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Studies on silk secretion in the trichoptera (F. Limnephilidae)

II. Structure and amino acid composition of the silk

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Summary

The ultrastructure and amino acid composition of the secreted silk of two species of trichopteran larvae, Pycnopsyche guttifer (Walk.) and Neophylax concinnus McL., were investigated. The spinnerets of these two animals were also examined by scanning electron microscopy. The silk consists of double-stranded, flat ribbons (1–4 μ wide), composed of bundles of 15–25 Å filaments. There are two components of the silk: the fiber proper and a surrounding coat thought to be a silk “gum”. Only the outer coat is positive to the EM PATP technique of Thiery (1967), which indicated the presence of neutral sugars. Amino acid analyses of Pycnopsyche silk show that, like other silks, two predominant amino acids are glycine and serine. Arginine, unexpectedly, is the third most abundant and there are a large number of basic and long side-chain amino acids. X-ray diffraction studies of the silk indicate that it has a less crystalline, more amorphous structure than that of other silks.

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References

  • Akai, H.: Ultrastructure of the fibroin in the silk gland of larval Bombyx mori. Exp. Cell Res. 69, 219–223 (1971)

    Google Scholar 

  • Allegret, P., Fraisse, R.: Étude expérimentale du fonctionnement de l'appareil fileur du Ver à soie, Bombyx mori (L.). C.R. Acad. Sci. (Paris) 249, 165–166 (1959)

    Google Scholar 

  • Ambrose, E.J., Bamford, C.H., Elliot, A., Hanby, W.E.: Water-soluble silk: an α-protein. Nature (Lond.) 167, 264–265 (1951)

    Google Scholar 

  • Asano, Y., Sinohara, H.: Amino sugars in various silk fibroins. Naturwissenschaften 55, 345 (1968)

    Google Scholar 

  • Baier, R.E., Shafrin, E.G., Zisman, W.A.: Adhesion: mechanisms that assist or impede it. Science 162, 1360–1368 (1968)

    Google Scholar 

  • Bamford, C.H., Elliot, A., Hanby, W.E.: Synthetic polypeptides, pp. 369–408. New York: Academic Press 1956

    Google Scholar 

  • Bergen, W. von, Knauss, W.: Textile fiber atlas. I. Wool. Rayon Tex. Mon. 21, 17–20 (1940)

    Google Scholar 

  • Bergmann, W.: Facts and theories concerning the formation of natural silk. Textile Res. J. 9, 329–342 (1939)

    Google Scholar 

  • Branch, H.E.: A contribution to the knowledge of the internal anatomy of Trichoptera. Ann. ent. Soc. Amer. 15, 256–275 (1922)

    Google Scholar 

  • Chen, J.L., Cyr, G.N.: Compositions producing adhesion through hydration. In: Adhesion in biological systems, ed. by R.S. Manly, Chap. 10. New York: Academic Press 1970

    Google Scholar 

  • DeWilde, J., Some physical properties of the spinning threads of Aranea diadema, L. Arch. néerl. Physiol. 27, 118–132 (1943)

    Google Scholar 

  • Dobb, M.G., Fraser, R.D.B., McRae, T.P.: The fine structure of silk fibroin. J. Cell Biol. 32, 289–295 (1967)

    Google Scholar 

  • Engster, M.: Studies on silk secretion in the Trichoptera (F. Limnephilidae). I. Histology, histochemistry, and ultrastructure of the silk glands. J. Morph. (in press)

  • Fraser, R.D.B., MacRae, T.P.: Conformation in fibrous proteins and related synthetic polypeptides. New York: Academic Press 1973

    Google Scholar 

  • Glascow, J.P.: Internal anatomy of a caddis (Hydropsyche colonica). Quart. J. micr. Sci. 79, 151–179 (1936)

    Google Scholar 

  • Glatz, L.: Der Spinnapparat haplogyner Spinnen (Arachnida, Araneae). Z. Morphol. Tiere 72, 1–25 (1972)

    Google Scholar 

  • Gottel L., Mammi, M., Pezzin, G.: Scanning electron microscope observations on elastin. Conn. Tiss. Res. 1, 61–67 (1972)

    Google Scholar 

  • Gross, J., Schmitt, F.O.: The structure of human skin collagen as studied with the electron microscope. J. exp. Med. 88, 555–569 (1948)

    Google Scholar 

  • Hall, F.K.: Wood pulp. Sci. Amer. 230, 52–62 (1974)

    Google Scholar 

  • Hazan, A., Gertler, A., Tahori, A.S., Gerson, U.: Spider mite webbing —III. Solubilization and amino acid composition of the silk protein. Comp. Biochem. Physiol. 51B, 457–462 (1975)

    Google Scholar 

  • Howitt, F.O.: Bibliography of the technical literature on silk. London: Hutchinson 1947

