LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 128

Search options

  1. Article ; Online: Translation elongation factor EF-Tu modulates filament formation of actin-like MreB protein in vitro.

    Defeu Soufo, Hervé Joël / Reimold, Christian / Breddermann, Hannes / Mannherz, Hans G / Graumann, Peter L

    Journal of molecular biology

    2015  Volume 427, Issue 8, Page(s) 1715–1727

    Abstract: EF-Tu has been shown to interact with actin-like protein MreB and to affect its localization in Escherichia coli and in Bacillus subtilis cells. We have purified YFP-MreB in an active form, which forms filaments on glass slides in vitro and was active in ...

    Abstract EF-Tu has been shown to interact with actin-like protein MreB and to affect its localization in Escherichia coli and in Bacillus subtilis cells. We have purified YFP-MreB in an active form, which forms filaments on glass slides in vitro and was active in dynamic light-scattering assays, polymerizing in milliseconds after addition of magnesium. Purified EF-Tu enhanced the amount of MreB filaments, as seen by sedimentation assays, the speed of filament formation and the length of MreB filaments in vitro. EF-Tu had the strongest impact on MreB filaments in a 1:1 ratio, and EF-Tu co-sedimented with MreB filaments, revealing a stoichiometric interaction between both proteins. This was supported by cross-linking assays where 1:1 species were well detectable. When expressed in E. coli cells, B. subtilis MreB formed filaments and induced the formation of co-localizing B. subtilis EF-Tu structures, indicating that MreB can direct the positioning of EF-Tu structures in a heterologous cell system. Fluorescence recovery after photobleaching analysis showed that MreB filaments have a higher turnover in B. subtilis cells than in E. coli cells, indicating different filament kinetics in homologous or heterologous cell systems. The data show that MreB can direct the localization of EF-Tu in vivo, which in turn positively affects the formation and dynamics of MreB filaments. Thus, EF-Tu is a modulator of the activity of a bacterial actin-like protein.
    MeSH term(s) Bacillus subtilis/cytology ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/analysis ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cytoskeletal Proteins/analysis ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Escherichia coli/cytology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Peptide Elongation Factor Tu/analysis ; Peptide Elongation Factor Tu/metabolism ; Protein Interaction Maps
    Chemical Substances Bacterial Proteins ; Cytoskeletal Proteins ; Peptide Elongation Factor Tu (EC 3.6.1.-)
    Language English
    Publishing date 2015-04-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2015.01.025
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article: Crystallization of actin in complex with actin-binding proteins.

    Mannherz, H G

    The Journal of biological chemistry

    1992  Volume 267, Issue 17, Page(s) 11661–11664

    MeSH term(s) Actins/chemistry ; Actins/metabolism ; Animals ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/metabolism ; Contractile Proteins ; Crystallization ; Deoxyribonuclease I/chemistry ; Deoxyribonuclease I/metabolism ; Gelsolin ; Microfilament Proteins/chemistry ; Microfilament Proteins/metabolism ; Profilins ; Protein Conformation
    Chemical Substances Actins ; Calcium-Binding Proteins ; Contractile Proteins ; Gelsolin ; Microfilament Proteins ; Profilins ; Deoxyribonuclease I (EC 3.1.21.1)
    Language English
    Publishing date 1992-06-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Infantile restrictive cardiomyopathy: cTnI-R170G/W impair the interplay of sarcomeric proteins and the integrity of thin filaments.

    Cimiotti, Diana / Fujita-Becker, Setsuko / Möhner, Desirée / Smolina, Natalia / Budde, Heidi / Wies, Aline / Morgenstern, Lisa / Gudkova, Alexandra / Sejersen, Thomas / Sjöberg, Gunnar / Mügge, Andreas / Nowaczyk, Marc M / Reusch, Peter / Pfitzer, Gabriele / Stehle, Robert / Schröder, Rasmus R / Mannherz, Hans G / Kostareva, Anna / Jaquet, Kornelia

    PloS one

    2020  Volume 15, Issue 3, Page(s) e0229227

    Abstract: TNNI3 encoding cTnI, the inhibitory subunit of the troponin complex, is the main target for mutations leading to restrictive cardiomyopathy (RCM). Here we investigate two cTnI-R170G/W amino acid replacements, identified in infantile RCM patients, which ... ...

