Gymnastik- och idrottshögskolan, GIH

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  • 1. Andersson, Ulrika
    et al.
    Leighton, Brendan
    Young, Martin E
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Newsholme, Eric A
    Inactivation of aconitase and oxoglutarate dehydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide.1998In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 249, no 2, p. 512-6Article in journal (Refereed)
    Abstract [en]

    Strips of rat soleus muscle were incubated in media containing a superoxide generating system and/or the nitric oxide donor sodium nitroprusside (SNP) before the maximal catalytic activities of aconitase, citrate synthase, and oxoglutarate dehydrogenase were measured. The maximal activities of aconitase and oxoglutarate dehydrogenase were both decreased by 25-30% by superoxide anions; however, only the maximal activity of aconitase was decreased, by approximately 50%, by incubation of muscles with SNP. Furthermore, when both superoxide and NO were present in the medium, aconitase activity was decreased by 70%. The maximal activity of citrate synthase was not affected by any of the treatments. This is the first time that superoxide anions or NO has been shown to inactivate aconitase and oxoglutarate dehydrogenase in skeletal muscle. It is suggested that these effects may be responsible for some alterations in skeletal muscle metabolism, and these possibilities are discussed.

  • 2.
    Durrant, Christelle
    et al.
    Université de Paris, France.
    Fuehring, Jana I
    Hannover Medical School, Germany.
    Willemetz, Alexandra
    Université de Paris, France.
    Chrétien, Dominique
    Université Paris Decartes, Sorbonnes Paris Cité, Institut Imagine, France.
    Sala, Giusy
    University of Milan, Italy.
    Ghidoni, Riccardo
    University of Milan, Italy.
    Katz, Abram
    Karolinska institutet, Stockholm, Sweden.
    Rötig, Agnès
    Université Paris Decartes, Sorbonnes Paris Cité, Institut Imagine, France.
    Thelestam, Monica
    Karolinska institutet, Stockholm, Sweden.
    Ermonval, Myriam
    Institut Pasteur, Department of Virology, Paris, France.
    Moore, Stuart E H
    Université de Paris, France.
    Defects in Galactose Metabolism and Glycoconjugate Biosynthesis in a UDP-Glucose Pyrophosphorylase-Deficient Cell Line Are Reversed by Adding Galactose to the Growth Medium.2020In: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 21, no 6, article id E2028Article in journal (Refereed)
    Abstract [en]

    UDP-glucose (UDP-Glc) is synthesized by UGP2-encoded UDP-Glc pyrophosphorylase (UGP) and is required for glycoconjugate biosynthesis and galactose metabolism because it is a uridyl donor for galactose-1-P (Gal1P) uridyltransferase. Chinese hamster lung fibroblasts harboring a hypomrphic UGP(G116D) variant display reduced UDP-Glc levels and cannot grow if galactose is the sole carbon source. Here, these cells were cultivated with glucose in either the absence or presence of galactose in order to investigate glycoconjugate biosynthesis and galactose metabolism. The UGP-deficient cells display < 5% control levels of UDP-Glc/UDP-Gal and > 100-fold reduction of [6-3H]galactose incorporation into UDP-[6-3H]galactose, as well as multiple deficits in glycoconjugate biosynthesis. Cultivation of these cells in the presence of galactose leads to partial restoration of UDP-Glc levels, galactose metabolism and glycoconjugate biosynthesis. The Vmax for recombinant human UGP(G116D) with Glc1P is 2000-fold less than that of the wild-type protein, and UGP(G116D) displayed a mildly elevated Km for Glc1P, but no activity of the mutant enzyme towards Gal1P was detectable. To conclude, although the mechanism behind UDP-Glc/Gal production in the UGP-deficient cells remains to be determined, the capacity of this cell line to change its glycosylation status as a function of extracellular galactose makes it a useful, reversible model with which to study different aspects of galactose metabolism and glycoconjugate biosynthesis.

