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Book ; Thesis: Rolle und Regulation von Calcium-permeablen Kationenkanälen der TRP Familie in neutrophilen Granulozyten

Heiner, Inka

(Berichte aus der Biologie)

2003

Title variant	Kationenkanäle der TRP Familie in neutrophilen Granulozyten
Author's details	Inka Heiner
Series title	Berichte aus der Biologie
Keywords	Calciumkanal ; Neutrophiler Granulozyt ; Kation
Language	German
Size	V, 93 S, Ill., graph. Darst, 21 c,
Publishing place	Aachen: Shaker
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Techn. Hochsch., Diss.--Aachen, 2003
ISBN	3832217983 ; 9783832217983
Database	Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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Book ; Online ; Thesis: Rolle und Regulation von Calcium-permeablen Kationenkanälen der TRP Familie in neutrophilen Granulozyten

Heiner, Inka [Verfasser]

2003

Author's details	Inka Heiner
Keywords	Pflanzen (Botanik) ; Plants (Botany)
Subject code	sg580
Language	German
Publisher	Shaker
Publishing place	Aachen
Document type	Book ; Online ; Thesis
ISBN	978-3-8322-1798-3 ; 3-8322-1798-3
Database	Digital theses on the web

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Article: TRPM2: a calcium influx pathway regulated by oxidative stress and the novel second messenger ADP-ribose.

Kühn, Frank J P / Heiner, Inka / Lückhoff, Andreas

Pflugers Archiv : European journal of physiology

2005 Volume 451, Issue 1, Page(s) 212–219

Abstract: A unique functional property within the transient receptor potential (TRP) family of cation channels is the gating of TRP (melastatin) 2 (TRPM2) channels by ADP-ribose (ADPR). ADPR binds to the intracellular C-terminal tail of TRPM2, a domain that shows ... ...

Abstract	A unique functional property within the transient receptor potential (TRP) family of cation channels is the gating of TRP (melastatin) 2 (TRPM2) channels by ADP-ribose (ADPR). ADPR binds to the intracellular C-terminal tail of TRPM2, a domain that shows homology to enzymes with pyrophosphatase activity. Cytosolic Ca(2+) enhances TRPM2 gating by ADPR; ADPR and Ca(2+) in concert may be an important messenger system mediating Ca(2+) influx. Other stimuli of TRPM2 include NAD and H(2)O(2) and cyclic ADPR, which may act synergistically with ADPR. H(2)O(2), an experimental paradigm of oxidative stress, may also induce the formation of ADPR in the nucleus or mitochondria. In this review, we summarize the gating properties of TRPM2 and the proposed pathways of channel activation in vivo. TRPM2 is likely to be a key player in several signalling pathways, mediating cell death in response to oxidative stress or in reperfusion injury. Moreover, it plays a decisive role in experimentally induced diabetes mellitus and in the activation of leukocytes.
MeSH term(s)	Adenosine Diphosphate Ribose/physiology ; Animals ; Calcium/metabolism ; Cyclic ADP-Ribose/physiology ; Drug Synergism ; Humans ; Hydrogen Peroxide/pharmacology ; Oxidative Stress/physiology ; Poly(ADP-ribose) Polymerases/physiology ; Second Messenger Systems/physiology ; TRPM Cation Channels/chemistry ; TRPM Cation Channels/drug effects ; TRPM Cation Channels/genetics ; TRPM Cation Channels/physiology
Chemical Substances	TRPM Cation Channels ; TRPM2 protein, human ; Cyclic ADP-Ribose (119340-53-3) ; Adenosine Diphosphate Ribose (20762-30-5) ; Hydrogen Peroxide (BBX060AN9V) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2005-10
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s00424-005-1446-y
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Article: Role and regulation of TRP channels in neutrophil granulocytes.