    Abstract TNNI3 encoding cTnI, the inhibitory subunit of the troponin complex, is the main target for mutations leading to restrictive cardiomyopathy (RCM). Here we investigate two cTnI-R170G/W amino acid replacements, identified in infantile RCM patients, which are located in the regulatory C-terminus of cTnI. The C-terminus is thought to modulate the function of the inhibitory region of cTnI. Both cTnI-R170G/W strongly enhanced the Ca2+-sensitivity of skinned fibres, as is typical for RCM-mutations. Both mutants strongly enhanced the affinity of troponin (cTn) to tropomyosin compared to wildtype cTn, whereas binding to actin was either strengthened (R170G) or weakened (R170W). Furthermore, the stability of reconstituted thin filaments was reduced as revealed by electron microscopy. Filaments containing R170G/W appeared wavy and showed breaks. Decoration of filaments with myosin subfragment S1 was normal in the presence of R170W, but was irregular with R170G. Surprisingly, both mutants did not affect the Ca2+-dependent activation of reconstituted cardiac thin filaments. In the presence of the N-terminal fragment of cardiac myosin binding protein C (cMyBPC-C0C2) cooperativity of thin filament activation was increased only when the filaments contained wildtype cTn. No effect was observed in the presence of cTn containing R170G/W. cMyBPC-C0C2 significantly reduced binding of wildtype troponin to actin/tropomyosin, but not of both mutant cTn. Moreover, we found a direct troponin/cMyBPC-C0C2 interaction using microscale thermophoresis and identified cTnI and cTnT, but not cTnC as binding partners for cMyBPC-C0C2. Only cTn containing cTnI-R170G showed a reduced affinity towards cMyBPC-C0C2. Our results suggest that the RCM cTnI variants R170G/W impair the communication between thin and thick filament proteins and destabilize thin filaments.
    MeSH term(s) Actins/metabolism ; Amino Acid Substitution ; Animals ; Calcium/metabolism ; Cardiomyopathy, Restrictive/genetics ; Cardiomyopathy, Restrictive/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Child, Preschool ; Guinea Pigs ; Humans ; Microscopy, Electron ; Models, Biological ; Myocardium/metabolism ; Protein Binding ; Sarcomeres/metabolism ; Tropomyosin/metabolism ; Troponin I/genetics
    Chemical Substances Actins ; Carrier Proteins ; TNNI3 protein, human ; Tropomyosin ; Troponin I ; myosin-binding protein C ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2020-03-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0229227
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: De Novo Missense Mutations in

    Hassoun, Roua / Budde, Heidi / Mannherz, Hans Georg / Lódi, Mária / Fujita-Becker, Setsuko / Laser, Kai Thorsten / Gärtner, Anna / Klingel, Karin / Möhner, Desirée / Stehle, Robert / Sultana, Innas / Schaaf, Thomas / Majchrzak, Mario / Krause, Verena / Herrmann, Christian / Nowaczyk, Marc M / Mügge, Andreas / Pfitzer, Gabriele / Schröder, Rasmus R /
    Hamdani, Nazha / Milting, Hendrik / Jaquet, Kornelia / Cimiotti, Diana

    International journal of molecular sciences

    2021  Volume 22, Issue 17

    Abstract: Rare pediatric non-compaction and restrictive cardiomyopathy are usually associated with a rapid and severe disease progression. While the non-compaction phenotype is characterized by structural defects and is correlated with systolic dysfunction, the ... ...

    Abstract Rare pediatric non-compaction and restrictive cardiomyopathy are usually associated with a rapid and severe disease progression. While the non-compaction phenotype is characterized by structural defects and is correlated with systolic dysfunction, the restrictive phenotype exhibits diastolic dysfunction. The molecular mechanisms are poorly understood. Target genes encode among others, the cardiac troponin subunits forming the main regulatory protein complex of the thin filament for muscle contraction. Here, we compare the molecular effects of two infantile de novo point mutations in
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Adult ; Calcium/metabolism ; Cardiomyopathies/genetics ; Cardiomyopathies/metabolism ; Cardiomyopathies/pathology ; Catechin/analogs & derivatives ; Catechin/pharmacology ; Humans ; Infant ; Male ; Microscopy, Electron, Transmission ; Mutation, Missense ; Myofibrils/drug effects ; Myofibrils/metabolism ; Myofibrils/ultrastructure ; Sarcomeres/drug effects ; Sarcomeres/metabolism ; Severity of Illness Index ; Simendan/pharmacology ; Tropomyosin/metabolism ; Troponin I/genetics ; Troponin I/metabolism
    Chemical Substances TNNI1 protein, human ; TNNI3 protein, human ; Tropomyosin ; Troponin I ; Simendan (349552KRHK) ; Catechin (8R1V1STN48) ; epigallocatechin gallate (BQM438CTEL) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2021-09-06
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22179625
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article: Protection against nuclear degradation by Dnase1 binding to actin

    Eulitz, D. / Mannherz, H. G.

