scholarly journals Simultaneous demonstration of acid phosphatase and glucose-6-phosphate dehydrogenase in mouse hepatocytes. A novel electron-microscopic dual staining enzyme-cytochemistry

10.4081/1685 ◽  
2010 ◽  
Vol 46 (3) ◽  
pp. 237 ◽  
Author(s):  
S Matsubara
Keyword(s):  
Acid Phosphatase ◽  
Electron Microscopic ◽  
Enzyme Cytochemistry ◽  
Mouse Hepatocytes ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Dual Staining

Integrated morphometrical and electron energy loss image analysis in cytochemistry

1989 ◽  
Vol 47 ◽  
pp. 402-403
Author(s):  
W.C. de Bruijn ◽  
A.A.W. de Jong ◽  
C.W.J. Sorber
Keyword(s):  
Image Analysis ◽  
Acid Phosphatase ◽  
Chemical Analysis ◽  
Active Form ◽  
List Type ◽  
Type Number ◽  
Enzyme Cytochemistry ◽  
Related Data ◽  
Endogenous Peroxidase ◽  
Electron Energy Loss

One aspect of enzyme cytochemistry is, whether all macrophage lysosomal hydrolytical enzymes are present in an active form, or are activated upon stimulation. Integrated morphometrical and chemical analysis has been chosen as a tool to illucidate that cytochemical problem. Mouse peritoneal resident macrophages have been used as a model for this complicated integration of morphometrical and element-related data. Only aldehyde-fixed cells were treated with three cytochemical reactions to detect different enzyme activities within one cell (for details see [1,2]). The enzyme-related precipitates anticipated to be differentiated, were:(1).lysosomal barium and sulphur from aryl sulphatase activity,(2).lysosomal cerium and phosphate from acid phosphatase activity and(3).platinum/di-amino-benzidine( D A B) complex from endogenous peroxidase activity.

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

scholarly journals Electron Microscopic Radioautographic Study on Protein Synthesis in Mitochondria of Binucleate Hepatocytes of Aging Mice

2007 ◽  
Vol 7 ◽  
pp. 1008-1023 ◽  
Author(s):  
Tetsuji Nagata
Keyword(s):  
Protein Synthesis ◽  
Labeling Index ◽  
Electron Microscopic ◽  
Protein Precursor ◽  
Binucleate Cells ◽  
Mouse Hepatocytes ◽  
Electron Microscopic Radioautography ◽  
Liver Tissues

In order to study the aging changes of intramitochondrial protein synthesis in mouse hepatocytes, 10 groups of aging mice, each consisting of three individuals, total 30, from fetal day 19 to postnatal year 2, were injected with3H-leucine, a protein precursor, sacrificed 1 h later, and the liver tissues processed for electron microscopic radioautography. On electron microscopic radioautograms obtained from each animal, the numbers of mitochondria, the numbers of labeled mitochondria, and the mitochondrial labeling index labeled with3H-leucine that showed protein synthesis in each hepatocyte, both mononucleate and binucleate cells, were counted and the averages in respective aging groups were compared. From the results, it was demonstrated that the numbers of mitochondria, the numbers of labeled mitochondria, and the labeling indices of intramitochondrial protein syntheses in both mononucleate and binucleate hepatocytes of mice at various ages increased due to development of animals. The numbers of mitochondria, the numbers of labeled mitochondria, and the labeling indices of intramitochondrial protein synthesis in binucleate hepatocytes were more than those of mononucleate hepatocytes at the same aging stages.

scholarly journals Lymphocyte Lysosomes and Lysosomal Enzymes in Chronic Lymphocytic Leukemia

Blood ◽  
1973 ◽  
Vol 41 (4) ◽  
pp. 511-518 ◽  
Author(s):  
Steven D. Douglas ◽  
Georg Cohnen ◽  
Erika KÖnig ◽  
GÜnter Brittinger
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Microscopic Level ◽  
Lymphocytic Leukemia ◽  
Electron Microscopic Level ◽  
Acid Hydrolase ◽  
Electron Microscopic ◽  
Normal Cells ◽  
Biochemical Studies ◽  
Cell Profile

