Histochemical characteristics of vertebrate striated muscle: a review.
(1) The histochemical staining pattern of succinic dehydrogenase (SDH) does not show unequivocal differentiation between the type I red and type II red fibres in mammalian striated muscles. (2) Since high biochemical activity of beta-hydroxybutyric dehydrogenase (beta-HOBDH) occurs in mitochondria of the type I red fibres, the histochemical localization of this enzyme may show a pattern of staining reciprocal to that seen for myofibrillar ATPase. (3) It remains to be confirmed that the type I red fibres, which are possibly slow-twitch physiologically, possess the highest concentration of myoglobin. The histochemical correlation of myoglobin and myofibrillar ATPase in serial sections should be studied. (4) In order to achieve a more realistic picture, various glycolytic and glycogenolytic enzymes should be incubated according to the gelatin film technique, or semipermeable membrane technique or collagen polypeptide technique. A histochemical correlation of phosphorylase, LDH, PFK, alpha-glycerophosphate dehydrogenase, and myofibrillar ATPase in adjacent muscle sections may throw light on the histochemical characteristics of the different fibre-types. (5) The specific histochemical demonstration of AMPase is achieved following preincubation of tissue sections. (6) ADPase has been demonstrated by the calcium precipitation technique only (GUTH and YELLIN, 1971). A number of studies claim, however, that ADPase is not demonstrable histochemically in muscle fibres. (7) The presence of magnesium ions is a prerequisite for the adequate histochemical demonstration of mitochondrial ATPase. The latter is inhibited almost completely by 40 mM Ca++ (when Mg++ is not added) at both neutral and alkaline pH values. (8) The histochemical activity of SR-AT-Pase seen as continuous reticula but without punctuate and sub-sarcolemmal staining possibly represents the extra ATPase of SR. (9) On the basis of myofibrillar ATPase reaction, an inherent heterogeneity, between the type II red and type II white may be recognized. In addition, the above fibre-types possess their respective sub-populations. (10) Following diK+ EDTA preincubation, some type II red fibres show selective lability. These are the mitochondria-rich fibres. Thus in the total absence of both punctuate and subsarcolemmal staining, the presence of mitochondrial ATPase activity under the histochemical conditions for myofibrillar ATPase is unlikely. (11) The reaction pattern of CK/ATPase (coupled reaction) at pH 6.9 is distinctly intermyofibrillar and unlike SDH-pattern. This reticular reaction is associated mainly with the SR and hence the importance of transphosphorylation in this organelle for the Ca++ uptake and muscle relaxation. (12) The CK/ATPase reaction at pH8.0 has shown important histoenzymatic characteristics. At this pH value the type I red fibres and slow-twitch soleus show myofibrillar reaction pattern. This identical histochemical behaviour suggests that type I red fibres are possibly slow-contracting...
D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D003402:Creatine Kinase / Q000032:analysis*; D003576:Electron Transport Complex IV / Q000032:analysis; D006006:Glycogen Synthase / Q000032:analysis; D006651:Histocytochemistry; D006884:Hydroxybutyrate Dehydrogenase / Q000032:analysis; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D008291:Malate Dehydrogenase / Q000032:analysis; D008931:Mitochondria, Muscle / Q000201:enzymology; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils / Q000201:enzymology; D009211:Myoglobin / Q000032:analysis; D009252:NADPH Dehydrogenase / Q000032:analysis; D010088:Oxidoreductases / Q000032:analysis*; D010732:Phosphofructokinase-1 / Q000032:analysis; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D006005:Phosphorylases / Q000032:analysis; D012519:Sarcoplasmic Reticulum / Q000201:enzymology; D013385:Succinate Dehydrogenase / Q000032:analysis; D009626:Terminology as Topic
D009211:Myoglobin; D010088:Oxidoreductases; D007770:L-Lactate Dehydrogenase; D006884:Hydroxybutyrate Dehydrogenase; D008291:Malate Dehydrogenase; D013385:Succinate Dehydrogenase; D009252:NADPH Dehydrogenase; D003576:Electron Transport Complex IV; D006005:Phosphorylases; D006006:Glycogen Synthase; D010732:Phosphofructokinase-1; D003402:Creatine Kinase; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases