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1Author    G. TripathiRequires cookie*
 Title    Thyroid Hormone-Induced Changes in Cytoplasmic and Mitochondrial Proteins of a Teleost  
 Abstract    The effect of triiodothyronine (T 3) on the cytoplasmic and mitochondrial protein contents were studied in the liver and skeletal muscle of a freshwater teleost. The fish exposed to thiouracil for 28 days showed 1 .5 -2 times reduction in the total protein contents of cyto­ plasmic and mitochondrial fractions. A single injection of T 3 to thiouracil exposed fish caused 
  Reference    Z. Naturforsch. 53c, 120 (1998); received June 2/Novem ber 18 1997 
  Published    1998 
  Keywords    Triiodothyronine, Protein, Liver, Skeletal Muscle, Fish 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0120.pdf 
 Identifier    ZNC-1998-53c-0120 
 Volume    53 
2Author    G. TripathiRequires cookie*
 Title    Kinetics of Thyroid Hormone Induced Changes in Liver and Skeletal Muscle Enzymes of Clarias batrachus  
 Abstract    Kinetics of triiodothyronine (T 3) induced changes were studied in cytoplasmic malate dehydrogenase (cM DH), mitochondrial malate dehydrogenase (mMDH) and lactate dehydrogenase (LD H) of the liver and skeletal muscle of a catfish, Clarias batrachus. The rates of gradual inductions in the activities of all the three metabolic enzymes were faster in skeletal muscle than those of the liver. These time-dependent and tissue-specific inductions may be due to the possible differ­ ences in the rates of different enzymic syntheses. The maximum inductions in the activities of cMDH, mMDH and LD H were recorded around 19 hr after T 3 treat­ ment. Thereafter, the activities of all the enzymes grad­ ually declined to their half levels within the next 12 hr which reflected the physiological half-life of these meta­ bolic enzymes in the freshwater catfish. 
  Reference    Z. Naturforsch. 54c, 458 (1999); received December 28 1998/March 1 1999 
  Published    1999 
  Keywords    Triiodothyronine, MDH, LDH, Liver, Skeletal Muscle 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0458_n.pdf 
 Identifier    ZNC-1999-54c-0458_n 
 Volume    54 
3Author    AnaR. De Boland, RicardoL. BolandRequires cookie*
 Title    Effects o f Vitamin D 3 on in vivo Labelling o f Chick Skeletal M uscle Proteins with pHJLeucine  
 Abstract    The effects o f the administration o f a single oral dose o f vitamin D 3 to rachitic chicks on the in vivo incorporation o f [3H]leucine to proteins o f skeletal muscle subcellular fractions was studied. A significant stim ulation (50%) o f labelling o f mitochondrial proteins could be seen. The sterol affected the labelling o f sarcoplasmic reticulum (20%) and contractile proteins (10%) to a lesser extent. These results confirm previous observations which im ­ plicate vitamin D 3 in the synthesis o f m itochondrial proteins. 
  Reference    Z. Naturforsch. 39c, 1015—1016 (1984); received April 24 1984 
  Published    1984 
  Keywords    Skeletal Muscle, Mitochondria, [3H]Leucine Labelling, Rickets, Vitamin D 3 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1015_n.pdf 
 Identifier    ZNC-1984-39c-1015_n 
 Volume    39 
4Author    Klaus-Joachim Schott, JochenG. Ehrm Ann, Ulla Potter, V. Olker, N. EuhoffRequires cookie*
 Title    On the Role of Branched-Chain Amino Acids in Protein Turnover of Skeletal Muscle. Studies in vivo with L-Norleucine  
 Abstract    1. The effect of L-norleucine, an isomer of leucine, on protein metabolism in vivo was studied in suckling rats. Rats were injected subcutaneously with various doses of L-norleucine (0.5 and 5.0 jo.mol/g body wt.) every 12 h from 3 to 15 days post partum. Protein concentration, amino acid concentrations, and incorporation of [3H]tyrosine into protein were analyzed in liver, muscles of thigh and small intestine. Amino acid concentrations and insulin levels in serum were also measured. 2. At 5 days of age, norleucine induced an increase in protein concentration of skeletal muscle with an increased incorporation of [3H]tyrosine into protein indicating an accelerated protein synthesis. Changes in protein metabolism were paralleled by alterations in the amino acid pattern of this tissue. 3. When protein concentration and protein synthesis were increased in skeletal muscle, protein concentration of small intestine was decreased, accompanied by elevated levels of amino acids in tissue. Protein synthesis of small intestine was not altered by the norleucine treatment. The results suggest a close interrelationship between skeletal muscle and small intestine with respect to protein turnover. 4. The effects of norleucine were less pronounced at 10 and 15 days of age, which indicates a metabolic adaptation to the treatment. 5. Alterations in amino acid concentrations of tissue due to changes in protein metabolism were not uniform but tissue-specific. 6. Current concepts for explaining the effects of branched-chain amino acids (BCAA) on protein turnover in skeletal muscle are based on the assumption that the BCAA or leucine alone might become rate-limiting for protein synthesis in muscle under catabolic conditions. The amino acid analogue norleucine, however, cannot replace any of the BCAA in protein. Additionally, norleucine affected protein metabolism in highly anabolic organisms. Therefore, the present^thoughts on this issue appear to be incomplete. 