Heiner, Inka / Eisfeld, Jörg / Lückhoff, Andreas

Cell calcium

2003 Volume 33, Issue 5-6, Page(s) 533–540

Abstract: Members of the transient receptor potential (TRP) family for which mRNA can be demonstrated in neutrophil granulocytes with RT-PCR include TRPC6 (as only "short" TRP), TRPM2, TRPV1, TRPV2, TRPV5 and TRPV6. When these are analyzed in heterologous ... ...

Abstract	Members of the transient receptor potential (TRP) family for which mRNA can be demonstrated in neutrophil granulocytes with RT-PCR include TRPC6 (as only "short" TRP), TRPM2, TRPV1, TRPV2, TRPV5 and TRPV6. When these are analyzed in heterologous overexpression experiments, TRPM2 is the only cation channel with characteristic properties that can be used as fingerprint to provide functional evidence for its expression in neutrophil granulocytes. As cells transfected with TRPM2, neutrophil granulocytes display non-selective cation currents and typical channel activity evoked by intracellular ADP-ribose and NAD. Thus, stimulation of TRPM2 is likely to occur after activation of CD38 (producing ADP-ribose) and during the oxidative burst (enhancing the NAD concentration). This novel mode of cation entry regulation may be of particular importance for the response of granulocytes to chemoattractants. TRPV6 is a likely but not exclusive candidate as subunit of the channels mediating store-operated Ca2+ entry (SOCE). Evidence for SOCE in granulocytes has been presented with the fura-2 technique but not with electrophysiological methods although Ca2+-selective store-operated currents can be demonstrated in HL-60 cells, a cell culture model of neutrophil granulocytes.
MeSH term(s)	Adenosine Diphosphate Ribose/pharmacology ; Animals ; Calcium Channels/metabolism ; Granulocytes/drug effects ; Granulocytes/metabolism ; Humans ; Hydrogen Peroxide/pharmacology ; NAD/pharmacology ; Neutrophils/drug effects ; Neutrophils/metabolism ; Oxidants/pharmacology ; Signal Transduction ; TRPC Cation Channels
Chemical Substances	Calcium Channels ; Oxidants ; TRPC Cation Channels ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2003-07-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/s0143-4160(03)00058-7
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Article: Regulation of TRPM2 channels in neutrophil granulocytes by ADP-ribose: a promising pharmacological target.

Heiner, Inka / Radukina, Natalia / Eisfeld, Jörg / Kühn, Frank / Lückhoff, Andreas

Naunyn-Schmiedeberg's archives of pharmacology

2005 Volume 371, Issue 4, Page(s) 325–333

Abstract: TRPM2 channels play an important role in the activation process of neutrophil granulocytes. One mechanism of TRPM2 channel gating is the binding of intracellular ADP ribose (ADPR) to the Nudix box domain in the C-terminal tail of TRPM2. Intracellular Ca( ... ...

Abstract	TRPM2 channels play an important role in the activation process of neutrophil granulocytes. One mechanism of TRPM2 channel gating is the binding of intracellular ADP ribose (ADPR) to the Nudix box domain in the C-terminal tail of TRPM2. Intracellular Ca(2+), although not an activator of TRPM2 by its own, significantly enhances TRPM2 gating by ADPR. Stimulation of neutrophil granulocytes with the chemoattractant peptide N-formyl-methionyl-leucyl-phenylalanine (fMLP) induces release of Ca(2+) ions from intracellular stores which in cooperation with endogenous ADPR levels enable Ca(2+) influx through TRPM2. Stimulation of the ectoenzyme CD38, a membrane-associated glycohydrolase with ADPR as main product, and uptake of ADPR into the cell may contribute to the effects of fMLP. Inhibition of ADPR production, of uptake and of binding to TRPM2 are all potential pharmacological principles by which a modulation of neutrophil function may become possible in future.
MeSH term(s)	Adenosine Diphosphate Ribose/metabolism ; Animals ; Calcium/metabolism ; Chemotaxis, Leukocyte/drug effects ; Humans ; Neutrophil Activation/drug effects ; Neutrophils/enzymology ; Neutrophils/metabolism ; Protein Binding ; TRPM Cation Channels/antagonists & inhibitors
Chemical Substances	TRPM Cation Channels ; TRPM2 protein, human ; Adenosine Diphosphate Ribose (20762-30-5) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2005-04
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	121471-8
ISSN	1432-1912 ; 0028-1298
ISSN (online)	1432-1912
ISSN	0028-1298
DOI	10.1007/s00210-005-1033-y
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Article ; Online: Endogenous ADP-ribose enables calcium-regulated cation currents through TRPM2 channels in neutrophil granulocytes.

