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  • 1.
    Larsson, Dennis
    et al.
    Högskolan i Skövde, Institutionen för vård och natur.
    Anderson, Deryk
    Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT, United States / Kansas City University of Medicine and Biosciences, Kansas City, MO, United States.
    Smith, Nathan M.
    Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT, United States.
    Nemere, Ilka
    Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT, United States / Department of Nutrition and Food Sciences, Utah State University, Logan, UT, United States.
    24,25-Dihydroxyvitamin D3 binds to catalase2006In: Journal of Cellular Biochemistry, ISSN 0730-2312, E-ISSN 1097-4644, Vol. 97, no 6, p. 1259-1266Article in journal (Refereed)
    Abstract [en]

    There is increasing evidence that the vitamin D metabolite, 24,25-dihydroxyvitamin D3 (24,25(OH)2D3) has endocrine actions. In the current work, we report that an endogenous binding protein for 24,25(OH)2D3 is catalase, based on sequence analysis of the isolated protein. An antibody (Ab 365) generated against equivalent protein recognized bovine catalase and a 64 kDa band in subcellular fractions of chick intestine. A commercially available anti-catalase antibody reduced specific [3H]24,25(OH)2D3 binding in subcellular fractions of chick intestine by greater than 65%, relative to the same fractions treated with an unrelated antibody (Ab 099). The same commercially available anti-catalase was able to block the inhibitory actions of 24,25(OH)2D3 on 32P uptake in isolated intestinal epithelial cell suspensions. We subsequently characterized binding of steroid to commercially available catalase, and found that between 0 and 5 nM of enzyme added to subcellular fraction P2 (20,000g, 10-min post-nuclear pellet) resulted in a linear increase in the amount of [3H]24,25(OH)2D3 specifically bound. Additional studies indicated that 25(OH)D3 was an effective competitor for binding, whereas 1,25(OH)2D3 only poorly displaced [3H]24,25(OH)2D3. Saturation analyses with added catalase yielded a physiologically relevant affinity constant (KD = 5.6 ± 2.7 nM) and a Bmax = 209 ± 34 fmols/mg protein, comparable to previous studies using purified basal lateral membranes or vesicular fractions. Moreover, in a study on subcellular fractions isolated from chickens of varying ages, we found that in females, both specific [3H]24,25(OH)2D3 binding and catalase activity increased from 7- to 58-week-old birds, whereas in males, elevated levels of both parameters were expressed in preparations of 7- and 58-week-old birds. The data suggest that signal transduction may occur through modulation of hydrogen peroxide production.

  • 2.
    Sogaard, Peter
    et al.
    Högskolan i Skövde, Forskningscentrum för Systembiologi.
    Szekeres, Ferenc
    Karolinska Institutet.
    Garcia-Roves, Pablo M.
    Karolinska Institutet.
    Larsson, Dennis
    Högskolan i Skövde, Forskningscentrum för Systembiologi.
    Chibalin, Alexander V.
    Karolinska Institutet.
    Zierath, Juleen R.
    Karolinska Institutet.
    Spatial Insulin Signalling in Isolated Skeletal Muscle Preparations2010In: Journal of Cellular Biochemistry, ISSN 0730-2312, E-ISSN 1097-4644, Vol. 109, no 5, p. 943-949Article in journal (Refereed)
    Abstract [en]

    During in vitro incubation in the absence or presence of insulin, glycogen depletion occurs in the inner core of the muscle specimen, concomitant with increased staining of hypoxia-induced-factor-1-alpha and caspase-3, markers of hypoxia and apoptosis, respectively. The aim of this study was to determine whether insulin is able to diffuse across the entire muscle specimen in sufficient amounts to activate signalling cascades to promote glucose uptake and glycogenesis within isolated mouse skeletal muscle. Phosphoprotein multiplex assay on lysates from muscle preparation was performed to detect phosphorylation of insulin-receptor on Tyr1146, Akt on Ser473 and glycogen-synthases-kinase-3 on Ser21/Ser9. To address the spatial resolution of insulin signalling, immunohistochemistry studies on cryosections were performed. Our results provide evidence to suggest that during the in vitro incubation, insulin sufficiently diffuses into the centre of tubular mouse muscles to promote phosphorylation of these signalling events. Interestingly, increased insulin signalling was observed in the core of the incubated muscle specimens, correlating with the location of oxidative fibres. In conclusion, insulin action was not restricted due to insufficient diffusion of the hormone during in vitro incubation in either extensor digitorum longus or soleus muscles from mouse under the specific experimental settings employed in this study. Hence, we suggest that the glycogen depleted core as earlier observed is not due to insufficient insulin action.

  • 3.
    Sögaard, Peter
    et al.
    Högskolan i Skövde, Forskningscentrum för Systembiologi.
    Szekeres, Ferenc
    Department of Molecular Medicine and Surgery, Section og Integrative Physiology, Karolinska Institutet.
    Holmström, Maria
    Department of Molecular Medicine and Surgery, Section of Integrative Physiology, Karolinska Institutet.
    Larsson, Dennis
    Högskolan i Skövde, Forskningscentrum för Systembiologi.
    Harlén, Mikael
    Högskolan i Skövde, Forskningscentrum för Systembiologi.
    Garcia-Roves, Pablo
    Section of Integrative Physiology, Department of Physiology and Pharmacology, Karolinska Institutet.
    Chibalin, Alexander V.
    Department of Molecular Medicine and Surgery, Section of Integrative Physiology, Karolinska Institutet.
    Effects of fibre type and diffusion distance on mouse skeletal muscle glycogen content in vitro2009In: Journal of Cellular Biochemistry, ISSN 0730-2312, E-ISSN 1097-4644, Vol. 107, no 6, p. 1189-1197Article in journal (Refereed)
    Abstract [en]

    In vitro incubation of isolated rodent skeletal muscle is a widely used procedure in metabolic research. One concern with this method is the development of an anoxic state during the incubation period that can cause muscle glycogen depletion. Our aim was to investigate whether in vitro incubation conditions influence glycogen concentration in glycolytic extensor digitorum longus (EDL) and oxidative soleus mouse muscle. Quantitative immunohistochemistry was applied to assess glycogen content in incubated skeletal muscle. Glycogen concentration was depleted, independent of insulin-stimulation in the incubated skeletal muscle. The extent of glycogen depletion was correlated with the oxidative fibre distribution and with the induction of hypoxia-induced-factor-1-alpha. Insulin exposure partially prevented glycogen depletion in soleus, but not in EDL muscle, providing evidence that glucose diffusion is not a limiting step to maintain glycogen content. Our results provide evidence to suggest that the anoxic milieu and the intrinsic characteristics of the skeletal muscle fibre type play a major role in inducing glycogen depletion in during in vitro incubations.

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