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Chitin synthesis in zygotes of Ascaris suum

Published online by Cambridge University Press:  05 June 2009

P. Dubinský ,
M. Ryboš ,
L. Turčeková  and
E. Ossikovski
P. Dubinský
Affiliation:
Helminthological Institute of the Slovak Academy of Sciences, Dukelskych hrdinov 3, 040 01 KoSicc Czechoslovakia
M. Ryboš
Affiliation:
Helminthological Institute of the Slovak Academy of Sciences, Dukelskych hrdinov 3, 040 01 KoSicc Czechoslovakia
L. Turčeková
Affiliation:
Helminthological Institute of the Slovak Academy of Sciences, Dukelskych hrdinov 3, 040 01 KoSicc Czechoslovakia
E. Ossikovski
Affiliation:
Central Laboratory of Helminthology, Bulgarian Academy of Sciences, BontchevStr. 25 1113 Sofia, Bulgaria
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Abstract

In Ascaris suum chitin is formed in the zygote immediately after oocyte fertilization, and its synthesis is completed in the eggs from the distal half of the uterus. Incorporation of radiocarbon [C] glucose into chitin of the eggshell was 40-fold higher than incorporation of [C] glucosamine. The same rank order also holds for the incorporation of label from these isotopes into the glycogen of the ovaries. A large part of the radiolabel was incorporated first into oocyte glycogen and only after fertilization was it incorporated into eggshell chitin. Actinomycin D inhibited chitin synthesis in the eggs from the distal half of the uterus and it significantly reduced incorporation of radiocarbon from glucose into chitin.

Keywords

Ascaris suumchitinzygoteradiolabelling
Type
Research Article
Information
Journal of Helminthology , Volume 60 , Issue 3 , September 1986 , pp. 187 - 192
Copyright
Copyright © Cambridge University Press 1986

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References

REFERENCES

Ashmarin, I. P. & Klyucharev, L. A. (1975) [Inhibitors of protein synthesis.] Publ. House Medicina: Moscow. [In Russian.]Google Scholar
Bade, M. L. (1974) Localization of molting chitinase in insect cuticle. Biochimica et Biophysica Acta, 372, 474–477.CrossRefGoogle Scholar
Bergmeyer, H. U. & Bernt, E. (1963) D-glucose. Determination with glucose oxidase and peroxidase. In: Methods of enzymatic analysis, (editor Bergmeyer, H. U.) Verlag Chemie, Weinheim, pp. 123–130.Google Scholar
Bocquet, J. & Pujol, J. P. (1973) Incorporation of [l-14C]-glucosamine in a selachian Scyliorhinus canicula. Comparative Biochemistry and Physiology, 45B, 113–123.Google Scholar
Coles, G. C. (1966) Studies on resilin biosynthesis. Journal of Insect Physiology, 12, 679–691.CrossRefGoogle ScholarPubMed
Dubinský, P., Ryboš, M. & Turčeková, Ľ. (1985) Enzymes regulating glucosamine 6-phosphate synthesis in the zygote of Ascaris suum. International Journal for Parasitology, 15, 415–419.CrossRefGoogle ScholarPubMed
Dubinský, P., Ryboš, M. & Turčekova, Ľ., (1986) Properties and localization of chitin synthase in Ascaris suum eggs. Parasilology, 92, 219–225.CrossRefGoogle ScholarPubMed
Ellison, T., Thomson, W. A. B. & Strong, F. M. (1960) Volatile fatty acids from axenic Ascaris lumbricoides. Archives of Biochemistry and Biophysics, 91, 247–254.CrossRefGoogle ScholarPubMed
Fairbairn, D. (1957) The biochemistry of Ascaris. Experimental Parasitology, 6, 491–554.CrossRefGoogle ScholarPubMed
Farkaš, V & Svoboda, A. (1980) Kinetics of P-glucan and chitin formation by cells and protoplasts of the yeast Saccharomyces cerevisiae. Current Microbiology, 4, 99–103.CrossRefGoogle Scholar
Hackett, C. J. & Chen, K. C. (1978) Quantitative isolation of native chitin from resistant structures of Sordaria and Ascaris species. Analytical Biochemistry. 89, 487–500.CrossRefGoogle ScholarPubMed
Kass, I. S., Larsen, D. A., Wang, C. C. & Stretton, A. O. W. (1982) Ascaris suum: Differential effects of avermectin B la on the intact animal and neuromuscular strip preparations. Experimental Parasitology, 54, 166–174.CrossRefGoogle Scholar
Kaulenas, M. S. & Fairbairn, D. (1968) RNA metabolism of fertilized Ascaris lumbricoides eggs during uterine development. Experimental Cell Research, 52, 233–251.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.CrossRefGoogle ScholarPubMed
Molano, J., Bowers, B. & Cabib, E. (1980) Distribution of chitin in the yeast cell wall. Journal of Cell Biology, 85, 199–212.CrossRefGoogle ScholarPubMed
Orpin, C. G., Huskisson, N. S. & Ward, P. F. (1976) Molecular structure and morphology of glycogen isolated from the cestode, Moniezia expansa, Parasitology, 73, 83–95.CrossRefGoogle ScholarPubMed
Sadler, T. W. & Kochhar, D. M. (1976) Biosynthesis of DNA, RNA and protein by mouse embryos of chlorambucil. Journal of Embryology and experimental Morphology, 36, 273–281.Google ScholarPubMed
Sakata, R. (1963) Studies on chitin. I. Investigations on the infra-red spectra of chitin of pig Ascaris egg. Japanese Journal of Parasitology, 12, 387–389.Google Scholar
Speck, U., Urich, K & Herz-Hübner, U. (1972) Nachweis einer Regulation der Glucosaminbildung bei dem Flusskrebs Orconectes limosus zur Zeit der Hãutung. Zeitschrift für vergleichende Physiologie, 76, 341–346.CrossRefGoogle Scholar
Stevenson, J. R. (1972) Changing activities of the crustacean epidermis during the molting cycle. American Zoologist, 12, 373–380.CrossRefGoogle Scholar
Surholt, B. (1975) Studies in vivo and in vitro on chitin synthesis during the larval-adult moulting cycle of the migratory locust, Locusta migratoria L. Journal of Comparative Physiology. 102, 135–147.CrossRefGoogle Scholar
Tracey, M. V. (1955) Chitin. In: Moderne Methoden der Pflanzenanalyse (Editors, Peach, K. & Tracey, M. V.) Springer Verlag, Berlin, Vol. 2, pp. 264–274.CrossRefGoogle Scholar
Ulane, R. E. & Cabib, E. (1976) The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of the activating factor. Journal of Biological Chemistry, 251, 3367–3374.CrossRefGoogle ScholarPubMed
Wharton, D. A. (1983) The production and functional morphology of helminth egg-shells. Parasitology, 86, 85–97.CrossRefGoogle ScholarPubMed