Heiner, Inka / Eisfeld, Jörg / Warnstedt, Maike / Radukina, Natalia / Jüngling, Eberhard / Lückhoff, Andreas

The Biochemical journal

2006 Volume 398, Issue 2, Page(s) 225–232

Abstract: TRPM2 (transient receptor potential melastatin 2) is a Ca2+-permeable cation channel gated by ADPR (ADP-ribose) from the cytosolic side. To test whether endogenous concentrations of intracellular ADPR are sufficient for TRPM2 gating in neutrophil ... ...

Abstract	TRPM2 (transient receptor potential melastatin 2) is a Ca2+-permeable cation channel gated by ADPR (ADP-ribose) from the cytosolic side. To test whether endogenous concentrations of intracellular ADPR are sufficient for TRPM2 gating in neutrophil granulocytes, we devised an HPLC method to determine ADPR contents in HClO4 cell extracts. The reversed-phase ion-pair HPLC method with an Mg2+-containing isocratic eluent allows baseline resolution of one ADPR peak. Intracellular ADPR concentrations were approx. 5 muM in granulocytes and not significantly altered by stimulation with the chemoattractant peptide fMLP (N-formylmethionyl-leucylphenylalanine). We furthermore determined intracellular concentrations of cADPR (cyclic ADPR) with a cyclase assay involving enzymatic conversion of cADPR into NAD+ and fluorimetric determination of NAD+. Intracellular cADPR concentrations were approx. 0.2 microM and not altered by fMLP. In patch-clamp experiments, ADPR (0.1-100 microM) was dialysed into granulocytes to analyse its effects on whole-cell currents characteristic for TRPM2, in the presence of a low (<10 nM) or a high (1 microM) intracellular Ca2+ concentration. TRPM2 currents were significantly larger at high than at low [Ca2+] (e.g. -225+/-27.1 versus -7+/-2.0 pA/pF at 5 muM ADPR), but no currents at all were observed in the absence of ADPR (ADPR concentration < or =0.3 microM). cADPR (0.1, 0.3 and 10 microM) was without effect even in the presence of subthreshold ADPR (0.1 microM). We conclude that ADPR enables an effective regulation of TRPM2 by cytosolic Ca2+. Thus ADPR and Ca2+ in concert behave as a messenger system for agonist-induced influx of Ca2+ through TRPM2 in granulocytes.
MeSH term(s)	Adenosine Diphosphate Ribose/metabolism ; Adenosine Diphosphate Ribose/pharmacology ; Calcium/chemistry ; Calcium/metabolism ; Cations, Divalent/chemistry ; Electrophysiology ; Humans ; Intracellular Membranes/chemistry ; Intracellular Membranes/drug effects ; Intracellular Membranes/metabolism ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/chemistry ; Neutrophils/drug effects ; Neutrophils/metabolism ; Patch-Clamp Techniques ; TRPM Cation Channels/metabolism
Chemical Substances	Cations, Divalent ; TRPM Cation Channels ; TRPM2 protein, human ; Adenosine Diphosphate Ribose (20762-30-5) ; N-Formylmethionine Leucyl-Phenylalanine (59880-97-6) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2006-09-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20060183
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Article: Activation of the cation channel long transient receptor potential channel 2 (LTRPC2) by hydrogen peroxide. A splice variant reveals a mode of activation independent of ADP-ribose.