    Verhandlungen der Anatomischen Gesellschaft : ... Versammlung

    2005  Volume -, Issue 100, Page(s) 100

    Language German
    Document type Article
    ZDB-ID 209662-6
    ISSN 0066-1562
    Database Current Contents Medicine

    More links

    Kategorien

  6. Article: The apoptosis endonucleases: cleaning up after cell death?

    Peitsch, M C / Mannherz, H G / Tschopp, J

    Trends in cell biology

    2004  Volume 4, Issue 2, Page(s) 37–41

    Abstract: The term apoptosis describes the predictable structural changes associated with many forms of programmed cell death. One of the first visible events of apoptosis is the collapse of the nucleus. Nuclear degradation is manifested by digestion of chromatin ... ...

    Abstract The term apoptosis describes the predictable structural changes associated with many forms of programmed cell death. One of the first visible events of apoptosis is the collapse of the nucleus. Nuclear degradation is manifested by digestion of chromatin into nucleosome-sized fragments or multiples of these. This digestion of DNA is enzymatic, and several attempts have been made to characterize apoptosis-specific endodeoxyribonucleases. Although there are strong candidates for such enzymes, direct evidence for their role in apoptosis is yet to be provided.
    Language English
    Publishing date 2004-03-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/0962-8924(94)90002-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  7. Article ; Online: Induction of fat cell necrosis in human fat tissue after treatment with phosphatidylcholine and deoxycholate.

    Bechara, F G / Mannherz, H G / Jacob, M / Mazur, A J / Sand, M / Altmeyer, P / Hoffmann, K

    Journal of the European Academy of Dermatology and Venereology : JEADV

    2012  Volume 26, Issue 2, Page(s) 180–185

    Abstract: Background: Injections with phosphatidylcholine- and deoxycholate-containing substances are used to treat localized fat accumulation and lipomas. It is believed that the injected substances induce fat cell destruction with subsequent acute panniculitis ... ...

    Abstract Background: Injections with phosphatidylcholine- and deoxycholate-containing substances are used to treat localized fat accumulation and lipomas. It is believed that the injected substances induce fat cell destruction with subsequent acute panniculitis followed by a repair process of the treated fat tissue.
    Objectives: We investigated whether necrosis or apoptosis of fat cells was induced by the injected substances.
    Methods: Samples of fat tissue of lipoma were collected at various times after injection and evaluated by light and electron microscopy, by immunostaining for active caspase-3 and antideoxyribonuclease I, in situ end-labelling (TUNEL staining), and biochemical caspase-3 assays.
    Results: Light and electron microscopy showed fat cell necrosis in all areas of the treated lipomas. Low levels of active caspase-3 indicated the absence of apoptosis.
    Conclusions: Injection of the lipolytic substances phosphatidylcholine and deoxycholate leads to fat cell necrosis rather than apoptosis. However, additional studies evaluating different dosing and further time points after treatment are necessary.
    MeSH term(s) Adipose Tissue/cytology ; Adipose Tissue/drug effects ; Caspase 3/metabolism ; Deoxycholic Acid/pharmacology ; Deoxyribonuclease I/metabolism ; Humans ; In Situ Nick-End Labeling ; Lipolysis ; Microscopy, Electron ; Necrosis ; Phosphatidylcholines/pharmacology
    Chemical Substances Phosphatidylcholines ; Deoxycholic Acid (005990WHZZ) ; Deoxyribonuclease I (EC 3.1.21.1) ; Caspase 3 (EC 3.4.22.-)
    Language English
    Publishing date 2012-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1128828-0
    ISSN 1468-3083 ; 0926-9959
    ISSN (online) 1468-3083
    ISSN 0926-9959
    DOI 10.1111/j.1468-3083.2011.04028.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  8. Article ; Online: Impaired DNase1-mediated degradation of neutrophil extracellular traps is associated with acute thrombotic microangiopathies.

    Jiménez-Alcázar, M / Napirei, M / Panda, R / Köhler, E C / Kremer Hovinga, J A / Mannherz, H G / Peine, S / Renné, T / Lämmle, B / Fuchs, T A

    Journal of thrombosis and haemostasis : JTH

    2015  Volume 13, Issue 5, Page(s) 732–742

    Abstract: Background: Acute thrombotic microangiopathies (TMAs) are characterized by excessive microvascular thrombosis and are associated with markers of neutrophil extracellular traps (NETs) in plasma. NETs are composed of DNA fibers and promote thrombus ... ...

