Lactic Dehydrogenases and Muscular Dystrophy in the Chicken

Kaplan, Nathan O.; Cahn, Robert D.

doi:10.1073/pnas.48.12.2123

Cited by 75 publications

(22 citation statements)

References 7 publications

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“…Furthermore, it was found that the pectoralis of mature dystrophic chickens contains isoenzyme species of lactic dehydrogenase [11] and acetylcholinesterase [22,23] which are characteristic of embryonic muscle. The results of the present study augment these observations and provide further evidence of the hypothesis that the muscle of mature dystrophic animals has embryonic characteristics.…”

Section: Discussionmentioning

confidence: 99%

Adenyl Cyclase in the Pectoral Mnscle of Normal Chickens and Chickens with Hereditary Muscular Dystrophy

Bz¹,

Dh²

1972

Enzyme

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Adenyl cyclase activity was determined in the pectoral muscle of normal chickens and chickens with hereditary muscular dystrophy at various stages of development. Significant differences were found in enzyme activity between these two types of tissue. The muscle of both normal and dystrophic embryos contained high levels of enzyme activity which decreased shortly after hatching. By 12 weeks ex ovo enzyme titers in the normal pectoralis were sharply reduced and remained unchanged up to 60 weeks. By contrast, enzyme levels in the dystrophic pectoralis declined to a lesser degree after hatching and then rose sharply beginning at 12 weeks ex ovo and remained high in the mature bird. Cyclic AMP phosphodiesterase activity levels were altered in a similar manner in the two tissues.

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Section: Discussionmentioning

confidence: 99%

Adenyl Cyclase in the Pectoral Mnscle of Normal Chickens and Chickens with Hereditary Muscular Dystrophy

Bz¹,

Dh²

1972

Enzyme

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“…It was also established for human liver and skeletal muscle -although not directly for small-intestinal mucosa -that the first enzyme which appears during embryogenesis is the pure H type. The activity of M gene is first recognized by the occurrence of hybrid enzymes and finally develops the pure M type Kaplan and Cahn, 1962;Kar and Pearson, 1963). We suggest that the abnormal enterocytes are the main source of the altered LDH isoenzymes in primary malabsorption.…”

Section: Fast-migrating Anodic Fractions Of Ldh (Ldhmentioning

confidence: 82%

“…These five forms are recognized as distinct bands of LDH activity (LDH 1-5) after electrophoretic migration, if both subunits differ in net charge at the pH used. Different amino acid composition (Appella and Markert, 1961;Cahn et al, 1962;Kaplan, 1963), isolated mutation of H subunit in some mice strains (Costello and Kaplan, 1963;Shaw and Barto, 1963) inherited in accordance with the Mendelian rules, as well as isolated alterations in the synthesis of M or H subunit during embryogenesis, under influence of hormones, in diseases Wachsmuth, 1961a, 1961b;Wieme and Herpol, 1962;Kaplan and Cahn, 1962;Kar and Pearson, 1963;Lauryssens, Lauryssens and Zondag, 1964;Emery, 1964), after tissue denervation, removal to tissue cultures, changes in oxygen supply, and other conditions (Dawson, Goodfriend and Kaplan, 1964) indicate that the production of both subunits is controlled by two separate genes. The distribution of H and M enzymes in individual tissues and species reflects their metabolic requirements.…”

Section: Discussionmentioning

confidence: 99%

“…We suggest that the abnormal enterocytes are the main source of the altered LDH isoenzymes in primary malabsorption. At present it must be admitted that the cellular infiltration and oedema of the propria may also contribute to it, although Kaplan and Cahn (1962) do not think that the connective tissue of dystrophic muscles would be of major influence on the pathologic pattern of LDH isoenzymes in chicken muscular dystrophy. The heterogenous etiology of advanced pancreatic insufficiency in our patients does not allow to explain exhaustively the changes of LDH isoenzymes which were significant only in comparison with controls.…”

Section: Fast-migrating Anodic Fractions Of Ldh (Ldhmentioning

confidence: 96%

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Lactate Dehydrogenase Isoenzymes of Small-Intestinal Mucosa in Malabsorption of Intestinal and Pancreatic Origin

Frič¹,

Lojda²

1966

Enzymol Biol Clin

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Lactate dehydrogenase isoenzymes were investigated in supernatants of small-intestinal mucosa of 24 men and 18 females with the method of electrophoresis in agar gel and tétrazolium staining. In nontropical sprue and children with celiac disease the most positively charged fraction (LDH 5) was always decreased with simultaneous elevations of LDH 4, LDH 3, the ratio (LDH 3 + LDH 4) : LDH 5 and the value of H subunits. These changes were significant in comparison with controls and patients with secondary malabsorption of small-intestinal as well as pancreatic origin. In advanced exocrine pancreatic insufficiency changes significant in comparison with controls were also observed. The distribution of LDH isoenzymes in ileal adenocarcinoma resembled more closely the pattern of primary malabsorption than any other condition examined. The pattern of LDH isoenzymes of small intestinal mucosa in primary malabsorption approximates the distribution found in human foetal tissues. The evidence of identity of nontropical sprue and celiac disease of children at the molecular evel of the cell is presented. The relative activities of genes controlling the synthesis of LDH monomers in small-intestinal mucosa appear to be altered in favor of the gene controlling the synthesis of H subunits. LDH isoenzymes of jejunal supernatants in advanced pancreatic insufficiency may be influenced by various factors and more definite explanation of the observed changes cannot be given on the basis of the present material. The results are discussed in view of their possible significance for future studies on pathophysiology and heredity of primary malabsorption.

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“…We have also measured the activity ratio with two concentrations of substrate pyruvate. According to Kaplan et al [14] the Pyruvate 10-4M (low) activity ratio is a function of the quantity of M type. Pyruvate 3 10_3M (high)…”

Section: Methodsmentioning

confidence: 99%

Fetal-like Patterns of Lactic-Dehydrogenase and Aldolase Isozymes in some Pathological Conditions

Schapira¹,

Dreyfus²,

Schapira³

1966

Enzymol Biol Clin

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A study of the variations of multiple molecular forms of two enzymes, lactic dehydrogenase and aldolase, has been conducted in muscular diseases and in cancer. The changes in LDH patterns are most characteristic in muscle diseases. The trend is toward the reappearance of a fetal-like pattern. Aldolase shows a modification of specificity in cancerous tissues and in atrophied muscle. The most interesting change is the regression of the liver-specific aldolase in human and experimental hepatomas.

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Lactic Dehydrogenases and Muscular Dystrophy in the Chicken

Cited by 75 publications

References 7 publications

Adenyl Cyclase in the Pectoral Mnscle of Normal Chickens and Chickens with Hereditary Muscular Dystrophy

Adenyl Cyclase in the Pectoral Mnscle of Normal Chickens and Chickens with Hereditary Muscular Dystrophy

Lactate Dehydrogenase Isoenzymes of Small-Intestinal Mucosa in Malabsorption of Intestinal and Pancreatic Origin

Fetal-like Patterns of Lactic-Dehydrogenase and Aldolase Isozymes in some Pathological Conditions

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