  • 3. Korten, Slobodanka
    et al.
    Albet-Torres, Nuria
    Paderi, Francesca
    ten Siethoff, Lasse
    Linneuniversitetet.
    Diez, Stefan
    Korten, Till
    te Kronnie, Geertruy
    Månsson, Alf
    Sample solution constraints on motor-driven diagnostic nanodevices2013In: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 13, no 5, p. 866-876Article in journal (Refereed)
    Abstract [en]

    The last decade has seen appreciable advancements in efforts towards increased portability of lab-on-a-chip devices by substituting microfluidics with molecular motor-based transportation. As of now, first proof-of-principle devices have analyzed protein mixtures of low complexity, such as target protein molecules in buffer solutions optimized for molecular motor performance. However, in a diagnostic workup, lab-on-a-chip devices need to be compatible with complex biological samples. While it has been shown that such samples do not interfere with crucial steps in molecular diagnostics (for example antibody-antigen recognition), their effect on molecular motors is unknown. This critical and long overlooked issue is addressed here. In particular, we studied the effects of blood, cell lysates and solutions containing genomic DNA extracts on actomyosin and kinesin-microtubule-based transport, the two biomolecular motor systems that are most promising for lab-on-a-chip applications. We found that motor function is well preserved at defined dilutions of most of the investigated biological samples and demonstrated a molecular motor-driven label-free blood type test. Our results support the feasibility of molecular-motor driven nanodevices for diagnostic point-of-care applications and also demonstrate important constraints imposed by sample composition and device design that apply both to kinesin-microtubule and actomyosin driven applications.

  • 4. Kumar, Saroj
    et al.
    ten Siethoff, Lasse
    Linnéuniversitetet.
    Persson, Malin
    Lard, Mercy
    Kronnie, Geertruy Te
    Linke, Heiner
    Månsson, Alf
    Antibodies Covalently Immobilized on Actin Filaments for Fast Myosin Driven Analyte Transport2012In: PLOS ONE, E-ISSN 1932-6203, Vol. 7, no 10, article id e46298Article in journal (Refereed)
    Abstract [en]

    Biosensors would benefit from further miniaturization, increased detection rate and independence from external pumps and other bulky equipment. Whereas transportation systems built around molecular motors and cytoskeletal filaments hold significant promise in the latter regard, recent proof-of-principle devices based on the microtubule-kinesin motor system have not matched the speed of existing methods. An attractive solution to overcome this limitation would be the use of myosin driven propulsion of actin filaments which offers motility one order of magnitude faster than the kinesin-microtubule system. Here, we realized a necessary requirement for the use of the actomyosin system in biosensing devices, namely covalent attachment of antibodies to actin filaments using heterobifunctional cross-linkers. We also demonstrated consistent and rapid myosin II driven transport where velocity and the fraction of motile actin filaments was negligibly affected by the presence of antibody-antigen complexes at rather high density (&gt;20 mu m(-1)). The results, however, also demonstrated that it was challenging to consistently achieve high density of functional antibodies along the actin filament, and optimization of the covalent coupling procedure to increase labeling density should be a major focus for future work. Despite the remaining challenges, the reported advances are important steps towards considerably faster nanoseparation than shown for previous molecular motor based devices, and enhanced miniaturization because of high bending flexibility of actin filaments.

  • 5. Lard, Mercy
    et al.
    ten Siethoff, Lasse
    Linneuniversitetet.
    Generosi, Johanna
    Persson, Malin
    Linke, Heiner
    Månsson, Alf
    Nanowire-Imposed Geometrical Control in Studies of Actomyosin Motor Function2015In: IEEE Transactions on Nanobioscience, ISSN 1536-1241, E-ISSN 1558-2639, Vol. 14, no 3, p. 289-297Article in journal (Refereed)
    Abstract [en]

