
Korkeus: 230 m mpy.
Alueen suhteellinen korkeus: 23 m
Muodon suhteellinen korkeus: 23 m
Moreenimuodostuman sijainti: Torvisen drumliini sijaitsee Sodankylän eteläosassa, Torvisen kylässä, noin 26 km Sodankylästä etelää
Adenosine receptor/dopamine receptor interactions : molecular and biochemical aspects
No full textThe dopamine receptors have been shown to be involved in a variety of higher brain functions, such as motor control, cognition and affective states. Agonist and antagonists of dopamine receptors are widely used to treat disorders such as Parkinson's disease and schizophrenia, respectively. Adenosine is a well-established neuromodulator in the central nervous system, generally having an inhibitory effect on neural activity, and mediates its effects via adenosine receptors that are widely distributed in the central nervous system. Results from previous studies at all levels from behaviour to biochemical radioligand binding experiments show an antagonistic interaction between adenosine and dopamine receptors. Increasing evidence suggests that antagonistic interactions between specific subtypes of adenosine and dopamine receptors in the basal ganglia are involved in the motor depressant effects of adenosine receptor agonists and the motor stimulant effects of adenosine receptor antagonists, such as caffeine.The aim of the present studies was to analyse the mechanistic aspects involved in the adenosine A1/dopamine D1 and adenosine A2A/dopamine D2 intramembrane receptor-receptor interactions at the cellular and molecular level. The results from studies with the A1/D1 cell line demonstrated an antagonistic interaction between adenosine A1/dopamine D1 receptors, both at the level of receptor binding and second messengers. Adenosine deaminase (ADA), an enzyme for breaking down adenosine, has recently been shown to be crucial for the high affinity binding state of A, receptors. The results from the present experiments showed that the presence of a structurally intact ADA is important in the A1-D1 interaction, probably by providing the high-affinity state of the A, receptor.Both A1/D1 and A2A/D2 receptors (but neither A1/D2 nor A2A/D1 receptors)-, were found to coimmunoprecipitate in membrane preparations from cotransfected cell lines, which indicate that A1/D1 and A2A/D2 receptors exist as heteromeric complexes. Moreover, double immunofluorescence experiments with confocal laser microscopy showed a high degree of colocalization between both A1/D1 and A2A/D2 receptors in cell lines and primary cultures. Treatment with adenosine and/or dopamine agonists affected the trafficking of both adenosine and dopamine receptors giving further evidence of functional heteromeric A1/D1 and A2A/D2 complexes. A 3 hour treatment with the D2 agonist induced coaggregation of the A2A and the D2 receptors followed by cointernalization of the two receptors after 15 hours, returning to the baseline level after 24 hours.A high homology between dopamine D2 and D3 receptors has been shown, and therefore the possible interactions between adenosine A2A receptors and dopamine D3 receptors were studied in an A2A/D3 cell line. The results from binding experiments showed that adenosine A2A and dopamine D3 receptors seem to interact like A2A and D2 receptors at the recognition level, and therefore also A2A/D3 heteromers may exist.Taken together, the present results give a molecular basis for subtype specific antagonistic adenosine-dopamine receptor interactions involving A1/D1 A2A/D2 and possible A2A/D3 heteromerizations, having implications for treatment of Parkinson's disease and schizophrenia.List of scientific papersI. Ferre S, Torvinen M, Antoniou K, Irenius E, Civelli O, Arenas E, Fredholm BB, Fuxe K (1998). Adenosine A1 receptor-mediated modulation of dopamine D1 receptors in stably cotransfected fibroblast cells. J Biol Chem. 273(8): 4718-24. https://pubmed.ncbi.nlm.nih.gov/9468534II. Gines S, Hillion J, Torvinen M, Le Crom S, Casado V, Canela EI, Rondin S, Lew JY, Watson S, Zoli M, Agnati LF, Verniera P, Lluis C, Ferre S, Fuxe K, Franco R (2000). Dopamine D1 and adenosine A1 receptors form functionally interacting heteromeric complexes. Proc Natl Acad Sci U S A. 97(15): 8606-11. https://pubmed.ncbi.nlm.nih.gov/10890919III. Torvinen M, Gines S, Hillion J, Latini S, Canals M, Ciruela F, Bordoni F, Staines W, Pedata F, Agnati LF, Lluis C, Franco R, Ferre S, Fuxe K (2002). Interactions among adenosine deaminase, adenosine A(1) receptors and dopamine D(1) receptors in stably cotransfected fibroblast cells and neurons. Neuroscience. 