Wehage, Edith / Eisfeld, Jörg / Heiner, Inka / Jüngling, Eberhard / Zitt, Christof / Lückhoff, Andreas

The Journal of biological chemistry

2002 Volume 277, Issue 26, Page(s) 23150–23156

Abstract: LTRPC2 is a cation channel recently reported to be activated by adenosine diphosphate-ribose (ADP-ribose) and NAD. Since ADP-ribose can be formed from NAD and NAD is elevated during oxidative stress, we studied whole cell currents and increases in the ... ...

Abstract	LTRPC2 is a cation channel recently reported to be activated by adenosine diphosphate-ribose (ADP-ribose) and NAD. Since ADP-ribose can be formed from NAD and NAD is elevated during oxidative stress, we studied whole cell currents and increases in the intercellular free calcium concentration ([Ca(2+)](i)) in long transient receptor potential channel 2 (LTRPC2)-transfected HEK 293 cells after stimulation with hydrogen peroxide (H(2)O(2)). Cation currents carried by monovalent cations and Ca(2+) were induced by H(2)O(2) (5 mm in the bath solution) as well as by intracellular ADP-ribose (0.3 mm in the pipette solution) but not by NAD (1 mm). H(2)O(2)-induced currents developed slowly after a characteristic delay of 3-6 min and receded after wash-out of H(2)O(2). [Ca(2+)](i) was rapidly increased by H(2)O(2) in LTRPC2-transfected cells as well as in control cells; however, in LTRPC2-transfected cells, H(2)O(2) evoked a second delayed rise in [Ca(2+)](i). A splice variant of LTRPC2 with a deletion in the C terminus (amino acids 1292-1325) was identified in neutrophil granulocytes. This variant was stimulated by H(2)O(2) as the wild type. However, it did not respond to ADP-ribose. We conclude that activation of LTRPC2 by H(2)O(2) is independent of ADP-ribose and that LTRPC2 may mediate the influx of Na(+) and Ca(2+) during oxidative stress, such as the respiratory burst in granulocytes.
MeSH term(s)	Adenosine Diphosphate Ribose/physiology ; Adult ; Base Sequence ; Calcium/metabolism ; Calcium Channels/drug effects ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Cloning, Molecular ; Humans ; Hydrogen Peroxide/pharmacology ; Ion Channels ; Membrane Proteins ; Molecular Sequence Data ; NAD/pharmacology ; Oxidative Stress ; TRPM Cation Channels
Chemical Substances	Calcium Channels ; Ion Channels ; Membrane Proteins ; TRPM Cation Channels ; TRPM2 protein, human ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; Hydrogen Peroxide (BBX060AN9V) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2002-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112096200
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Article: Candidate gene association study of type 2 diabetes in a nested case-control study of the EPIC-Potsdam cohort - role of fat assimilation.

Fisher, Eva / Nitz, Inke / Lindner, Inka / Rubin, Diana / Boeing, Heiner / Möhlig, Matthias / Hampe, Jochen / Schreiber, Stefan / Schrezenmeir, Jürgen / Döring, Frank

Molecular nutrition & food research

2007 Volume 51, Issue 2, Page(s) 185–191

Abstract: To search for common variants etiological for type 2 diabetes, we screened 15 genes involved in fat assimilation for sequence variants. Approximately 55 kb in promoter and coding regions, and intron/splice sites were sequenced by cycle sequencing. In the ...

