Insulin-Like Growth Factor-I Increases Laminin, Integrin Subunits and Metalloprotease ADAM12 in Mouse Myoblasts

Grzelkowska-Kowalczyk, Katarzyna; Grabiec, Kamil; Tokarska, J.; Gajewska, Małgorzata; Błaszczyk, Maciej; Milewska, Magdalena

doi:10.3409/fb63_4.241

Cited by 5 publications

(7 citation statements)

References 19 publications

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“…In myoblasts subjected to differentiation in vitro, fibronectin is detected primarily in the extracellular environment as a thick mesh. At the same time, laminin appears ultimately in the cytosolic fraction, which confirms delayed synthesis of this protein during myogenesis, in comparison to fibronectin [29]. During myogenic differentiation, the laminin synthesis increases, and laminin begins to accumulate in the medium in soluble form, followed by the formation of insoluble cell-associated fraction [30].…”

Section: Changes In Ecm Assembly and Function During Myogenesismentioning

confidence: 58%

“…A critical phase of myogenesis is the fusion of mononucleated myoblasts and the formation of long multinucleated myotubes. Myoblast fusion and myotube formation are associated with increased expression of integrin alpha3, particularly abundant in myotube membrane [29]. Overexpression of the full-length integrin alpha3 subunit induces myoblast fusion, whereas the inhibition of integrin alpha3 extracellular domain impairs this process [33].…”

Section: Changes In Ecm Assembly and Function During Myogenesismentioning

confidence: 99%

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The Importance of Extracellular Matrix in Skeletal Muscle Development and Function

Grzelkowska-Kowalczyk¹

2016

Composition and Function of the Extracellular Matrix in the Human Body

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Skeletal muscle tissue makes up approximately 40% of the total body mass in adult mammals. Contractile muscle fibers building skeletal muscle tissue are coated by an extracellular matrix material (ECM), accounting for 1-10% of the muscle mass. The ECM in skeletal muscle was initially considered as a structure, providing mechanical support for bearing force transmission. Now it is evident that muscle cells adhere to and connect with the ECM, also for signaling, and the ECM provides an appropriate and permissive environment for muscle development and functioning. This chapter summarizes current knowledge on the role of ECM components in skeletal muscle growth and regeneration, which is of great importance for potential therapeutic interventions. It also focuses on the contribution of ECM in the motor function of skeletal muscle as well as on mechanisms mediating muscle ECM remodeling during adaptation to physical activity. The role of the ECM in the metabolic function of skeletal muscle tissue and the ECM disturbances associated with insulin resistance are described. Finally, the attention is paid on potential implications of changes in skeletal muscle ECM assembly and function in health and disease.

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Section: Changes In Ecm Assembly and Function During Myogenesismentioning

confidence: 58%

Section: Changes In Ecm Assembly and Function During Myogenesismentioning

confidence: 99%

The Importance of Extracellular Matrix in Skeletal Muscle Development and Function

Grzelkowska-Kowalczyk¹

2016

Composition and Function of the Extracellular Matrix in the Human Body

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“…Apparently, ADAM12-cytoskeleton interactions, and, in turn, ADAM12 breakdown are diminished in the presence of TNF-α, that is in line with increased cellular level of the metalloprotease under cytokine treatment. In our previous study a long 100 kDa isoform of ADAM12 was increased in myoblasts differentiating for 3 days in the presence of IL-1β (Grabiec et al 2013) and IGF-I (Grzelkowska- Kowalczyk et al 2015), suggesting similar effects of proinflammatory cytokines and anabolic growth factors on early stages of myogenesis.…”

Section: Discussionmentioning

confidence: 99%

Tumor necrosis factor-α alters integrins and metalloprotease ADAM12 levels and signaling in differentiating myoblasts

