Summary
-
1.
By means of current methods oxidative enzymes, glycogen and lipid have been localized on the histological and cytological level in Myxine. musculature.
-
2.
Red muscle fibres (belonging to the “slow” physiological variety) and heart muscle cells contain large quantities of most enzymes studied as well as of glycogen. In addition red fibres of m. parietalis contain large quantities of storage lipid.
-
3.
White fibres (which are typical “fast” fibres) contain practically no cytochrome oxidase and Krebs' cycle dehydrogenases, except for some activity of NAD-dependent malic dehydrogenase. However, these fibres are approximately as rich in lactate dehydrogenase and NAD-dependent α-glycerophosphate dehydrogenase as red fibres. Glycogen content of different fibres varies somewhat, mostly it stains equal in red, white and intermediate fibres.
-
4.
Intermediate fibres generally show an intermediate activity of enzymes and content of glycogen and lipid.
Non-NAD-dependent α-glycerophosphate, glucose-6-phosphate, and β—hydroxybutyrate dehydrogenases were not detected by the histochemical methods used.
-
5.
These observations are discussed in relation to physiological and ultrastructural findings in Myxine as well as to investigations on muscle of other animals.
Similar content being viewed by others
Abbreviations
- SDH:
-
Succinate dehydrogenase
- α-GPDH (M):
-
“Menadione-linked” α-glycerophosphate dehydrogenase
- α-GPDH (NAD):
-
NAD-linked α-glycerophosphate dehydrogenase
- β-HO-BDH:
-
β-hydroxybutyrate dehydrogenase
- CYO:
-
Cytochrome oxydase
- G-6-PDH:
-
Glucose-6-phosphate dehydrogenase
- IDH (NAD):
-
NAD-linked isocitrate dehydrogenase
- IDH (NADP):
-
NADP-linked isocitrate dehydrogenase
- LDH:
-
Lactate dehydrogenase
- MDH (NAD):
-
NAD-linked malate dehydrogenase
- MDH (NADP):
-
NADP-linked malate dehydrogenase
- NBT:
-
Nitro blue tetrazolium
- PMS:
-
Phenazine methosulfate
References
Alnaes, E., J. K. S. Jansen, and T. Rudjord: Spontaneous junctional activity of fast and slow parietal muscle fibres of the hagfish. Acta physiol. scand. 60, 240–255 (1964).
Andersen, P., J. K. S. Jansen, and Y. Löyning: Slow and fast muscle fibres in the Atlantic hagfish (Myxine glutinosa). Acta physiol. scand. 57, 167–179 (1963).
Benitez, L., and R. Fischer: A modification to the “incubation mixture film method” for the histochemical localization of lactic dehydrogenase. J. Histochem. Cytochem. 12, 858–859 (1964).
Bergman, R. A., and D. G. Walker: The cytochemical localization of oxydative enzymatic activity and glycogen in frog striated muscle. Bull. Johns Hopk. Hosp. 104, 179–198 (1959).
Bone, Q.: Some observations upon the peripheral nervous system of the hagfish, Myxine glutinosa. J. mar. biol. Ass. U. K. 132, 61–73 (1963).
—: Patterns of muscular innervation in the lower chordates. Int. Rev. Neurobiol. 6, 99–147 (1964).
Brody, I. A., and W. K. Engel: Effects of phenazine methosulphate in histochemistry. J. Histochem. Cytochem. 12, 928–929 (1964).
Bruño, W., and N. I. Germino: Distribution of succinic dehydrogenase in the organs of the adult albino rat. Acta anat. (Basel) 33, 161–174 (1958).
Burstone, M. S.: Histochemical demonstration of cytochrome oxidase with new amine reagents. J. Histochem. Cytochem. 8, 63–70 (1960).
Cole, F. J.: A monograph on the general morphology of the myxinoid fishes, based on a study of Myxine. Part II. The anatomy of muscles. Trans. roy. Soc. Edinb. 45, 683–757 (1907).
—: A monograph on the general morphology of the myxinoid fishes, based on a study of Myxine. Part IV. The morphology of the vascular system. Trans. roy. Soc. Edinb. 54, 309–342 (1926).