Abstract	To search for common variants etiological for type 2 diabetes, we screened 15 genes involved in fat assimilation for sequence variants. Approximately 55 kb in promoter and coding regions, and intron/splice sites were sequenced by cycle sequencing. In the set of 15 genes, 71 single nucleotide polymorphisms (SNPs) were detected. 33 SNPs were presumed to be functionally significant and were genotyped in 192 incident type 2 diabetes subjects and 384 matched controls from the European Prospective Investigation into Cancer and Nutrition-Potsdam cohort. A total of 27 SNPs out of 15 genes showed no statistical association with type 2 diabetes in our study. Six SNPs demonstrated nominal association with type 2 diabetes, with the most significant marker (FABP6 Thr79Met) having an adjusted odds ratio of 0.45 (95% CI 0.22-0.92) in homozygous Met allele carriers. Evidence for an association with disease status was also found for a novel Arg109Cys (g.2129C > T) variant of colipase, 5'UTR (rs2084202) and Met71Val (rs8192506) variants of diazepam-binding inhibitor, Arg298His (rs13283456) of PTGES2, and a novel promoter variant (g.-1324G > A) of SLC27A5. The results presented here provide preliminary evidence for the association of common variants in genes involved in fat assimilation with the genetic susceptibility of type 2 diabetes. However, they definitely need further verification.
MeSH term(s)	Adult ; Aged ; Case-Control Studies ; Colipases/genetics ; Diabetes Mellitus, Type 2/genetics ; Fatty Acid Transport Proteins/genetics ; Fatty Acid-Binding Proteins/genetics ; Fatty Acids/metabolism ; Female ; Gastrointestinal Hormones ; Genetic Predisposition to Disease ; Humans ; Intramolecular Oxidoreductases/genetics ; Male ; Middle Aged ; Polymorphism, Single Nucleotide ; Prostaglandin-E Synthases
Chemical Substances	Colipases ; Fatty Acid Transport Proteins ; Fatty Acid-Binding Proteins ; Fatty Acids ; Gastrointestinal Hormones ; SLC27A5 protein, human ; fatty acid-binding protein 6 (117849-44-2) ; Intramolecular Oxidoreductases (EC 5.3.-) ; PTGES2 protein, human (EC 5.3.99.3) ; Prostaglandin-E Synthases (EC 5.3.99.3)
Language	English
Publishing date	2007-02
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2161265-1
ISSN	1613-4125
ISSN	1613-4125
DOI	10.1002/mnfr.200600162
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Article: L-FABP T94A is associated with fasting triglycerides and LDL-cholesterol in women.

Fisher, Eva / Weikert, Cornelia / Klapper, Maja / Lindner, Inka / Möhlig, Matthias / Spranger, Joachim / Boeing, Heiner / Schrezenmeir, Jürgen / Döring, Frank

Molecular genetics and metabolism

2007 Volume 91, Issue 3, Page(s) 278–284

Abstract: To determine the possible role of the common FABP1 T94A polymorphism in modulating susceptibility to traits of the metabolic syndrome, we analysed a random sample of 826 subjects from the European Prospective Investigation into Cancer and Nutrition (EPIC) ...

Abstract	To determine the possible role of the common FABP1 T94A polymorphism in modulating susceptibility to traits of the metabolic syndrome, we analysed a random sample of 826 subjects from the European Prospective Investigation into Cancer and Nutrition (EPIC)-Potsdam cohort. Multivariate adjusted linear trend regression analysis of metabolic, anthropometric and blood pressure variables in FABP1 T94A genotypes were performed in both genders. In women, a significant trend of higher plasma triglyceride (P=0.01) and LDL-cholesterol (P=0.02) concentrations were seen for A-allele carriers after adjustment for age, menopausal status, hormone intake and Apo E genotype. Because elevated triglyceride and cholesterol levels are important risk factors of cardiovascular disease (CVD) and type 2 diabetes mellitus (T2DM), we additionally analysed the association of the T94A variant and disease risks in two studies enrolling 220 incident CVD and 192 incident T2DM patients of the EPIC-Potsdam cohort. After adjusting for age, sex, BMI and other covariates, we found no association between FABP1 T94A and CVD or T2DM. In conclusion, our study provides evidence for an association of the FABP1 T94A polymorphism and fasting triglycerides and LDL-cholesterol levels in females. These results support previous findings in fenofibrate-treated individuals and thereby provide some additional indication of the functional relevance of the FABP1 T94A SNP in hepatic fatty acid and lipid metabolism in humans.
MeSH term(s)	Cardiovascular Diseases/genetics ; Cardiovascular Diseases/metabolism ; Case-Control Studies ; Cholesterol, LDL/blood ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Fasting ; Fatty Acid-Binding Proteins/genetics ; Fatty Acid-Binding Proteins/metabolism ; Female ; Genetic Predisposition to Disease ; Humans ; Male ; Metabolic Syndrome/genetics ; Metabolic Syndrome/metabolism ; Middle Aged ; Polymorphism, Single Nucleotide ; Prospective Studies ; Triglycerides/blood
Chemical Substances	Cholesterol, LDL ; FABP1 protein, human ; Fatty Acid-Binding Proteins ; Triglycerides
Language	English
Publishing date	2007-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2007.03.002
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Article: Expression profile of the transient receptor potential (TRP) family in neutrophil granulocytes: evidence for currents through long TRP channel 2 induced by ADP-ribose and NAD.

