TY - JOUR AU - Okawa, H. AU - Tanaka, Y. AU - Takahashi, A. TI - Network of extracellular vesicles surrounding senescent cells JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109953 UR - https://m2.mtmt.hu/api/publication/34770344 ID - 34770344 N1 - Export Date: 4 April 2024 CODEN: ABBIA Correspondence Address: Takahashi, A.; Division of Cellular Senescence, 3Ariake, Koto-ku, Japan; email: akiko.takahashi@jfcr.or.jp LA - English DB - MTMT ER - TY - JOUR AU - He, F. AU - Wang, F. AU - Xiang, H. AU - Ma, Y. AU - Lu, Q. AU - Xia, Y. AU - Zhou, H. AU - Wang, Y. AU - Ke, J. TI - Activation of adenosine A2B receptor alleviates myocardial ischemia-reperfusion injury by inhibiting endoplasmic reticulum stress and restoring autophagy flux JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109945 UR - https://m2.mtmt.hu/api/publication/34765474 ID - 34765474 N1 - Export Date: 2 April 2024 CODEN: ABBIA Correspondence Address: Ke, J.; Department of Anesthesiology, China; email: 1219628972@qq.com Correspondence Address: Wang, Y.; Department of Anesthesiology, China; email: wyl0342@sina.com LA - English DB - MTMT ER - TY - JOUR AU - Maiorov, S.A. AU - Kairat, B.K. AU - Berezhnov, A.V. AU - Zinchenko, V.P. AU - Gaidin, S.G. AU - Kosenkov, A.M. TI - Peculiarities of ion homeostasis in neurons containing calcium-permeable AMPA receptors JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109951 UR - https://m2.mtmt.hu/api/publication/34761757 ID - 34761757 N1 - Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences”, Institute of Cell Biophysics of the Russian Academy of Sciences, Pushchino, 142290, Russian Federation Al-Farabi Kazakh National University, Almaty, 050040, Kazakhstan Export Date: 28 March 2024 CODEN: ABBIA Correspondence Address: Kosenkov, A.M.; Institute of Cell Biophysics of the Russian Academy of SciencesRussian Federation; email: kosenckov406@yandex.ru Correspondence Address: Gaidin, S.G.; Institute of Cell Biophysics of the Russian Academy of SciencesRussian Federation; email: sergeigaidin@pbcras.ru LA - English DB - MTMT ER - TY - JOUR AU - Mohamed, H. AU - Child, S.A. AU - Doherty, D.Z. AU - Bruning, J.B. AU - Bell, S.G. TI - Structural determination and characterisation of the CYP105Q4 cytochrome P450 enzyme from Mycobacterium marinum JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109950 UR - https://m2.mtmt.hu/api/publication/34744044 ID - 34744044 N1 - Department of Chemistry, University of AdelaideSA 5005, Australia School of Biological Sciences, University of AdelaideSA 5005, Australia Export Date: 18 March 2024 CODEN: ABBIA Correspondence Address: Bell, S.G.; Department of Chemistry, Australia; email: stephen.bell@adelaide.edu.au LA - English DB - MTMT ER - TY - JOUR AU - Sergeeva, K.V. AU - Tyganov, S.A. AU - Zaripova, K.A. AU - Bokov, R.O. AU - Nikitina, L.V. AU - Konstantinova, T.S. AU - Kalamkarov, G.R. AU - Shenkman, B.S. TI - Mechanical and signaling responses of unloaded rat soleus muscle to chronically elevated β-myosin activity JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109961 UR - https://m2.mtmt.hu/api/publication/34742354 ID - 34742354 N1 - Institute of Biomedical Problems of the Russian Academy of Sciences, Moscow, Russian Federation Institute of Immunology and Physiology, Ural Branch of the Russian Academy of Sciences, Ekaterinburg, Russian Federation Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russian Federation Export Date: 6 April 2024 CODEN: ABBIA Correspondence Address: Sergeeva, K.V.; Institute of Biomedical Problems of the Russian Academy of SciencesRussian Federation; email: sergeeva_xenia@mail.ru Chemicals/CAS: isoflurane, 26675-46-7; omecamtiv mecarbil, 873697-71-3; proteasome, 140879-24-9; ubiquitin, 60267-61-0 Tradenames: ck 1827452, Adooq; isoflutek, laboratories karizoo Manufacturers: Adooq; laboratories karizoo LA - English DB - MTMT ER - TY - JOUR AU - Pupart, H. AU - Lukk, T. AU - Väljamäe, P. TI - Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativity JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 754 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109931 UR - https://m2.mtmt.hu/api/publication/34736510 ID - 34736510 N1 - Department of Chemistry and Biotechnology, Tallinn University of Technology, Akadeemia tee 15, Tallinn, 12618, Estonia Institute of Molecular and Cell Biology, University of Tartu, Riia 23b-202, Tartu, 51010, Estonia Export Date: 13 March 2024 CODEN: ABBIA Correspondence Address: Väljamäe, P.; Institute of Molecular and Cell Biology, Riia 23b-202, Estonia; email: priit.valjamae@ut.ee LA - English DB - MTMT ER - TY - JOUR AU - Tutzauer, J. AU - Serafin, D.S. AU - Schmidt, T. AU - Olde, B. AU - Caron, K.M. AU - Leeb-Lundberg, L.M.F. TI - G protein-coupled estrogen receptor (GPER)/GPR30 forms a complex with the β1-adrenergic receptor, a membrane-associated guanylate kinase (MAGUK) scaffold protein, and protein kinase A anchoring protein (AKAP) 5 in MCF7 breast cancer cells JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 752 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109882 UR - https://m2.mtmt.hu/api/publication/34632928 ID - 34632928 N1 - Department of Experimental Medical Science, Lund University, Lund, 22184, Sweden Department of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, United States Wallenberg Center for Molecular Medicine, Department of Clinical Sciences Lund, Division of Pediatrics, Lund University, Lund, 22184, Sweden Department of Clinical Sciences, Division of Cardiology, Lund University, Lund, 22184, Sweden Export Date: 19 February 2024 CODEN: ABBIA Correspondence Address: Leeb-Lundberg, L.M.F.; Department of Experimental Medical Science, BMC D12, Sölvegatan 19, Sweden; email: fredrik.leeb-lundberg@med.lu.se Chemicals/CAS: carrier protein, 80700-39-6; cyclic AMP dependent protein kinase; guanylate kinase, 9026-59-9; A Kinase Anchor Proteins; AKAP5 protein, human; Carrier Proteins; Cyclic AMP-Dependent Protein Kinases; GTP-Binding Proteins; Guanylate Kinases; Receptors, Adrenergic; Receptors, Estrogen; Receptors, G-Protein-Coupled Funding details: National Institutes of Health, NIH, DK119145, HL129086, T32 NIHT32CA071341 Funding details: Swedish Cancer Foundation, CAN 2016/423 Funding details: Vetenskapsrådet, VR, 2016–02427 Funding text 1: This work was supported by the Swedish Cancer Foundation [ CAN 2016/423 , 19 0479 Pj ], the Swedish Research Council [ 2016–02427 ], and the National Institutes of Health [ T32 NIHT32CA071341 , HL129086 , DK119145 ]. AB - G protein-coupled receptor 30 (GPR30), also named G protein-coupled estrogen receptor (GPER), and the β1-adrenergic receptor (β1AR) are G protein-coupled receptors (GPCR) that are implicated in breast cancer progression. Both receptors contain PSD-95/Discs-large/ZO-1 homology (PDZ) motifs in their C-terminal tails through which they interact in the plasma membrane with membrane-associated guanylate kinase (MAGUK) scaffold proteins, and in turn protein kinase A anchoring protein (AKAP) 5. GPR30 constitutively and PDZ-dependently inhibits β1AR-mediated cAMP production. We hypothesized that this inhibition is a consequence of a plasma membrane complex of these receptors. Using co-immunoprecipitation, confocal immunofluorescence microscopy, and bioluminescence resonance energy transfer (BRET), we show that GPR30 and β1AR reside in close proximity in a plasma membrane complex when transiently expressed in HEK293. Deleting the GPR30 C-terminal PDZ motif (-SSAV) does not interfere with the receptor complex, indicating that the complex is not PDZ-dependent. MCF7 breast cancer cells express GPR30, β1AR, MAGUKs, and AKAP5 in the plasma membrane, and co-immunoprecipitation revealed that these proteins exist in close proximity also under native conditions. Furthermore, expression of GPR30 in MCF7 cells constitutively and PDZ-dependently inhibits β1AR-mediated cAMP production. AKAP5 also inhibits β1AR-mediated cAMP production, which is not additive with GPR30-promoted inhibition. These results argue that GPR30 and β1AR form a PDZ-independent complex in MCF7 cells through which GPR30 constitutively and PDZ-dependently inhibits β1AR signaling via receptor interaction with MAGUKs and AKAP5. © 2024 The Authors LA - English DB - MTMT ER - TY - JOUR AU - Qiu, Jumei AU - Liu, Jing AU - Tian, Limin AU - Yu, Jing AU - Duan, Qidang AU - Liu, Yaqian AU - Zhao, Wenshu AU - Si, Huiling AU - Lu, Xun AU - Zhang, Qi TI - Knockdown of LOX-1 ameliorates bone quality and generation of type H blood vessels in diabetic mice JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 752 PY - 2024 PG - 12 SN - 0003-9861 DO - 10.1016/j.abb.2023.109870 UR - https://m2.mtmt.hu/api/publication/34624236 ID - 34624236 LA - English DB - MTMT ER - TY - JOUR AU - Mitchell-White, J.I. AU - Briggs, D.A. AU - Mistry, S.J. AU - Mbiwan, H.A. AU - Kellam, B. AU - Holliday, N.D. AU - Briddon, S.J. AU - Kerr, I.D. TI - A time-resolved Förster resonance energy transfer assay to investigate drug and inhibitor binding to ABCG2 JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 753 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2024.109915 UR - https://m2.mtmt.hu/api/publication/34582642 ID - 34582642 N1 - School of Life Sciences, University of Nottingham, Queen's Medical, Centre, Nottingham, NG7 