Grzelkowska-Kowalczyk¹,

Tokarska²,

Grabiec³

et al. 2016

Polish Journal of Veterinary Sciences

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The extracellular matrix (ECM) is important in the regulation of myogenesis. We hypothesized that tumor necrosis factor-α (TNF-α) modifies ECM during differentiation of mouse C2C12 myoblasts. Exogenous TNF-α (1 ng/ml) stimulated myoblast fusion on the 3 rd day (by 160% vs control) but not on the 5 th day of myogenesis. The level of integrin α5 was significantly augmented by TNF-α during 5 day-differentiation; however, integrin β1 was higher than control only on the 3 rd day of cytokine treatment. Both the abundance of integrin α5 bound to actin and the level of integrin β1 complexed with integrin α5 increased in the presence of TNF-α, especially on the 3 rd day of differentiation. Similarly, the stimulatory effects of TNF-α on integrin α3, metalloprotease ADAM12 and kinases related to integrins, FAK and ILK, were limited to the 3 rd day of differentiation. We concluded that TNF-α-induced changes in ECM components in differentiating myogenic cells, i.e. i) increased expression of integrin α5, β1, α3, and metalloprotease ADAM12, ii) enhanced formation of α5β1 integrin receptors and interaction of integrin α5-cytoskeleton, and iii) increased expression of kinases associated with integrin signaling, FAK and ILK, were temporarily associated with the onset of myocyte fusion.

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“…Control and cytokine-treated adipocytes were stimulated with 100 nmol/l insulin for 30 min (Woody et al, 2013), then fixed with 3.7% paraformaldehyde and permeabilized with 0.05% Triton X-100 in PBS. To visualize cellular profiles of Rab4a fluorescence lines were drawn on cell images and the fluorescence distribution was estimated along with these lines, as described previously (Grzelkowska-Kowalczyk et al, 2015). The cells were visualized by confocal laser scanning microscope FV-500 system (Olympus Optical Co, Hamburg, Germany).…”

Section: Immunofluorescence and Confocal Microscopymentioning

confidence: 99%

“…Ten independent fields from control and experimentally-treated cells were photographed and the intensity of fluorescence was measured using the MicroImage analysis system (Olympus Optical Poland). To visualize cellular profiles of Rab4a fluorescence lines were drawn on cell images and the fluorescence distribution was estimated along with these lines, as described previously (Grzelkowska-Kowalczyk et al, 2015). The Rab4a fluorescence (green) sharing the same range of linear profile with 7-AAD fluorescence (red) was considered as cytoplasmic near-nuclear fluorescence.…”

Section: Immunofluorescence and Confocal Microscopymentioning

confidence: 99%

Insulin‐dependent cytoplasmic distribution of Rab4a in mouse adipocytes is inhibited by interleukin‐6, ‐8, and ‐15

Błaszczyk

Gajewska

Milewska

et al. 2017

Cell Biology International

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The purpose of the study was to examine the effect of interleukins, IL-6, IL-8, and IL-15, on insulin-mediated redistribution of Rab4a, an early endosome marker, in mouse 3T3-L1 adipocytes. The interleukins did not affect cell viability; however, cell number was slightly but significantly higher in cultures exposed to IL-8 and IL-15. IL-8 and IL-15 decreased lipid storage in adipocytes, whereas IL-6 had no effect. Rab4A showed cytoplasmic localization, and in control unstimulated adipocytes it was found primarily nearby nucleus, that was supported by cellular fluorescence distribution profile, and by calculated indices, that is, high percentage of near-nuclear area fluorescence and a low mean peripheral cytoplasmic fluorescence/mean near-nuclear fluorescence ratio. Insulin stimulation (100 nmol/l, 30 min) altered the cytoplasmic localization of Rab4a in control adipocytes, which was manifested by its redistribution towards plasma membrane. This effect of insulin was prevented in adipocytes exposed to IL-6, IL-8, or IL-15. We concluded that insulin-dependent Rab4a redistribution, probably reflecting stimulation of vesicle-mediated transport, is inhibited in adipocytes subjected to differentiation in the presence of IL-6, IL-8, or IL-15. Such alterations may be involved in the mechanisms contributing to development of insulin resistance associated with inflammation; however, further studies in this field are required.

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Insulin-Like Growth Factor-I Increases Laminin, Integrin Subunits and Metalloprotease ADAM12 in Mouse Myoblasts

Cited by 5 publications

References 19 publications

The Importance of Extracellular Matrix in Skeletal Muscle Development and Function

The Importance of Extracellular Matrix in Skeletal Muscle Development and Function

Tumor necrosis factor-α alters integrins and metalloprotease ADAM12 levels and signaling in differentiating myoblasts

Insulin‐dependent cytoplasmic distribution of Rab4a in mouse adipocytes is inhibited by interleukin‐6, ‐8, and ‐15

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