113(3): 709-19. https://pubmed.ncbi.nlm.nih.gov/12150791IV. Hillion J, Canals M, Torvinen M, Casado V, Scott R, Terasmaa A, Hansson A, Watson S, Olah ME, Mallol J, Canela EI, Zoli M, Agnati LF, Ibanez CF, Lluis C, Franco R, Ferre S, Fuxe K (2002). Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors. J Biol Chem. 277(20): 18091-7. https://pubmed.ncbi.nlm.nih.gov/11872740V. Torvinen M, Torri C, Tombesi A, Watson S, Franco R, Fuxe K, Agnati L (2002). Agonist and antagonist regulation of adenosine A2A and dopamine D2 receptor cotrafficking. [Manuscript]VI. Torvinen M, Kozell L, Neve K, Ibanez C, Fuxe K (2002). Intarmembrane interactions between adenosine A2A and dopamine D3 receptors and adenosine A2a/chimeric D2/D1 receptors. A biochemical binding study. [Manuscript]</p
Noncovalent complexation of glucosylthioureidocalix[4]arenes with carboxylates and their gas-phase characteristics – An ESI-FTICR mass spectrometric study
No full textThe noncovalent complexation of three glucosylcalix[4]arenes (1-3) towards 23 mono- and dicarboxylic acid anions were studied by ESI-FTICR mass spectrometry. Competitive complexation, collision-induced dissociation and gas-phase H/D-exchange experiments were performed to obtain information on selectivity of calixarenes towards carboxylates and characteristics of their complexes. The flexibility and number of glucose units of the host and the spatial disposition of the hydrogen bonding groups on the carboxylate guests were found to affect the selectivity of complexation strongly. The glucosylcalixarenes exhibited particular selectivity for dicarboxylic acid anions incorporating π-systems, and clear isomeric selectivity was observed for isophthalic among phthalic acid anions and for fumaric acid over maleic acid anio
Mielenterveyshäiriöt ensiaputilanteessa : Opas SPR Rovaniemen osaston ensiapuryhmälle
No full textRovaniemen ammattikorkeakoulu
Terveys- ja liikunta-ala
Hoitotyön koulutusohjelma; sairaanhoitaja
Tekijä: Sanna Torvinen Vuosi 2010
Toimeksiantaja: Suomen Punainen Risti, Rovaniemen osasto
Työn nimi: Mielenterveyshäiriöt ensiaputilanteessa
Sivu- ja liitemäärä: 31 + 1 (opas)
Opinnäytetyöni tehtävänä oli tehdä opas mielenterveyshäiriöistä ja ensiavusta Suomen Punaisen Ristin Rovaniemen osastolle, kohderyhmänä ensiapuryhmä. Oppaan tarkoituksena oli antaa hyödyllistä lisätietoa ensiapuryhmälle muiden koulutusten lisäksi.
Opinnäytetyö koostuu kirjallisesta raportista ja oppaasta. Raportti käsittelee työn taustaa, oppaan suunnittelua ja toteutusta, lisäksi siinä käsitellään teoreettisena viitekehyksenä mielenterveyttä, yleisiä mielenterveyshäiriöitä sekä ensiaputilannetta, jossa autettavalla on mielenterveyshäiriö. Lähdemateriaalina on käytetty pääasiassa lääketieteen ja hoitotyön oppikirjoja, artikkeleita ja julkaisuja.
Oppaassa kerrotaan yleisesti mielenterveydestä ja mielenterveyshäiriöstä, minkä jälkeen käydään läpi yleisiä mielenterveyshäiriöitä eli masennustila, kaksisuuntainen mielialahäiriö, ahdistuneisuushäiriöt sekä psykoosit. Lisäksi oppaassa kerrotaan mielenterveyshäiriöstä kärsivän auttamisesta ensiaputilanteessa ja itsetuhoisen ja aggressiivisen ihmisen kohtaamisesta.
Oppaan tavoitteena oli lisätä ensiapuryhmän tietoutta mielenterveyshäiriöstä ja häiriöstä kärsivän auttamisesta ensiaputilanteessa. Tavoitteena oli tiedon lisäämisen kautta mahdollisesti helpottaa mielenterveyshäiriöistä kärsivän kohtaamista.Rovaniemi University of Applied Sciences
School of Healthcare and Sports
Degree Proramme in Nursing and Health Care
Author: Sanna Torvinen Year 2010
Commissioned by: The Finnish Red Cross, Rovaniemi Branch
Subject of thesis: Mental Health Disorders in Emergency Situations
Number of pages:31 + 1 (guide)
The purpose of my thesis was to make a guide on mental health disorders and first aid to the Finnish Red Cross, Rovaniemi branch. The target group for the guide was a first aid team. The goal of the guide was to give useful information for the first aid team and to complement their training.
The thesis consists of a report and a guide. The report deals with the background of the thesis, designing and implementing the guide. In addition, the theoretical framework consists of the topics of mental health, the most com-mon mental health disorders and emergency situations that involve people with mental health disorders. The source of information for the thesis include medical and nursing textbooks, articles and publications.
The guide is mainly about mental health and mental disorders. It goes through general mental health disorders i.e. depression, bipolar disorder, anxiety and psychosis. The guide also includes information about helping a person who has a mental health disorder and about facing a suicidal or an aggressive person.
The aim of the guide was to increase knowledge about mental health disor-ders and to help the first aid team to encounter people who suffer from them
Noncovalent Complexation of Monoamine Neurotransmitters and Related Ammonium Ions by Tetramethoxy-Tetraglucosylcalix[4]arene
No full textThe noncovalent complexation of monoamine neurotransmitters and related ammonium and quaternary ammonium ions by a conformationally flexible tetramethoxy glucosylcalix[4]arene was studied by electrospray ionization Fourier transform ion cyclotron resonance (ESI-FTICR) mass spectrometry. The glucosylcalixarene exhibited highest binding affinity towards serotonin, norepinephrine, epinephrine, and dopamine. Structural properties of the guests, such as the number, location, and type of hydrogen bonding groups, length of the alkyl spacer between the ammonium head-group and the aromatic ring structure, and the degree of nitrogen substitution affected the complexation. Competition experiments and guest-exchange reactions indicated that the hydroxyl groups of guests participate in intermolecular hydrogen bonding with the glucocalixarene
Fluorescence in situ hybridization using peptide nucleic acid probes for rapid detection of Mycobacterium avium subsp. avium and Mycobacterium avium subsp. paratuberculosis in potable-water biofilms
No full textHere, we present for the first time a high-affinity peptide nucleic acid (PNA) oligonucleotide sequence for detecting Mycobacterium avium bacteria, including the opportunistically pathogenic subspecies M. avium subsp. avium, M. avium subsp. paratuberculosis, and M. avium subsp. silvaticum, by the fluorescence in situ hybridization (FISH) method. There is evidence that M. avium subsp. avium especially is able to survive and grow in drinking-water biofilms and possibly transmit via drinking water. The designed PNA probe (MAV148) specificity was tested with several bacterial species, including other mycobacteria and mycolic acid-containing bacteria. From the range of bacterial strains tested, only M. avium subsp. avium and M. avium subsp. paratuberculosis strains were hybridized. The PNA FISH method was applied successfully to detect M. avium subsp. avium spiked in water samples and biofilm established within a Propella biofilm reactor fed with potable water from a distribution supply
Computer-assisted image analysis of Caveolin-1 involvement in the iternalization process of adenosine A2A-dopamine D2 Receptor heterodimers
No full textA functional aspect of horizontal molecular networks has been investigated experimentally, namely the heteromerization between adenosine A(2A) and doparnine D-2 receptors and the possible role of caveolin-1 in the cotrafficking of these molecular complexes. This study has been carried out by means of computer-assisted image analysis procedure of laser images of membrane immunoreactivity of caveolin-1, A(2A), D-1, and D-2 receptors obtained in two clones of Chinese hamster ovary cells-one transfected with A(2A) and dopamine D, receptors and the other one with A(2A) and D-2 receptors. Cells were treated for 3 h with 10 mu M D-1 receptor agonist SKF 38393,50 mu M D-2-D-3 receptor agonist quinpirole, and 200 nM A(2A) receptor agonist CGS 21680. In A(2A)-D-1-cotransfected cells, caveolin-1 was found to colocalize with both A2A and D, receptors and treatment with SKF 38393 induced internalization of caveolin-1 and D-1 receptors, with a preferential internalization of D, receptors colocalized. with caveolin-1. In A(2A)-D-2-cotransfected cells, caveolin-1 was found to colocalize with both A2A and D2 receptors and either CGS 21680 or quinpirole treatment induced internalization of caveolin-1 and A2A and D2 receptors, with a preferential internalization of A2A and D2 receptors colocalized with caveolin-1. The results suggest that A2A and D2 receptors and caveolin-1 likely interact forming a macrocomplex that internalizes upon agonist treatment. These observations are discussed in the frame of receptor oligomerization and of the possible functional role of caveolin-1 in the process of co-internalization and, hence, in controlling the permanence of receptors at the plasma membrane level (prerequisite for receptor mosaic organization and plastic adjustments) and in the control of receptor desensitization
