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  • 1.
    Cannon, Barbara
    et al.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Nedergaard, Jan
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    What Ignites UCP1?2017In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 26, no 5, p. 697-698Article in journal (Other academic)
    Abstract [en]

    We thought we knew how the heat-producing uncoupling protein 1 in brown adipose tissue was activated: by fatty acids released upon lipid droplet breakdown in the brown adipocytes. However, two studies in this issue (Schreiber et al., 2017; Shin et al., 2017) imply that this classical model may not be valid: heat can be produced in brown fat without intracellular lipolysis.

  • 2. Correia, Jorge C.
    et al.
    Kelahmetoglu, Yildiz
    Jannig, Paulo R.
    Schweingruber, Christoph
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Karolinska Institutet, Sweden.
    Shvaikovskaya, Dasha
    Zhengye, Liu
    Cervenka, Igor
    Khan, Naveen
    Stec, Michael
    Oliveira, Mariana
    Nijssen, Jik
    Martínez-Redondo, Vicente
    Ducommun, Serge
    Azzolini, Michele
    Lanner, Johanna T.
    Kleiner, Sandra
    Hedlund, Eva
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Karolinska Institutet, Sweden.
    Ruas, Jorge L.
    Muscle-secreted neurturin couples myofiber oxidative metabolism and slow motor neuron identity2021In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 33, no 11, p. 2215-2230Article in journal (Refereed)
    Abstract [en]

    Endurance exercise promotes skeletal muscle vascularization, oxidative metabolism, fiber-type switching, and neuromuscular junction integrity. Importantly, the metabolic and contractile properties of the muscle fiber must be coupled to the identity of the innervating motor neuron (MN). Here, we show that muscle-derived neurturin (NRTN) acts on muscle fibers and MNs to couple their characteristics. Using a muscle-specific NRTN transgenic mouse (HSA-NRTN) and RNA sequencing of MN somas, we observed that retrograde NRTN signaling promotes a shift toward a slow MN identity. In muscle, NRTN increased capillary density and oxidative capacity and induced a transcriptional reprograming favoring fatty acid metabolism over glycolysis. This combination of effects on muscle and MNs makes HSA-NRTN mice lean with remarkable exercise performance and motor coordination. Interestingly, HSA-NRTN mice largely recapitulate the phenotype of mice with muscle-specific expression of its upstream regulator PGC-1a1. This work identifies NRTN as a myokine that couples muscle oxidative capacity to slow MN identity.

  • 3. Mossmann, Dirk
    et al.
    Voegtle, F-Nora
    Taskin, Asli Aras
    Teixeira, Pedro Filipe
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Ring, Julia
    Burkhart, Julia M.
    Burger, Nils
    Pinho, Catarina Moreira
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Tadic, Jelena
    Loreth, Desiree
    Graff, Caroline
    Metzger, Friedrich
    Sickmann, Albert
    Kretz, Oliver
    Wiedemann, Nils
    Zahedi, Rene P.
    Madeo, Frank
    Glaser, Elzbieta
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Meisinger, Chris
    Amyloid-beta Peptide Induces Mitochondrial Dysfunction by Inhibition of Preprotein Maturation2014In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 20, no 4, p. 662-669Article in journal (Refereed)
    Abstract [en]

    Most mitochondrial proteins possess N-terminal presequences that are required for targeting and import into the organelle. Upon import, presequences are cleaved off by matrix processing peptidases and subsequently degraded by the peptidasome Cym1/PreP, which also degrades Amyloid-beta peptides (A beta). Here we find that impaired turnover of presequence peptides results in feedback inhibition of presequence processing enzymes. Moreover, A beta inhibits degradation of presequence peptides by PreP, resulting in accumulation of mitochondrial preproteins and processing intermediates. Dysfunctional preprotein maturation leads to rapid protein degradation and an imbalanced organellar proteome. Our findings reveal a general mechanism by which A beta peptide can induce the multiple diverse mitochondrial dysfunctions accompanying Alzheimer's disease.

  • 4.
    Nedergaard, Jan
    et al.
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Bengtsson, Tore
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Cannon, Barbara
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    New Powers of Brown Fat: Fighting the Metabolic Syndrome2011In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 13, no 3, p. 238-240Article in journal (Refereed)
    Abstract [en]

    An understanding of the full powers of brown adipose tissue (BAT) is only successively being accumulated. In a paper in Nature Medicine, Bartelt et al. (2011) add further impressive aspects to the potential powers of BAT in the combat against the metabolic syndrome by demonstrating its vast capacity for triglyceride clearance and glucose disposal.

