Please use this identifier to cite or link to this item: http://hdl.handle.net/10201/18816

Title: Ultrastructure of invertebrate muscle cell types
Issue Date: 1996
Publisher: Murcia : F. Hernández
ISSN: 0213-3911
Related subjects: CDU::5 - Ciencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citología
Keywords: Invertebrate muscle cells
Smooth muscle
Abstract: The muscular cells of invertebrates can be divided into three major classes on the basis of their striation pattem: transversely striated, obliquely striated, or smooth muscle. Transversely striated muscles have either continuous or discontinuous Z lines and, thus, can be subdivided into two types respectively. Of al1 invertebrate muscles, the transversely striated muscle with continuos Z lines is the most similar to the vertebrate skeletal muscle and is present in arthropods, whose musculature (including the visceral muscles) only consists of this cell type. These muscles are multinucleate cells that contain myofibrils showing welldefined sarcomeres. Transversely striated muscles with discontinuous Z lines, consisting of multiple small electrondense patches, are found in the translucent portions of adductor muscles of some bivalves and in the heart muscle of the gastropods. This muscle is formed by mononucleated cells with centrally-located nuclei and a single myofibril. The obliquely striated muscle appears in nematodes, annelids, molluscs, brachiopods and chaetognathes and consists of mononucleated cells with both thick and thin myofilaments which form sarcomeres delimited by Z lines. Myofilaments are not perpendicular but oblique to the Z lines, so that both A and 1 bands may be seen together in each of the three spatial planes of view. Smooth muscle has been reported in coelenterates, annelids, molluscs, brachiopods and echinoderms, but is lacking in arthropods. These muscle cells have a centrally-located nucleus and abundant thin and thick myofilaments without apparent sarcomeres. The most relevant characteristics of invertebrate muscle cells are the following. The thick (myosin) myofilarnents show a variable length (from 2.2 pm up to 6 pm) and width (from 14 nm up to 231 nm) and contain a central core of paramyosin, which is absent in vertebrate muscles. Thick filaments are homogenous in transversely striated muscles and either homogeneous or fusiform in the obliquely striated and smooth muscles. Thin filaments measure 6 nm in diameter. They contain tropomyosin and, only in striated muscles, also troponin. The thinlthick filament ratio varies from 311 to 611, even in smooth muscles. The plaques for filament anchorage (Z lines in striated muscles or electrondense bodies in smooth muscles) contain a-actinin. The striated (transversely or obliquely) muscles show long sarcomeres (up to 9 pm) and the number of thin filaments around each thick filament varies from 3 to 12, so that each thin filament is shared by two thick filaments. Z lines in the striated muscles show a variety of structures that differ from one species to another (filament bundles in nematodes, bars in annelids, small patches in molluscs, etc). Many striated muscles contain titin (connectin) and intermediate filaments and display a sarcotubular system consisting of T tubules and sarcoplasmic reticulum tubules. Both structures form dyads and, more rarely, triads. The location of T tubules as well as the configuration and distribution of sarcoplasmic reticulum vary among muscles and species. Invertebrate smooth muscle differs from that of vertebrates principally in the higher proportion and larger diameter of thick myofilaments. These may be fusiform and their size and number may vary widely among cells. These muscle cells may be classified by the characteristics of both the thick filaments and the electrondense bodies for filament anchorage.
Primary author: Paniagua, R.
Royuela, M.
García-Anchuelo, R.M.
Fraile, Benito
Published in: Histology and histopathology
URI: http://hdl.handle.net/10201/18816
Document type: info:eu-repo/semantics/article
Number of pages / Extensions: 21
Rights: info:eu-repo/semantics/openAccess
Appears in Collections:Vol.11, nº 1 (1996)

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