Adenosine A(2A) receptor and dopamine D-3 receptor interactions: Evidence of functional A(2A)/D-3 heteromeric complexes
No full textAdenosine A(2A) and dopamine D-2 receptors have been shown previously to form heteromeric complexes and interact at the level of agonist binding, G protein coupling, and trafficking. Because dopamine D-2 and D-3 receptors show a high degree of sequence homology, A(2A) and D-3 receptors may also interact in a similar manner. The present studies with confocal microscopy showed that A(2A)-yellow fluorescent protein (YFP) and D-3-green fluorescent protein 2 (GFP2) receptors colocalize in the plasma membrane. Furthermore, fluorescence resonance energy transfer (FRET) analysis demonstrated that A(2A)-YFP and D-3-GFP2 receptors give a positive FRET efficiency and are thereby likely to exist as heteromeric A(2A)/D-3 receptor complexes. Saturation experiments with [H-3] dopamine demonstrated that the A(2A) receptor agonist 4-[2-[[6-amino-9(N-ethyl-beta-D-ribofuranuronaminoamidosyl)-9H-purin-2-yl]amino]ethyl]benzenepropanoic acid (CGS-21680) reduced the affinity of the high-affinity agonist binding state of the D-3 receptor for [H-3] dopamine. The A(2A) and D-3 receptors seem to interact also at the level of G protein coupling, because the adenosine A(2A) receptor agonist CGS-21680 fully counteracted the D-3 receptor-mediated inhibition of a forskolin-mediated increase in cAMP levels. Taken together, when coexpressed in the same neuron, A(2A) and D-3 receptors seem to form A(2A)/D-3 heteromeric receptor complexes in which A(2A) receptors antagonistically modulate both the affinity and the signaling of the D-3 receptors. D-3 receptor is one of the therapeutic targets for treatment of schizophrenia, and therefore, the A(2A)/D-3 receptor interactions could provide an alternative antischizophrenic treatment
Large glucosylthioureidocalixarenes: selective hosts for mono- and bisphosphonates
No full textNon-covalent complexation of mono- and bisphosphonates by hexaglucosylthioureidocalix[6]arene and octaglucosylthioureidocalix[
8]arene was studied by electrospray ionisation Fourier transform ion cyclotron resonance mass spectrometry.
Glucosylthioureidocalix[8]arene formed 1:1 and 1:2 complexes with bisphosphonates, with a marked preference towards
risedronate, clodronate, zoledronate and etidronate. In contrast, up to four guest molecules were bound in the case of
monophosphonates, suggesting a different type of binding in comparison to bisphosphonates. Hexaglucosylthioureidocalix[
6]arene also formed complexes with phosphonates with a somewhat similar binding selectivity. Interestingly, the
addition of calcium ions into the sample of etidronate–glucosylthioureidocalix[8]arene complex resulted in a complete
release of the guest due to the very high affinity between calcium and bisphosphonate. In the gas-phase hydrogen/deuterium
exchange reactions, glucosylthioureidocalix[8]arene exhibited a number of exchangeable hydrogens and a bimodal
exchange distribution was observed, suggesting a presence of multiple gas-phase conformations. Surprisingly, no exchange
or very slow exchange for the complexes of glucosylthioureidocalix[8]arene was observed
Biochemical identification of the dopamine D2 receptor domains interacting with the adenosine A2A receptor
No full textFunctional interactions between adenosine A2A and dopamine D2 receptors have been demonstrated both at the D2 agonist-binding and second messenger levels. The present studies use a [3H]dopamine-binding assay as a sensitive measure of A2A receptor-mediated modulation of D2 receptors. Co-incubation with an A2A receptor agonist increased the Kd value of high-affinity [3H]dopamine-binding sites of the D2 receptor without changing their Bmax values in a cotransfected cell line. This interaction was shown to be subtype specific, as the A2A receptor agonist did not modulate the affinity of the D1 receptor for [3H]dopamine. The domains of the D2 receptor important for the A2A/D2 receptor interaction were studied with chimeric dopamine D2/D1 receptors. The results showed that the A2A receptor agonist still strongly reduced the affinity of a D2/D1 chimera with the sixth transmembrane (TM) domain and third extracellular loop from the D1 receptor. However, the A2A receptor agonist was not able to modulate a D2/D1 chimeric receptor containing the fifth and sixth TM domains and the third intracellular and extracellular loops from the D1 receptor, indicating that the fifth TM domain and/or the third intracellular loop may be involved in the interaction between A2A and D2 receptors
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