    Abstract Background: Acute thrombotic microangiopathies (TMAs) are characterized by excessive microvascular thrombosis and are associated with markers of neutrophil extracellular traps (NETs) in plasma. NETs are composed of DNA fibers and promote thrombus formation through the activation of platelets and clotting factors.
    Objective: The efficient removal of NETs may be required to prevent excessive thrombosis such as in TMAs. To test this hypothesis, we investigated whether TMAs are associated with a defect in the degradation of NETs.
    Methods and results: We show that NETs generated in vitro were efficiently degraded by plasma from healthy donors. However, NETs remained stable after exposure to plasma from TMA patients. The inability to degrade NETs was linked to a reduced DNase activity in TMA plasma. Plasma DNase1 was required for efficient NET degradation and TMA plasma showed decreased levels of this enzyme. Supplementation of TMA plasma with recombinant human DNase1 restored NET-degradation activity.
    Conclusions: Our data indicate that DNase1-mediated degradation of NETs is impaired in patients with TMAs. The role of plasma DNases in thrombosis is, as of yet, poorly understood. Reduced plasma DNase1 activity may cause the persistence of pro-thrombotic NETs and thus promote microvascular thrombosis in TMA patients.
    MeSH term(s) Deoxyribonuclease I/metabolism ; Extracellular Traps/metabolism ; Humans ; Hydrolysis ; Neutrophils/metabolism ; Thrombotic Microangiopathies/blood
    Chemical Substances Deoxyribonuclease I (EC 3.1.21.1)
    Language English
    Publishing date 2015-04-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2112661-6
    ISSN 1538-7836 ; 1538-7933
    ISSN (online) 1538-7836
    ISSN 1538-7933
    DOI 10.1111/jth.12796
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  9. Article ; Online: Reelin and cofilin cooperate during the migration of cortical neurons: a quantitative morphological analysis.

    Chai, Xuejun / Zhao, Shanting / Fan, Li / Zhang, Wei / Lu, Xi / Shao, Hong / Wang, Shaobo / Song, Lingzhen / Failla, Antonio Virgilio / Zobiak, Bernd / Mannherz, Hans G / Frotscher, Michael

    Development (Cambridge, England)

    2016  Volume 143, Issue 6, Page(s) 1029–1040

    Abstract: In reeler mutant mice, which are deficient in reelin (Reln), the lamination of the cerebral cortex is disrupted. Reelin signaling induces phosphorylation of LIM kinase 1, which phosphorylates the actin-depolymerizing protein cofilin in migrating neurons. ...

    Abstract In reeler mutant mice, which are deficient in reelin (Reln), the lamination of the cerebral cortex is disrupted. Reelin signaling induces phosphorylation of LIM kinase 1, which phosphorylates the actin-depolymerizing protein cofilin in migrating neurons. Conditional cofilin mutants show neuronal migration defects. Thus, both reelin and cofilin are indispensable during cortical development. To analyze the effects of cofilin phosphorylation on neuronal migration we used in utero electroporation to transfect E14.5 wild-type cortical neurons with pCAG-EGFP plasmids encoding either a nonphosphorylatable form of cofilin 1 (cofilin(S3A)), a pseudophosphorylated form (cofilin(S3E)) or wild-type cofilin 1 (cofilin(WT)). Wild-type controls and reeler neurons were transfected with pCAG-EGFP. Real-time microscopy and histological analyses revealed that overexpression of cofilin(WT) and both phosphomutants induced migration defects and morphological abnormalities of cortical neurons. Of note, reeler neurons and cofilin(S3A)- and cofilin(S3E)-transfected neurons showed aberrant backward migration towards the ventricular zone. Overexpression of cofilin(S3E), the pseudophosphorylated form, partially rescued the migration defect of reeler neurons, as did overexpression of Limk1. Collectively, the results indicate that reelin and cofilin cooperate in controlling cytoskeletal dynamics during neuronal migration.
    MeSH term(s) Animals ; Cell Adhesion Molecules, Neuronal/metabolism ; Cell Count ; Cell Movement ; Cell Shape ; Cerebral Cortex/cytology ; Cofilin 1/metabolism ; Electroporation ; Embryo, Mammalian/cytology ; Extracellular Matrix Proteins/metabolism ; Female ; Mice, Inbred C57BL ; Nerve Tissue Proteins/metabolism ; Neurons/cytology ; Neurons/metabolism ; Serine Endopeptidases/metabolism ; Transfection
    Chemical Substances Cell Adhesion Molecules, Neuronal ; Cofilin 1 ; Extracellular Matrix Proteins ; Nerve Tissue Proteins ; Serine Endopeptidases (EC 3.4.21.-) ; reelin protein (EC 3.4.21.-)
    Language English
    Publishing date 2016-03-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.134163
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  10. Article: MDia, Thymosin Beta 4 and Actin polymerisation

    Sokoll, A. / Ritenberg, U. / Mannherz, H. G.

    Verhandlungen der Anatomischen Gesellschaft : ... Versammlung

    2005  Volume -, Issue 100, Page(s) 177

    Language German
    Document type Article
    ZDB-ID 209662-6
    ISSN 0066-1562
    Database Current Contents Medicine

    More links

    Kategorien

To top