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Fine structure and origin of the tunic of Perophora viridis
Author(s) -
Deck J. David,
Hay Elizabeth D.,
Revel JeanPaul
Publication year - 1966
Publication title -
journal of morphology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.652
H-Index - 74
eISSN - 1097-4687
pISSN - 0362-2525
DOI - 10.1002/jmor.1051200304
Subject(s) - golgi apparatus , endoplasmic reticulum , biology , cytoplasm , vesicle , organelle , cellulose , glycoprotein , ultrastructure , microbiology and biotechnology , melanosome , secretion , mantle (geology) , polysaccharide , biophysics , biochemistry , anatomy , melanin , membrane , paleontology
The fine structure of the tunic of a typical ascidian was investigated because of the cellulose‐like polysaccharide known to occur in its substance. The glycoprotein mantle does contain filaments very much like plant cellulose in morphology. Tunicin filaments are 35–50 Å in diameter, often beaded, and of indeterminate length. Histochemical evidence that they are composed of cellulose is given here and past chemical and physical studies on the unusual ascidian polysaccharide are reviewed. Moreover, we present here for the first time direct autoradiographic evidence that epidermal cells are involved in the synthesis and secretion of tunicin. Tritiated glucose is immediately incorporated into the Golgi zone of epidermal cells and labeled product appears in the tunic at later intervals. The fine structure of the epidermal cell is described in detail. Unlike the rather moribund appearing vanadocyte that wanders through the tunic, the epidermal cell has well‐developed cytoplasmic organelles and a large vesicular nucleus. The granular endoplasmic reticulum is abundant and the Golgi complex is highly developed. It seems likely that the lamellae and vesicles of the Golgi complex are involved in the production of the tunic sugar and that tunic proteins of as yet unknown nature are produced by the ergastoplasm. Further investigation of the ascidian mantle should be of interest because of the possibility that cellulose is a more general component of glycoprotein surface coats in animals than has heretofore been recognized.

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