Aspects of normal and dystrophic chicken muscle grown in vitro

1979 ◽  
Vol 31 (1) ◽  
pp. 243-250 ◽  
Author(s):  
E. Raworth Allen ◽  
James F. May
Keyword(s):  
Chicken Muscle ◽  
Dystrophic Chicken

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Biochemistry ◽  
1988 ◽  
Vol 27 (19) ◽  
pp. 7519-7524 ◽  
Author(s):  
Jose Galindo ◽  
Michael S. Hudecki ◽  
Faith B. Davis ◽  
Paul J. Davis ◽  
Harshad R. Thacore ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Calcium Atpase ◽  
Muscle Membrane ◽  
Chicken Muscle ◽  
Abnormal Response ◽  
Dystrophic Chicken

Suppression of myotonia in dystrophic chicken muscle by phenytoin

1979 ◽  
Vol 237 (3) ◽  
pp. C131-C136 ◽  
Author(s):  
R. K. Entrikin ◽  
S. H. Bryant
Keyword(s):  
Direct Action ◽  
Repetitive Firing ◽  
Electromyographic Activity ◽  
Direct Stimulation ◽  
Chicken Muscle ◽  
Chicken Muscles ◽  
In Vivo Effects ◽  
Dystrophic Chicken

We describe myotonic electromyographic activity in muscles of genetically dystrophic chickens and show that this activity is antagonized in vivo by doses of phenytoin (DPH) that improve righting ability. To test the possibility that the in vivo effects of DPH can be accounted for by a direct action on skeletal muscle we studied posterior latissimus dorsi fibers in vitro at 23 degrees C with intracellular microelectrodes. Compared to normal fibers, fibers from untreated dystrophic chicks had larger diameters, increased membrane capacitance, longer latencies at rheobase, and a greater tendency to fire repetitively in response to direct stimulation. DPH (10 or 50 micrograms/ml in the bath solution) decreased latencies at rheobase and repetitive firing in fibers from untreated chicks. In DPH-free solution fibers from dystrophic chicks treated chronically with DPH were still abnormal with respect to latencies at rheobase and ease of repetitive firing. The data support the hypothesis that abnormalities of membrane electrical properties are major features of dystrophic chicken muscles and furthermore, show that DPH suppresses, but does not abolish, these abnormalities.

Precocious in vitro development of satellite cells from dystrophic chicken muscle

In Vitro ◽  
1983 ◽  
Vol 19 (9) ◽  
pp. 723-729 ◽  
Author(s):  
D. D. Johnson ◽  
R. Wilcox ◽  
B. Wenger
Keyword(s):  
Satellite Cells ◽  
In Vitro Development ◽  
Chicken Muscle ◽  
Vitro Development ◽  
Dystrophic Chicken

scholarly journals PROPERTIES OF THE CAUSATIVE AGENT OF A CHICKEN TUMOR

1929 ◽  
Vol 50 (3) ◽  
pp. 315-326 ◽  
Author(s):  
F. Duran-Reynals ◽  
James B. Murphy
Keyword(s):  
Muscle Tissue ◽  
Causative Agent ◽  
Chicken Muscle

Ground muscle from susceptible chickens fixes in vitro in a proportion of instances the agent of the filterable Chicken Tumor I, and in a lesser degree inactivates it, whereas the muscle from resistant animals such as rabbit and pigeon, is without effect. It is shown that the power of fixation of the chicken muscle is far greater than its inactivating properties. Brain and liver from chicken, rabbit and pigeon seem devoid of any action on the agent. The desiccated chicken muscle tissue shares the properties of the fresh organ; and the process of desiccation does not release the agent from the inactive or slightly active mixture of fresh muscle and filtrate.

scholarly journals Contractile activity is required for the expression of neonatal myosin heavy chain in embryonic chick pectoral muscle cultures.

1986 ◽  
Vol 103 (6) ◽  
pp. 2153-2161 ◽  
Author(s):  
L C Cerny ◽  
E Bandman
Keyword(s):  
Monoclonal Antibody ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Contractile Activity ◽  
Pectoral Muscle ◽  
Chicken Muscle ◽  
High K ◽  
Muscle Cultures ◽  
Spontaneous Contractions