  Reference    Z. Naturforsch. 40c, 427 (1985); received March 11 1985 
  Published    1985 
  Keywords    Protein Turnover, Skeletal Muscle, Branched-Chain Amino Acids, L-Norleucine 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0427.pdf 
 Identifier    ZNC-1985-40c-0427 
 Volume    40 
5Author    M. Nogues, A. Cuenda, F. H. Enao, C. Gutierrez-M, ErinoRequires cookie*
 Title    Ca2+ Uptake Coupled to Glycogen Phosphorolysis in the Glycogenolytic-Sarcoplasmic Reticulum Complex from Rat Skeletal Muscle  
 Abstract    The glycogenolytic-sarcoplasmic reticulum complex from rat skeletal muscle accumulates C a2+ upon stimulation of glycogen phosphorolysis in the absence of added ATP. It is shown that an efficient C a2+ uptake involves the sequential action of glycogen phosphorylase, phos-phoglucomutase and hexokinase, which generate low concentrations of A TP (approximately 1 -2 ^m) compartm entalized in the immediate vicinity of the sarcoplasmic reticulum C a2+, Mg2+-ATPase (the C a2+ pump). The C a2+ uptake supported by glycogenolysis in this subcel-lular structure is strongly stimulated by micromolar concentrations of AMP, showing that the glycogen phosphorylase associated with this complex is in the dephosphorylated b form. The results point out that the flux through this compartmentalized metabolic pathway should be enhanced in physiological conditions leading to increased A M P concentrations in the sarcoplasm, such as long-lasting contractions and in ischemic muscle. 
  Reference    Z. Naturforsch. 51c, 591 (1996); received January 9/February 28 1996 
  Published    1996 
  Keywords    C a2 +-U ptake, Glycogenolysis, Sarcoplasmic Reticulum, Rat, Skeletal Muscle 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0591.pdf 
 Identifier    ZNC-1996-51c-0591 
 Volume    51 
6Author    Virginia Massheimer, LuisM. Fernandez, AnaR. De BolandRequires cookie*
 Title    Stimulation of Calmodulin Binding to Skeletal Muscle Membrane Proteins by 1,25-Dihydroxy-Vitamin D 3  
 Abstract    Previous work has shown that 1,25-dihydroxy-vitamin D 3 rapidly increases calmodulin lev­ els of skeletal muscle membranes without altering the muscle cell calmodulin content. There­ fore, the effects of the sterol on the binding of calmodulin to specific muscle membrane pro­ teins were investigated. Soleus muscles from vitamin D-deficient chicks were treated in vitro for short intervals (5-15 min) with physiological concentrations of 1,25-dihydroxy-vitamin D 3. Proteins of mitochondria and microsomes isolated by differential centrifugation were sep­ arated on sodium dodecyl sulfate polyacrylamide gels. Calmodulin-binding proteins were identified by a [125I]calmodulin gel overlay procedure followed by autoradiography. 1,25-Di-hydroxy-vitamin D 3 increased the binding of labelled calmodulin to a major, calcium-inde­ pendent, calmodulin-binding protein of 28 Kda localized in microsomes, and to minor calmo­ dulin-binding proteins of 78 and 130 Kda proteins localized in mitochondria. The binding of [125I]calmodulin to these proteins was abolished by flufenazine or excess non-radioactive cal­ modulin. 1,25-Dihydroxy-vitamin D 3 rapidly increased muscle tissue Ca uptake and cyclic AM P levels and stimulated the phosphorylation of several membrane proteins including those whose calmodulin-binding capacity potentiates. Analogously to the sterol, forskolin increased membrane calmodulin content, calmodulin binding to the 28 Kda microsomal protein and 45Ca uptake by soleus muscle preparations. Forskolin also induced a similar profile of changes in muscle membrane protein phosphorylation as the hormone. These results suggest that 1,25-dihydroxy-vitamin D 3 affects calmodulin distribution in muscle cells through cyclic AMP-de-pendent phosphorylation of membrane calmodulin-binding proteins. These changes may play a role in the stimulation of muscle Ca uptake by the sterol. 
  Reference    Z. Naturforsch. 45c, 663—670 (1990); received October 2/November 3 1989 
  Published    1990 
  Keywords    1, 25-Dihydroxy-Vitamin D 3, Skeletal Muscle, Muscle Membranes, Calmodulin Binding, Protein Phosphorylation 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0663.pdf 
 Identifier    ZNC-1990-45c-0663 
 Volume    45 
7Author    JoachimR. Sommer, NancyR. Wallace, Wilhelm HasselbachRequires cookie*
 Title    T he Collapse of the Sarcoplasmic Reticulum in Skeletal Muscle  
 Abstract    W hen various cations, including Ca2+, are in the fixative, both sarcoplasmic reticulum (S R) of whole skeletal muscle and isolated SR vesicles collapse to form pentalaminate " compound mem­ branes" that result from the apparent fusion of the lumenal lamellae of the membranous envelope of the SR. The process may be reversed by subsequently soaking the tissue in 1 m NaCl. An identical morphological phenomenon is observed in unfixed quickly frozen isolated frog skeletal muscle fibers, the cation in that case com ing from endogenous sources. The hypothesis is advanced that the collapse is an in vivo process mediated by the sequestration of Ca2+ after contraction. The resulting obliteration of the SR lumen would have the effect of displacing the SR contents into the junctional SR, as w ell as electrically isolating the free SR from the junctional SR during relaxation. As a consequence, resistive coupling between the plasmalemma and the junctional SR becomes a plausible mechanism for the translation of the action potential into Ca2+ release, since the bulk of the SR membrane capacitance would now remain separated from the plasmalemma during relaxation. 
  Reference    Z. Naturforsch. 33c, 561 (1978); received June 7 1978 
  Published    1978 
  Keywords    Excitation-Contraction Coupling, Quick-Freeze SR M orphology, SR M orphology Cation Modulation, Isolated SR M orphology, Sarcoplasmic Reticulum, Skeletal Muscle 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0561.pdf 
 Identifier    ZNC-1978-33c-0561 
 Volume    33