    Recently, molecular motor gliding assays with actin and myosin from muscle have been realized on semiconductor nanowires coated with Al2O3. This opens for unique nanotechnological applications and novel fundamental studies of actomyosin motor function. Here, we provide a comparison of myosin-driven actin filament motility on Al2O3 to both nitrocellulose and trimethylchlorosilane derivatized surfaces. We also show that actomyosin motility on the less than 200 nm wide tips of arrays of Al2O3-coated nanowires can be used to control the number, and density, of myosin-actin attachment points. Results obtained using nanowire arrays with different inter-wire spacing are consistent with the idea that the actin filament sliding velocity is determined both by the total number and the average density of attached myosin heads along the actin filament. Further, the results are consistent with buckling of long myosin-free segments of the filaments as a factor underlying reduced velocity. On the other hand, the findings do not support a mechanistic role in decreasing velocity, of increased nearest neighbor distance between available myosin heads. Our results open up for more advanced studies that may use nanowire-based structures for fundamental investigations of molecular motors, including the possibility to create a nanowire-templated bottom-up assembly of 3D, muscle-like structures.

  • 6. Lard, Mercy
    et al.
    ten Siethoff, Lasse
    Linneuniversitetet.
    Kumar, Saroj
    Persson, Malin
    te Kronnie, Geertruy
    Linke, Heiner
    Månsson, Alf
    Ultrafast molecular motor driven nanoseparation and biosensing2013In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 48, p. 145-152Article in journal (Refereed)
    Abstract [en]

    Portable biosensor systems would benefit from reduced dependency on external power supplies as well as from further miniaturization and increased detection rate. Systems built around self-propelled biological molecular motors and cytoskeletal filaments hold significant promise in these regards as they are built from nanoscale components that enable nanoseparation independent of fluidic pumping. Previously reported microtubule-kinesin based devices are slow, however, compared to several existing biosensor systems. Here we demonstrate that this speed limitation can be overcome by using the faster actomyosin motor system. Moreover, due to lower flexural rigidity of the actin filaments, smaller features can be achieved compared to microtubule-based systems, enabling further miniaturization. Using a device designed through optimization by Monte Carlo simulations, we demonstrate extensive myosin driven enrichment of actin filaments on a detector area of less than 10 μm2, with a concentration half-time of approximately 40 s. We also show accumulation of model analyte (streptavidin at nanomolar concentration in nanoliter effective volume) detecting increased fluorescence intensity within seconds after initiation of motor-driven transportation from capture regions. We discuss further optimizations of the system and incorporation into a complete biosensing workflow.

  • 7. Lard, Mercy
    et al.
    ten Siethoff, Lasse
    Linneuniversitetet.
    Månsson, Alf
    Linke, Heiner
    Tracking Actomyosin at Fluorescence Check Points2013In: Scientific Reports, E-ISSN 2045-2322, Vol. 3, article id 1092Article in journal (Refereed)
    Abstract [en]

    Emerging concepts for on-chip biotechnologies aim to replace microfluidic flow by active, molecular-motor driven transport of cytoskeletal filaments, including applications in bio-simulation, biocomputation, diagnostics, and drug screening. Many of these applications require reliable detection, with minimal data acquisition, of filaments at many, local checkpoints in a device consisting of a potentially complex network of channels that guide filament motion. Here we develop such a detection system using actomyosin motility. Detection points consist of pairs of gold lines running perpendicular to nanochannels that guide motion of fluorescent actin filaments. Fluorescence interference contrast (FLIC) is used to locally enhance the signal at the gold lines. A cross-correlation method is used to suppress errors, allowing reliable detection of single or multiple filaments. Optimal device design parameters are discussed. The results open for automatic read-out of filament count and velocity in high-throughput motility assays, helping establish the viability of active, motor-driven on-chip applications.