Conklin, J. L., M. M. Dewey, and R.H. Kahn: Cytochemical localization of certain oxidative enzymes. Amer. J. Anat. 110, 19–27 (1962).
Diculesco, I., D. Onicesco, and L. Mischiu: A histochemical analysis of dehydrogenase in the different types of muscular tissues. J. Histochem. Cytochem. 12, 145–152 (1964).
Fahimi, H. D., and C. R. Amarasingham: Cytochemical localization of lactic dehydrogenase in white skeletal muscle. J. Cell Biol. 22, 29–48 (1964).
Flood, P. R.: Skeletal muscle fibre types in Amphioxus lanceolatus and Myxine glutinosa. J. Ultrastruct. Res. 12, 238 (1965a).
- Personal communication 1965b.
—, and J. Storm Mathisen: A third type of muscle fibre in the parietal muscle of the Atlantic hagfish Myxine glutinosa (L.)? Z. Zellforsch. 58, 638–640 (1962).
Grenacher, H.: Beiträge zur näheren Kenntnis der Muskulatur der Cyclostomen und Leptocardier. Z. wiss. Zool. 17, 577–597 (1867).
Hashimoto, T., J. S. Kaluza, and M. S. Burstone: The effect of menadione and phenazine methosulfate on the tetrazolium reduction system under histochemical conditions. J. Histochem. Cytochem. 12, 797–804 (1964).
Hitzeman, J. W.: Observations on the subcellular localization of oxidative enzymes with nitro blue tetrazolium. J. Histochem. Cytochem. 11, 62–70 (1963).
Jansen, J., P. Andersen, and J. K. S. Jansen: On the structure and innervation of the parietal muscle of the hagfish (Myxine glutinosa). Acta morph. neerl.-scand. 5, 329–338 (1963).
Johansen, K.: The cardiovascular system of Myxine glutinosa L. In: The biology of Myxine (eds. A. Brodal and R. Fänge), p. 289–316. Oslo: Universitetsforlaget 1963.
—, and R. Strahan: The respiratory system of Myxine glutinosa L. In: The biology of Myxine (eds. A. Brodal and R. Fänge), p. 352–371. Oslo: Universitetsforlaget 1963.
Lehninger, A. L.: The mitochondrion. Molecular basis of structure and function. New York and Amsterdam: W. A. Benjamin Inc. 1964.
—, H. C. Sudduth, and J. B. De Wise: The D-β-hydroxybutyric dehydrogenase of mitochondria. J. biol. Chem. 235, 2450–2455 (1960).
Manwell, C.: The blood proteins of cyclostomes. A study in phylogenetic and ontogenetic biochemistry. In: The biology of Myxine (eds. A. Brodal and R. Fänge), p. 372–455. Oslo: Universitetsforlaget 1963.
Marinelli, W., u. A. Strenger: Vergleichende Anatomie und Morphologie der Wirbeltiere, Bd. I, S. 81–172. Wien: Franz Deuticke 1956.
Mathisen, J. Storm: Unpublished observations 1963.
—, and S. I. Mellgren: Some observations concerning the role of phenazine methosulfate in histochemical dehydrogenase methods. J. Histochem. Cytochem. 13, 408–409 (1965).
Maurer, F.: Die Elemente der Rumpfmuskulatur bei Cyclostomen und höheren Wirbeltieren. Morph. Jb. 21, 473–619 (1894).
Nachmias, V. T., and H. A. Padykula: A histochemical study of normal and denervated red and white skeletal muscles of the rat. J. biophys. biochem. Cytol. 4, 47–54 (1958).
Nicolaysen, K.: In preparation.
Novikoff, A. B.: Preservation of the fine structure of isolated liver cell particulates with polyvinylpyrrolidone-sucrose. J. biophys. biochem. Cytol. 2, No 4 (Suppl.) (1956).
—: Electron transport enzymes: Biochemical and tetrazolium staining studies. In: Histochemistry and cytochemistry Proceedings of the First Internat. Congr. (ed. E. Wegmann), p. 465–481. Oxford-London-New York-Paris: Pergamon Press 1963.
Ogata, T.: A histochemical study of the red and white muscle fibers. I. Activity of succinoxydase system in muscle fibers. Acta Med. Okayama 12, 216–227 (1958).