    Google Scholar 

  • Hunt, S.: Polysaccharide-protein complexes in invertebrates. New York: Academic Press 1970

    Google Scholar 

  • Iizuka, E.:Mechanism of fiber formation by the silkworm, Bombyx mori. Biorheology 3, 141–152 (1966)

    Google Scholar 

  • Lenormat, H.: Infra-red spectra and structure of the proteins of the silk glands. Trans. Faraday Soc. 52, 549–553 (1956)

    Google Scholar 

  • Lloyd, J.T.: The biology of North American caddis fly larvae. Bull. Lloyd Libr., Entomol. Ser. 1, 21, 1–124 (1921)

    Google Scholar 

  • Lucas, F., Rudall, K.M.: Extracellular fibrous proteins: the silks. In: Comprehensive biochemistry, vol. 26B, ed. by M. Florkin and E. Stotz, pp. 475–558. New York: Elsevier Publishing Co. 1968

    Google Scholar 

  • Lucas, F., Shaw, J.T.B., Smith, S.G.: The silk fibroins. Adv. Protein Chem. 13, 107–242 (1958)

    Google Scholar 

  • Lucas, F., Shaw, J.T.B., Smith, S.G.: Comparative studies of fibroin. I. The amino acid composition of various fibroins and its significance in relation to their crystal structure and taxonomy. J. molec. Biol. 2, 339–349 (1960)

    Google Scholar 

  • Lucas, R.: Beiträge zur Kenntnis der Mundwerkzeuge der Trichoptera. Arch. Naturgesch. 59, 285–330 (1893)

    Google Scholar 

  • Mercer, E.H.: Formation of the silk fibre by the silkworm. Nature (Lond.) 168, 792–793 (1951)

    Google Scholar 

  • Meyer, K.H., Jeannerat, J.: Les proprietés des polymères en solution. XI. Sur la formation du fil de soie à partir du continu liquide de la glande. Helv. chim. Acta 22, 22–30 (1939)

    Google Scholar 

  • Peters, H.M.:Über den Spinnapparat von Nephila madagascariensis (Radnetzspinnen, Fam. Argiopidae). Z. Naturforsch. 10b, 395–404 (1955)

    Google Scholar 

  • Ramsden, W.: Coagulation by shearing and by freezing. Nature (Lond.) 142, 1120–1121 (1938)

    Google Scholar 

  • Raven, D.J., Earland, C., Little, M.: Occurrence of dityrosine in tussah silk fibroin and keratin. Biochem. biophys.Acta (Amst.) 251, 96–97 (1971)

    Google Scholar 

  • Rudall, K.M.: Silk and other cocoon proteins. Comp. Biochem. 4, 397–433 (1962)

    Google Scholar 

  • Rudall, K.M., Kenchington, W.: Arthropod silks: the problem of fibrous proteins in animal tissues. Ann. Rev. Entomol. 16, 73–96 (1971)

    Google Scholar 

  • Seifter, S., Gallop, P.M.: The structure proteins. In: The proteins: Composition, structure, and function, 2nd ed., ed. by A. Neurath, Vol. IV. New York: Academic Press 1963

    Google Scholar 

  • Senti, F.C.: Structure of protein fibers. Amer. Dyestuff Reporter 36, 230–237 (1947)

    Google Scholar 

  • Sinohara, Y., Asano, Y.: Carbohydrate content of fibroin and sericin of the silkworm, Bombyx mor. J. Biochem. 62, 129–130 (1967)

    Google Scholar 

  • Thiery, J.P.: de]Mise en évidence des polysaccharides sur coupes fines en microscopie électronique. J. Micr. (Paris) 6, 987–1018 (1067)

    Google Scholar 

  • Tindall, A.R.: The larval case of Triaenodes bicolor Curtis (Trichoptera: Leptoceridae). Proc. roy. ent. Soc. London A 35, 93–96 (1960)

    Google Scholar 

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Submitted to the Department of Biological Sciences of the State University of New York at Albany in partial fulfillment of the requirements for the degree of Doctor of Philosophy

Acknowledgements. This study was supported in part by a National Institutes of Health Graduate Student Traineeship grant # GM-02014. The author would like to express sincere gratitude to Dr. Stephen Brown for his encouragement and help during the course of this study. I would also like to thank Dr. Curtis Hemenway and Mr. Douglas Halgren of Dudley Observatory for the use of their scanning electron microscope as well as Dr. Helen Ghiradella and Mr. William Radigan for help with the scanning electron microscopy. I owe special appreciation to Dr. Y. Myer of the Chemistry Department of SUNYA for doing an amino acid analysis of the silk and to Dr. K.M. Rudall of the University of Leeds for doing the X-ray diffraction studies of the silk samples

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Engster, M.S. Studies on silk secretion in the trichoptera (F. Limnephilidae). Cell Tissue Res. 169, 77–92 (1976). https://doi.org/10.1007/BF00219309

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