  • 8. Månsson, Alf
    et al.
    ten Siethoff, Lasse
    Linneuniversitetet.
    Lard, Mercy
    Generosi, Johanna
    Andersson, Håkan S.
    Linke, Heiner
    Three-Dimensionally Constrained Actomyosin Motility on Oxide Coated Semiconductor Nanowires2014In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 106, no 2, p. 453A-453AArticle in journal (Other academic)
  • 9. Persson, Malin
    et al.
    Bengtsson, Elina
    ten Siethoff, Lasse
    Linneuniversitetet.
    Månsson, Alf
    Non-Linear Cross-Bridge Elasticity, ATP-Independent Detachment and ATP-Velocity Relationships for Skeletal Muscle Actomyosin2014In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 106, no 2, p. 158A-158AArticle in journal (Other academic)
  • 10.
    Põlajeva, Jelena
    et al.
    Uppsala universitet, Cancer och vaskulärbiologi.
    Swartling, Fredrik
    Uppsala universitet, Cancer och vaskulärbiologi.
    Jiang, Yiwen
    Uppsala universitet, Cancer och vaskulärbiologi.
    Singh, Umashankar
    Uppsala universitet, Cancer och vaskulärbiologi.
    Pietras, Kristian
    Department of Medical Biochemistry and Biophysics, Karolinska Institutet.
    Uhrbom, Lene
    Uppsala universitet, Cancer och vaskulärbiologi.
    Westermark, Bengt
    Uppsala universitet, Cancer och vaskulärbiologi.
    Roswall, Pernilla
    Uppsala universitet, Institutionen för immunologi, genetik och patologi.
    miRNA-21 is developmentally regulated in mouse brain and is co-expressed with SOX2 in glioma2012In: BMC Cancer, ISSN 1471-2407, E-ISSN 1471-2407, Vol. 12, p. 378-Article in journal (Refereed)
    Abstract [en]

    Background

    MicroRNAs (miRNAs) and their role during tumor development have been studied in greatdetail during the last decade, albeit their expression pattern and regulation during normaldevelopment are however not so well established. Previous studies have shown that miRNAsare differentially expressed in solid human tumors. Platelet-derived growth factor (PDGF)signaling is known to be involved in normal development of the brain as well as in malignantprimary brain tumors, gliomas, but the complete mechanism is still lacking. We decided toinvestigate the expression of the oncogenic miR-21 during normal mouse development andglioma, focusing on PDGF signaling as a potential regulator of miR-21.

    Methods

    We generated mouse glioma using the RCAS/tv-a system for driving PDGF-BB expression ina cell-specific manner. Expression of miR-21 in mouse cell cultures and mouse brain wereassessed using Northern blot analysis and in situ hybridization. Immunohistochemistry andWestern blot analysis were used to investigate SOX2 expression. LNA-modified siRNA wasused for irreversible depletion of miR-21. For inhibition of PDGF signaling Gleevec(imatinib mesylate), Rapamycin and U0126, as well as siRNA were used. Statisticalsignificance was calculated using double-sided unpaired Student´s t-test.

    Results

    We identified miR-21 to be highly expressed during embryonic and newborn braindevelopment followed by a gradual decrease until undetectable at postnatal day 7 (P7), thiscorrelated with SOX2 expression. Furthermore, miR-21 and SOX2 showed up-regulation andoverlapping expression pattern in RCAS/tv-a generated mouse brain tumor specimens. Uponirreversible depletion of miR-21 the expression of SOX2 was strongly diminished in bothmouse primary glioma cultures and human glioma cell lines. Interestingly, in normalfibroblasts the expression of miR-21 was induced by PDGF-BB, and inhibition of PDGFsignaling in mouse glioma primary cultures resulted in suppression of miR-21 suggesting thatmiR-21 is indeed regulated by PDGF signaling.

    Conclusions

    Our data show that miR-21 and SOX2 are tightly regulated already during embryogenesisand define a distinct population with putative tumor cell of origin characteristics. We believethat miR-21 is a mediator of PDGF-driven brain tumors, which suggests miR-21 as apromising target for treatment of glioma.

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