Literature DB >> 2475466

A silver-reducing component in rat striated muscle. I. Selective localization at the level of the terminal cistern/transverse tubule system. Light and electron microscope studies with a new histochemical procedure.

C J Tandler1, A Pellegrino de Iraldi.   

Abstract

This study reports the presence of a silver-reducing constituent in rat striated muscle fiber located selectively at the level of the terminal cistern/transverse tubule system. It is related to the T tubule network at or near sites that participate in junctions with terminal cisternae, i.e., at both sides of the T tubule in skeletal muscle (triad) and, predominantly, at one side in the ventricle (dyad). Little reactivity is present in the auricle due to the scarcity of those membrane systems. The longitudinal sarcoplasmic reticulum, the sarcolemma, mitochondria and myofibrils are not outlined by the reaction product. Extraction of low molecular weight substances, nucleic acids and lipids did not suppress the chemical reaction. A new argentaffin (Hg--Ag) technique is described. Ethanol or aldehyde fixed muscles were passed to water, postfixed 6-24 h with mercuric acetate (5% w/v in 1% acetic acid), washed with 1% acetic acid and distilled water, stained 12-24 h at 43 degrees C with ammoniacal silver nitrate (60% w/v) and washed in 10% sodium sulfite (three changes) and water. All steps were carried out in darkness. Postfixation with mercuric acetate proved to be essential for immobilizing the argentaffin component without interfering with its strong argentaffinity. The procedure also provides a simple method for tracing the pathway of transversally oriented membrane systems in skeletal and cardiac muscle cells.

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Year:  1989        PMID: 2475466     DOI: 10.1007/bf00495010

Source DB:  PubMed          Journal:  Histochemistry        ISSN: 0301-5564


  23 in total

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Authors:  C J TANDLER
Journal:  J Histochem Cytochem       Date:  1954-05       Impact factor: 2.479

2.  Factors affecting the formation of metallic silver and the binding of silver ions by tissue components.

Authors:  F Gallyas
Journal:  Histochemistry       Date:  1979-11

3.  The messenger across the gap.

Authors:  A P Somlyo
Journal:  Nature       Date:  1985 Jul 25-31       Impact factor: 49.962

4.  Physico-chemical mechanism of the argyrophil I reaction.

Authors:  F Gallyas
Journal:  Histochemistry       Date:  1982

5.  Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures.

Authors:  M Inui; A Saito; S Fleischer
Journal:  J Biol Chem       Date:  1987-11-15       Impact factor: 5.157

6.  RETICULAR ORGANIZATIONS WITHIN THE STRIATED MUSCLE CELL : An Historical Survey of Light Microscopic Studies.

Authors:  D S Smith
Journal:  J Biophys Biochem Cytol       Date:  1961-08-01

7.  THE LOCATION OF ADENINE NUCLEOTIDE IN THE STRIATED MUSCLE OF THE TOAD.

Authors:  D K HILL
Journal:  J Cell Biol       Date:  1964-03       Impact factor: 10.539

8.  Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle.

Authors:  A Saito; S Seiler; A Chu; S Fleischer
Journal:  J Cell Biol       Date:  1984-09       Impact factor: 10.539

9.  The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study.

Authors:  C Franzini-Armstrong; L J Kenney; E Varriano-Marston
Journal:  J Cell Biol       Date:  1987-07       Impact factor: 10.539

10.  Isolation, characterization, and localization of the spanning protein from skeletal muscle triads.

Authors:  R M Kawamoto; J P Brunschwig; K C Kim; A H Caswell
Journal:  J Cell Biol       Date:  1986-10       Impact factor: 10.539

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  2 in total

1.  A silver-reducing component in rat striated muscle. II. Isolated sarcoplasmic reticulum vesicles.

Authors:  C J Tandler; D A Gonzalez; P G Remorini; A Pellegrino de Iraldi
Journal:  Histochemistry       Date:  1989

2.  An 'axis-like' material in the centromeric region of metaphase-I chromosomes from mouse spermatocytes.

Authors:  C J Tandler; A J Solari
Journal:  Genetica       Date:  1991       Impact factor: 1.082

  2 in total

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