  • 5.
    Nedergaard, Jan
    et al.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Cannon, Barbara
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    The Browning of White Adipose Tissue: Some Burning Issues2014In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 20, no 3, p. 396-407Article, review/survey (Refereed)
    Abstract [en]

    Igniting thermogenesis within white adipose tissue (i.e., promoting expression and activity of the uncoupling protein UCP1) has attracted much interest. Numerous browning agents'' have now been described (gene ablations, transgenes, foodcomponents, drugs, environments, etc.). The implied action of browning agents is that they increase UCP1 through this heat production, leading to slimming. Here, we particularly point to the possibility that cause and effect may on occasion be the reverse: browning agents may disrupt, for example, the fur, leading to increased heat loss, increased thermogenic demand to counteract this heat loss, and thus, through sympathetic nervous system activation, to enhanced UCP1 expression in white (and brown) adipose tissues.

  • 6.
    Suhm, Tamara
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Kaimal, Jayasankar Mohanakrishnan
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Dawitz, Hannah
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Peselj, Carlotta
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Masser, Anna E.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Hanzén, Sarah
    Ambrožič, Matevž
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Smialowska, Agata
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
    Björck, Markus L.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Brzezinski, Peter
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Nyström, Thomas
    Büttner, Sabrina
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute. University of Graz, Austria.
    Andréasson, Claes
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Mitochondrial Translation Efficiency Controls Cytoplasmic Protein Homeostasis2018In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 27, no 6, p. 1309-1322Article in journal (Refereed)
    Abstract [en]

    Cellular proteostasis ismaintained via the coordinated synthesis, maintenance, and breakdown of proteins in the cytosol and organelles. While biogenesis of the mitochondrial membrane complexes that execute oxidative phosphorylation depends on cytoplasmic translation, it is unknown how translation within mitochondria impacts cytoplasmic proteostasis and nuclear gene expression. Here we have analyzed the effects of mutations in the highly conserved accuracy center of the yeast mitoribosome. Decreased accuracy of mitochondrial translation shortened chronological lifespan, impaired management of cytosolic protein aggregates, and elicited a general transcriptional stress response. In striking contrast, increased accuracy extended lifespan, improved cytosolic aggregate clearance, and suppressed a normally stress-induced, Msn2/4-dependent interor-ganellar proteostasis transcription program (IPTP) that regulates genes important for mitochondrial proteostasis. Collectively, the data demonstrate that cytosolic protein homeostasis and nuclear stress signaling are controlled by mitochondrial translation efficiency in an inter-connected organelle quality control network that determines cellular lifespan.

  • 7. Xue, Yuan
    et al.
    Petrovic, Natasa
    Stockholm University, Faculty of Science, The Wenner-Gren Institute, Physiology.
    Cao, Renhai
    Larsson, Ola
    Lim, Sharon
    Chen, Shaohua
    Feldmann, Helena M.
    Stockholm University, Faculty of Science, The Wenner-Gren Institute, Physiology.
    Liang, Zicai
    Zhu, Zhenping
    Nedergaard, Jan
    Stockholm University, Faculty of Science, The Wenner-Gren Institute, Physiology.
    Cannon, Barbara
    Stockholm University, Faculty of Science, The Wenner-Gren Institute, Physiology.
    Cao, Yihai
    Hypoxia-independent angiogenesis in adipose tissues during cold acclimation.2009In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 9, no 1, p. 99-109Article in journal (Refereed)
    Abstract [en]

    The molecular mechanisms of angiogenesis in relation to adipose tissue metabolism remain poorly understood. Here, we show that exposure of mice to cold led to activation of angiogenesis in both white and brown adipose tissues. In the inguinal depot, cold exposure resulted in elevated expression levels of brown-fat-associated proteins, including uncoupling protein-1 (UCP1) and PGC-1alpha. Proangiogenic factors such as VEGF were upregulated, and endogenous angiogenesis inhibitors, including thrombospondin, were downregulated. In wild-type mice, the adipose tissues became hypoxic during cold exposure; in UCP1(-/-) mice, hypoxia did not occur, but, remarkably, the augmented angiogenesis was unaltered and was thus hypoxia independent. Intriguingly, VEGFR2 blockage abolished the cold-induced angiogenesis and significantly impaired nonshivering thermogenesis capacity. Unexpectedly, VEGFR1 blockage resulted in the opposite effects: increased adipose vascularity and nonshivering thermogenesis capacity. Our findings have conceptual implications concerning application of angiogenesis modulators for treatment of obesity and metabolic disorders.

