Results 31 to 40 of about 3,043 (170)

Reduced PGC-1β protein expression may underlie corticosterone inhibition of mitochondrial biogenesis and oxidative phosphorylation in chicken muscles

Frontiers in Physiology, 2022
To uncover the molecular mechanism underlying glucocorticoid-induced loss of mitochondrial integrity in skeletal muscles, studies were performed to investigate whether the peroxisome proliferator-activated receptor γ coactivator 1 (PGC-1)-mediated ...
Sheng Li, Zhi Wang, Jing Wen Yao, Hong Chao Jiao, Xiao Juan Wang, Hai Lin, Jing Peng Zhao   +6 more
doaj   +1 more source

An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix. [PDF]

, 1995
Agrin is an extracellular matrix (ECM) protein with a calculated relative molecular mass of more than 200 kD that induces the aggregation of acetylcholine receptors (AChRs) at the neuromuscular junction. This activity has been mapped to its COOH terminus.
Ruegg, M. A., A J Denzer, B Schumacher, Denzer, A J, M A Ruegg, Gesemann, M., Schumacher, B, M Gesemann, Schumacher, B., Gesemann, M, Ruegg, M A, Denzer, A. J.   +11 more
core   +1 more source

Accumulation of muscle ankyrin repeat protein transcript reveals local activation of primary myotube endcompartments during muscle morphogenesis [PDF]

, 1997
The characteristic shapes and positions of each individual body muscle are established during the process of muscle morphogenesis in response to patterning information from the surrounding mesenchyme. Throughout muscle morphogenesis, primary myotubes are
Arber, S., Baumeister, A., Pico Caroni, Caroni, P., Anja Baumeister, Silvia Arber   +5 more
core   +1 more source

Agrin binds to the nerve-muscle basal lamina via laminin. [PDF]

, 1997
Agrin is a heparan sulfate proteoglycan that is required for the formation and maintenance of neuromuscular junctions. During development, agrin is secreted from motor neurons to trigger the local aggregation of acetylcholine receptors (AChRs) and other ...
Brandenberger, R, Ralph Brandenberger, Matthias Gesemann, Gesemann, M., Denzer, A. J., Chiquet, M, Ruegg, M. A., Denzer, A J, Brandenberger, R., Markus A. Ruegg, Matthias Chiquet, Gesemann, M, Ruegg, M A, Chiquet, M., Alain J. Denzer   +14 more
core   +1 more source

The regenerative plasticity of isolated urodele myofibers and its dependence on Msx1 [PDF]

, 2004
The conversion of multinucleate postmitotic muscle fibers to dividing mononucleate progeny cells (cellularisation) occurs during limb regeneration in salamanders, but the cellular events and molecular regulation underlying this remarkable process are not
Brockes, J.P., Cristiana P Velloso, Cristiana P Velloso (56684), Kumar, A, Yutaka Imokawa (46), Brockes, JP, Imokawa, Y., Kumar, A., Imokawa, Y, Velloso Cristiana P, Anoop Kumar, Jeremy P Brockes, Jeremy P Brockes (56685), Velloso, Cristiana, Velloso, CP, Brockes Jeremy P, Yutaka Imokawa, Anoop Kumar (44), Velloso, C.P., Kumar Anoop, Imokawa Yutaka, Brockes, J.P   +21 more
core   +1 more source

Myofibrillar Proteolysis in Chick Myotubes during Oxidative Stress

Journal of Nutritional Science and Vitaminology, 2004
Changes in protein conformation and proteolysis in chick myotubes in response to the induction of oxidative stress by H2O2 treatment were studied. Myotubes were treated for 1 h with H2O2. After this treatment, the H2O2 was removed and the cells were cultured in serum-free medium for 6 and 24 h.
NAKASHIMA, Kazuki, NONAKA, Itoko, MASAKI, Shigehiko   +2 more
openaire   +3 more sources

Cysteine Suppresses Oxidative Stress-Induced Myofibrillar Proteolysis in Chick Myotubes [PDF]

Bioscience, Biotechnology, and Biochemistry, 2004
The effects of cysteine as an antioxidant nutrient on change in protein modification and myofibrillar proteolysis in chick myotubes by induction of oxidative stress by H(2)O(2) treatment were investigated. Myotubes were treated for 1 h with H(2)O(2) (1 mM).
NAKASHIMA, Kazuki, MASAKI, Shigehiko, YAMAZAKI, Makoto, ABE, Hiroyuki   +3 more
openaire   +2 more sources

Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site. [PDF]

, 1995
Agrin is a basal lamina protein that induces aggregation of acetylcholine receptors (AChRs) and other molecules at the developing neuromuscular junction.
Ruegg, M. A., A J Denzer, Denzer, A J, M A Ruegg, Gesemann, M., M Gesemann, Gesemann, M, Ruegg, M A, Denzer, A. J.   +8 more
core   +1 more source

cDNA that encodes active agrin [PDF]

, 1992
Agrin is thought to mediate the motor neuron-induced aggregation of AChRs and AChE on the surface of muscle fibers at neuromuscular junctions. We have isolated a cDNA from a chick brain library that, based on sequence homology and expression experiments,
Kröger, Stephan, Tsim, K. W., McMahan, U. J., Ruegg, M. A., Escher, G., Tsim, Karl W. K., Ruegg, Markus A., Escher, Gérard, Tsim, Karl W.K., Kroger, S.   +9 more
core   +1 more source

Permeability properties of chick myotube acetylcholine-activated channels

Biophysical Journal, 1984
The acetylcholine-(ACh-)activated channels of chick myotubes were studied by the patch-clamp method. Single-channel amplitudes were measured over a wide range of potentials in solutions of cesium, arginine, and three small amines. Symmetrical, isotonic cesium solutions gave a linear I-V relationship with the single-channel conductance, gamma, of 42 pS ...
Dwyer, T.M., Farley, J.M.
openaire   +2 more sources