—, and M. Mori: Histochemical study of oxidative enzymes in vertebrate muscles. J. Histochem. Cytochem. 12, 171–182 (1964).
Peachey, L. D., and A. F. Huxley: Structural identification of twitch and slow striated muscle fibres of the frog. J. Cell Biol. 13, 177–180 (1962).
Pearse, A. G. E.: Histochemistry. Theoretical and applied, 2nd ed. London: J. & A. Churchill Ltd. 1960.
—: Direct relationship of phorphorylase and mitochondrial α-glycerophosphate dehydrogenase activity in skeletal muscle. Nature (Lond.) 191, 504 (1961).
Pette, D., and H. Brandau: Intercellular localization of glycolytic enzymes in cross striated muscles of Locusta migratoria. Biochem. biophys. Res. Commun. 9, 367–370 (1962).
Scarpelli, D. G., and A. G. E. Pearse: Physical and chemical protection of cell constituents and the precise localization of enzymes. J. Histochem. Cytochem. 6, 369–376 (1958).
Schott, H. S.: Zur Frage der histochemischen Fettspezifität des Sudanschwarz B und zur Methode der Auftrennung seiner Fraktionen. Histochemie 3, 467–476 (1964).
Shamarina, N. M.: Electric response of “tonic” muscle fibres of the frog skeletal musculature. Nature (Lond.) 193, 783–784 (1962).
Smith, B.: The localization of enzymes within skeletal muscle fibres using the tetrazolium technique. J. Histochem. Cytochem. 12, 847–851 (1964).
Stein, J. M., and H. A. Padykula: Histochemical classification of individual skeletal muscle fibers of the rat. Amer. J. Anat. 110, 103–124 (1962).
Strahan, R.: The behaviour of Myxine and other myxinoids. In: The biology of Myxine (eds. A. Brodal and R. Fänge), p. 22–32. Oslo: Universitetsforlaget 1963.
Wachstein, M., and E. Meisel: The distribution of histochemically demonstrable succinic dehydrogenase and of mitochondria in tongue and skeletal muscle. J. biophys. biochem. Cytol. 1, 483–488 (1955).
Waravdekar, V. S., P. J. Goldblatt, B. F. Trump, C. C. Griffin, and R. E. Stowell: Effect of freezing and thawing on certain nuclear and mitochondria! enzymes of mouse liver. J. Histochem. Cytochem. 12, 498–503 (1964).
Wattenberg, L. W., and J. Lionel Leong: Effects of co-enzyme Q10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction. J. Histochem. Cytochem. 8, 296–303 (1960).
Wihje, M. Van, M. C. Blanchaer, and W. R. Jacyk: The oxydation of lactate and α—glycerophosphate by red and white skeletal muscle: II. Histochemical studies. J. Histochem. Cytochem. 11, 505–510 (1963).
Williams, D., and H. J. Whiteley: Variations in formazan production in mitochondrial dehydrogenase studies on osmotically protected fresh frozen sections. J. Histochem. Cytochem. 11, 89–95 (1963).
Zimmermann, H., and A. G. E. Pearse: Limitations in the histochemical demonstration of pyridine nucleotide-linked dehydrogenases (“nothing dehydrogenase”). J. Histochem. Cytochem. 7, 271–275 (1959).
Author information
Authors and Affiliations
Additional information
This study was supported by The Norwegian Research Council for Science and the Humanities and by U. S. Public Health Service (Grant NB 02215-06).
The authors are indebted to Professor Dr. philos. Bjørn Føyn and Cand. real. Finn Walvig, Biological Station, University of Oslo. Drøbak, for generous supply of hagfish material. We also wish to thank Professor Jan Jansen, M. D. and Associate Professor Th. Blackstad, M. D. for reading the manuscript, and Mrs. A. Holter and Mr. E. Risnes for technical assistance.
Rights and permissions
About this article
Cite this article
Mellgren, S.I., Mathisen, J.S. Oxidative enzymes, glycogen and lipid in striated muscle. Zeitschrift für Zellforschung 71, 169–188 (1966). https://doi.org/10.1007/BF00335745
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00335745