The expression of neonatal myosin heavy chain (MHC) was examined in developing embryonic chicken muscle cultures using a monoclonal antibody (2E9) that has been shown to be specific for that isoform (Bandman, E., 1985, Science (Wash. DC), 227: 780-782). After 1 wk in vitro some myotubes could be stained with the antibody, and the number of cells that reacted with 2E9 increased with time in culture. All myotubes always stained with a second monoclonal antibody that reacted with all MHC isoforms (AG19) or with a third monoclonal antibody that reacted with the embryonic but not the neonatal MHC (EB165). Quantitation by ELISA of an extract from 2-wk cultures demonstrated that the neonatal MHC represented between 10 and 15% of the total myosin. The appearance of the neonatal isoform was inhibited by switching young cultures to medium with a higher [K+] which has been shown to block spontaneous contractions of myotubes in culture. Furthermore, if mature cultures that reacted with the neonatal antibody were placed into high [K+] medium, neonatal MHC disappeared from virtually all myotubes within 3 d. The effect of high [K+] medium was reversible. When cultures maintained in high [K+] medium for 2 wk were placed in standard medium, which permitted the resumption of contractile activity, within 24 h cells began to react with the neonatal specific antibody, and by 72 h many myotubes were strongly positive. Since similar results were also obtained by inhibiting spontaneous contractions with tetrodotoxin, we suggest that the development of contractile activity is not only associated with the maturation of myotubes in culture, but may also be the signal that induces the expression of the neonatal MHC.

Development of the iris in the chicken embryo

Development ◽  
1984 ◽  
Vol 81 (1) ◽  
pp. 169-183
Author(s):  
Patricia A. Ferrari ◽  
William E. Koch
Keyword(s):  
Epithelial Cells ◽  
Chicken Embryo ◽  
Muscle Differentiation ◽  
Muscle Fibres ◽  
Tissue Interactions ◽  
Morphological Organization ◽  
Chicken Muscle ◽  
Muscle Myosin

The developmental capabilities of the iris rudiment in the chicken embryo, as well as the role of tissue interactions in the differentiation of the iris, were investigated in vitro. Sectors of the intact iris from 7½- through 9-day embryos (stages 32 through 35) lost their morphological organization in vitro, but were capable of normal histodifferentiation. The pigmentation of the epithelium increased, and muscle differentiation occurred. Developing muscle was identified using immunocytochemistry with antiserum against chicken muscle myosin; this procedure permitted positive identification of myoblasts, myotubes, and muscle fibres in cultures in which histological features alone were equivocal. The proportion of irideal explants which developed muscle increased with the age of the embryo, and correlated with the incidence of epithelial buds and epithelial cells in the stroma. Irideal mesenchyme from stage-32 through stage-35 embryos was already populated with stromal epithelial cells when isolated, but growth and muscle differentiation in these cultures compared poorly with that in the intact iris in vitro. Isolated irideal epithelium (stages 32 through 37) demonstrated even more limited muscle differentiation in vitro, suggesting reciprocal interaction between irideal epithelium and mesenchyme during development. Irideal epithelium was also cultured in direct association with non-irideal mesenchyme from various embryonic organ rudiments, but muscle differentiation was not enhanced.

Comparative enzymology of 5′-AMP aminohydrolase from normal and genetically dystrophic chicken muscle

1979 ◽  
Vol 21 (3) ◽  
pp. 352-365 ◽  
Author(s):  
Clarence H. Suelter ◽  
Debra Thompson ◽  
Gerard Oakley ◽  
Mary Pearce ◽  
H.David Husic ◽  
...  
Keyword(s):  
Chicken Muscle ◽  
Comparative Enzymology ◽  
Dystrophic Chicken

scholarly journals The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes

1974 ◽  
Vol 143 (1) ◽  
pp. 171-179 ◽  
Author(s):  
Buddha P. Roy
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Chicken Breast ◽  
Thiol Groups ◽  
Dystrophic Muscle ◽  
Muscle Enzymes ◽  
Chicken Muscle ◽  
Dystrophic Chicken

The major14C-labelled peptides from creatine kinase from normal and dystrophic chicken muscle obtained by carboxymethylating the reactive thiol groups with iodo[2-14C]acetic acid and digestion with trypsin were purified by ion-exchange chromatography on Dowex-50 (X2) and by paper electrophoresis. The chromatographic characteristics of the14C-labelled peptides, their electrophoretic mobilities at pH6.5, and their amino acid compositions were identical for the two enzymes. The sequence of amino acids around the essential thiol groups of creatine kinase from normal and dystrophic chicken muscle was shown to be Ile-Leu-Thr-CmCys-Pro-Ser-Asn-Leu-Gly-Thr-Gly-Leu-Arg (CmCys, carboxymethylcysteine). This sequence is almost identical with that for the creatine kinases in human and ox muscle and bovine brain and is very similar to that of arginine kinase from lobster muscle. Antibodies to the enzymes were raised in rabbits and their reaction with the creatine kinase from normal and dystrophic muscles in interfacial, immunodiffusion and immunoelectrophoretic experiments was studied. The cross-reaction between normal muscle creatine kinase and antisera against the dystrophic muscle enzyme (or vice versa) observed by immunodiffusion and by immunoelectrophoretic experiments further suggests that the enzymes from normal and dystrophic chicken muscle are similar in structure. The results of the present study, the identical amino acid sequence of the peptides containing the reactive thiol group from both the normal and dystrophic chicken muscle enzymes and the immunological similarities of the two enzymes are in accord with the similarity of the two enzymes observed by Roy et al. (1970).

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