Heiner, Inka / Eisfeld, Jörg / Halaszovich, Christian R / Wehage, Edith / Jüngling, Eberhard / Zitt, Christof / Lückhoff, Andreas

The Biochemical journal

2003 Volume 371, Issue Pt 3, Page(s) 1045–1053

Abstract: An early key event in the activation of neutrophil granulocytes is Ca(2+) influx. Members of the transient receptor potential (TRP) channel family may be held responsible for this. The aim of the present study is to analyse the expression pattern of TRP ... ...

Abstract	An early key event in the activation of neutrophil granulocytes is Ca(2+) influx. Members of the transient receptor potential (TRP) channel family may be held responsible for this. The aim of the present study is to analyse the expression pattern of TRP mRNA and identify characteristic currents unambiguously attributable to particular TRP channels. mRNA was extracted from human neutrophils, isolated by gradient centrifugation and also by magnetically labelled CD15 antibodies. The presence of mRNA was demonstrated using reverse transcriptase-PCR in neutrophils (controlled to be CD5-negative) as well as in human leukaemic cell line 60 (HL-60) cells, for the following TRP species: the long TRPC2 (LTRPC2), the vanilloid receptor 1, the vanilloid receptor-like protein 1 and epithelial Ca(2+) channels 1 and 2. TRPC6 was specific for neutrophils, whereas only in HL-60 cells were TRPC1, TRPC2, TRPC3, melastatin 1 and melastatin-related 1 found. Patch-clamp measurements in neutrophils revealed non-selective cation currents evoked by intracellular ADP-ribose and by NAD(+). Both these modes of activation have been found to be characteristic of LTRPC2. Furthermore, single-channel activity was resolved in neutrophils and it was indistinguishable from that in LTRPC2-transfected HEK-293 cells. The results provide evidence that LTRPC2 in neutrophil granulocytes forms an entry pathway for Na(+) and Ca(2+), which is regulated by ADP-ribose and the redox state.
MeSH term(s)	Adenosine Diphosphate Ribose/pharmacology ; Base Sequence ; Calcium Channels/drug effects ; Calcium Channels/genetics ; Calcium Channels/physiology ; Cell Line ; DNA Primers ; Gene Expression Profiling ; Humans ; Ion Channels ; Membrane Proteins ; NAD/pharmacology ; Neutrophils/drug effects ; Neutrophils/metabolism ; RNA, Messenger/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; TRPC Cation Channels ; TRPM Cation Channels
Chemical Substances	Calcium Channels ; DNA Primers ; Ion Channels ; Membrane Proteins ; RNA, Messenger ; TRPC Cation Channels ; TRPC2 protein, human ; TRPM Cation Channels ; TRPM2 protein, human ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5)
Language	English
Publishing date	2003-05-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
DOI	10.1042/BJ20021975
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