2UH, United Kingdom Centre of Membrane Proteins and Receptors, Universities of Birmingham and Nottingham, The Midlands, United Kingdom School of Pharmacy, University of Nottingham, Nottingham, NG7 2UH, United Kingdom Export Date: 14 February 2024 CODEN: ABBIA Correspondence Address: Kerr, I.D.; School of Life Sciences, United Kingdom; email: ian.kerr@nottingham.ac.uk Correspondence Address: Mitchell-White, J.I.; School of Life Sciences, United Kingdom; email: jamesjimitchell@gmail.com Funding details: Biotechnology and Biological Sciences Research Council, BBSRC, BB/M008770/1, BB/S001611/1 Funding text 1: This work was supported by Biotechnology and Biological Sciences Research Council [grant number: BB/S001611/1 ] to IDK, SJB and NDH. HAM was supported by BBSRC Doctoral Training Grant [ BB/M008770/1 ] AB - The human ATP-binding cassette (ABC) transporter, ABCG2, is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications for wider pharmacokinetics. The binding of substrates and inhibitors is a key stage in the transport cycle of ABCG2. Here, we describe a novel binding assay using a high affinity fluorescent inhibitor based on Ko143 and time-resolved Förster resonance energy transfer (TR-FRET) to measure saturation binding to ABCG2. This binding is displaced by Ko143 and other known ABCG2 ligands, and is sensitive to the addition of AMP-PNP, a non-hydrolysable ATP analogue. This assay complements the arsenal of methods for determining drug:ABCG2 interactions and has the possibility of being adaptable for other multidrug pumps. © 2024 The Author(s) LA - English DB - MTMT ER - TY - JOUR AU - Guner-Yılmaz, O.Z. AU - Kurkcuoglu, O. AU - Akten, E.D. TI - Tunnel-like region observed as a potential allosteric site in Staphylococcus aureus Glyceraldehyde-3-phosphate dehydrogenase JF - ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS J2 - ARCH BIOCHEM BIOPHYS VL - 752 PY - 2024 SN - 0003-9861 DO - 10.1016/j.abb.2023.109875 UR - https://m2.mtmt.hu/api/publication/34560679 ID - 34560679 N1 - Department of Chemical Engineering, Istanbul Technical University, Istanbul, Turkey Department of Molecular Biology and Genetics, Faculty of Engineering and Natural Sciences, Kadir Has University, Istanbul, Turkey Export Date: 6 February 2024 CODEN: ABBIA Correspondence Address: Akten, E.D.; Department of Molecular Biology and Genetics, Turkey; email: demet.akten@khas.edu.tr Chemicals/CAS: glyceraldehyde 3 phosphate dehydrogenase, 9001-50-7; nicotinamide adenine dinucleotide, 53-84-9; terlipressin, 14636-12-5 Funding details: Türkiye Bilimsel ve Teknolojik Araştırma Kurumu, TÜBİTAK, 218M320 Funding text 1: This work has been partially supported by The Scientific and Technological Research Council of Turkey (TÜBİTAK Project # 218M320 ). AB - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyzing the sixth step of glycolysis has been investigated for allosteric features that might be used as potential target for specific inhibition of Staphylococcus aureus (S.aureus). X-ray structure of bacterial enzyme for which a tunnel-like opening passing through the center previously proposed as an allosteric site has been subjected to six independent 500 ns long Molecular Dynamics simulations. Harmonic bond restraints were employed at key residues to underline the allosteric feature of this region. A noticeable reduction was observed in the mobility of NAD+ binding domains when restrictions were applied. Also, a substantial decrease in cross-correlations between distant Cα fluctuations was detected throughout the structure. Mutual information (MI) analysis revealed a similar decrease in the degree of correspondence in positional fluctuations in all directions everywhere in the receptor. MI between backbone and side-chain torsional variations changed its distribution profile and decreased considerably around the catalytic sites when restraints were employed. Principal component analysis clearly showed that the restrained state sampled a narrower range of conformations than apo state, especially in the first principal mode due to restriction in the conformational flexibility of NAD+ binding domain. Clustering the trajectory based on catalytic site residues displayed a smaller repertoire of conformations for restrained state compared to apo. Representative snapshots subjected to k-shortest pathway analysis revealed the impact of bond restraints on the allosteric communication which displayed distinct optimal and suboptimal pathways for two states, where observed frequencies of critical residues Gln51 and Val283 at the proposed site changed considerably. © 2023 Elsevier Inc. LA - English DB - MTMT ER -