  • 8. Zenius Jespersen, Naja
    et al.
    Juhlin Larsen, Therese
    Peijs, Lone
    Daugaard, Søren
    Homøe, Preben
    Loft, Annika
    de Jong, Jasper
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Mathur, Neha
    Cannon, Barbara
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Nedergaard, Jan
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Klarlund Pedersen, Bente
    Møller, Kirsten
    Scheele, Camilla
    A classical brown adipose tissue mRNA signature partly overlaps with brite in the supraclavicular region of adult humans2013In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 17, no 5, p. 798-805Article in journal (Refereed)
    Abstract [en]

    Human brown adipose tissue (BAT) has been detected in adults but was recently suggested to be of brite/beige origin. We collected BAT from the supraclavicular region in 21 patients undergoing surgery for suspected cancer in the neck area and assessed the gene expression of established murine markers for brown, brite/beige, and white adipocytes. We demonstrate that a classical brown expression signature, including upregulation of miR-206, miR-133b, LHX8, and ZIC1 and downregulation of HOXC8 and HOXC9, coexists with an upregulation of two newly established brite/beige markers, TBX1 and TMEM26. A similar mRNA expression profile was observed when comparing isolated human adipocytes from BAT and white adipose tissue (WAT) depots, differentiated in vitro. In conclusion, our data suggest that human BAT might consist of both classical brown and recruitable brite adipocytes, an observation important for future considerations on how to induce human BAT.

  • 9. Zhang, Qian
    et al.
    Delessa, Challa Tenagne
    Augustin, Robert
    Bakhti, Mostafa
    Colldén, Gustav
    Drucker, Daniel J.
    Feuchtinger, Annette
    Garcia Caceres, Cristina
    Grandl, Gerald
    Harger, Alexandra
    Herzig, Stephan
    Hofmann, Susanna
    Holleman, Cassie Lynn
    Jastroch, Martin
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Keipert, Susanne
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Kleinert, Maximilian
    Knerr, Patrick J.
    Kulaj, Konxhe
    Legutko, Beata
    Lickert, Heiko
    Liu, Xue
    Luippold, Gerd
    Lutter, Dominik
    Malogajski, Emilija
    Tarquis Medina, Marta
    Mowery, Stephanie A.
    Blutke, Andreas
    Perez-Tilve, Diego
    Salinno, Ciro
    Sehrer, Laura
    DiMarchi, Richard D.
    Tschöp, Matthias H.
    Stemmer, Kerstin
    Finan, Brian
    Wolfrum, Christian
    Müller, Timo D.
    The glucose-dependent insulinotropic polypeptide (GIP) regulates body weight and food intake via CNS-GIPR signaling2021In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 33, no 4, p. 833-844Article in journal (Refereed)
    Abstract [en]

    Uncertainty exists as to whether the glucose-dependent insulinotropic polypeptide receptor (GIPR) should be activated or inhibited for the treatment of obesity. Gipr was recently demonstrated in hypothalamic feeding centers, but the physiological relevance of CNS Gipr remains unknown. Here we show that HFD-fed CNS-Gipr KO mice and humanized (h)GIPR knockin mice with CNS-hGIPR deletion show decreased body weight and improved glucose metabolism. In DIO mice, acute central and peripheral administration of acyl-GIP increases cFos neuronal activity in hypothalamic feeding centers, and this coincides with decreased body weight and food intake and improved glucose handling. Chronic central and peripheral administration of acyl-GIP lowers body weight and food intake in wild-type mice, but shows blunted/absent efficacy in CNS-Gipr KO mice. Also, the superior metabolic effect of GLP-1/GIP co-agonism relative to GLP-1 is extinguished in CNS-Gipr KO mice. Our data hence establish a key role of CNS Gipr for control of energy metabolism.

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