Abstract Electron microscopic cytochemical and biochemical studies of lysosomal markers have been performed in unstimulated normal and chronic lymphotic leukemia (CLL) lymphocytes. Decreased activities of the lysosomal enzymes acid phosphatase and β-glucuronidase but not of the nonlysosomal enzyme malate dehydrogenase were observed in CLL lymphocytes as compared to normal cells. At the electron microscopic level, the number of membrane-bounded acid phosphatase-positive organelles was diminished in CLL cells. (Average 1.07 per cell profile in normal cells and 0.17 in CLL lymphocytes). The findings indicate that the diminution of acid hydrolase activities in CLL lymphocytes is most likely due to a reduced number of lysosomes, rather than to a diminished enzyme content of these organelles.

Acid Phosphatase Activity in Spiral Ganglion Neurons of C57BL/6 Mice

1998 ◽  
Vol 4 (S2) ◽  
pp. 1104-1105
Author(s):  
Glenn M. Cohen
Keyword(s):  
Acid Phosphatase ◽  
Spiral Ganglion ◽  
Distribution Patterns ◽  
Electron Microscopic ◽  
Age Related ◽  
Sensory Hair Cells ◽  
Dense Deposits ◽  
Underlying Mechanisms ◽  
Ganglion Neurons ◽  
Marker Molecule

C57BL/6 mice, along with several other mouse genotypes, have served as models for human presbycusis (age-related hearing losses). C57BL/6 mice and their genetic substrain C57/M6 show progressively severe hearing losses, starting as early as 30 days postnatally. The hearing losses result from sweeping degeneration of sensory (hair) cells and neurons that begins in the basal end of the cochlea and advances apically. Although the underlying mechanisms orchestrating sensory and neural degeneration are not known, it is possible to correlate degenerative events with the cytoplasmic levels and distribution patterns of a marker molecule, such as acid phosphatase (AP). AP, a representative lysosomal enzyme, plays a role in both normal cellular metabolism and degenerative changes (trauma and senescence). AP activity is visualized histochemically at the light and electron microscopic levels by the presence of dense deposits within lysosomes.

Leakage of periplasmic enzymes from lipopolysaccharide-defective mutants of Salmonella typhimurium

1976 ◽  
Vol 22 (10) ◽  
pp. 1549-1560 ◽  
Author(s):  
Arun K. Chatterjee ◽  
Helen Ross ◽  
Kenneth E. Sanderson
Keyword(s):  
Acid Phosphatase ◽  
Salmonella Typhimurium ◽  
Osmotic Shock ◽  
Significant Proportion ◽  
Phosphoglucose Isomerase ◽  
Nutrient Broth ◽  
Higher Temperature ◽  
Ribonuclease I ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Smooth Strain

Mutants of Salmonella typhimurium with defects in the heptose region of the lipopolysaccharide (LPS) molecule (heptose-deficient, chemotype Re) leak periplasmic enzymes (acid phosphatase (EC 3.1.3.2), cyclic phosphodiesterase, ribonuclease I (EC 3.1.4.22), and phosphoglucose isomerase (EC 5.3.1.9) (PGI is at least partially periplasmic in E. coli and S. typhimurium; see below)) and do not leak an internal enzyme (glucose-6-phosphate dehydrogenase) into the growth medium. The extent of this leakage is markedly increased at higher temperature (42 °C). Leakage of periplasmic enzymes from the strains lacking units distal to heptose I in the LPS molecule (chemotype Rd2) occurs only at 42 °C, and not at 30 or 37 °C. The extent of leakage of these enzymes from smooth strain and mutants of other LPS chemotypes (Rc, Rd1) is not significant, and is not influenced by growth temperatures. The kinetics of leakage of periplasmic enzymes after shift to 42 °C in nutrient broth reveal an accelerated release into the medium from heptose-deficient strains of cyclic phosphodiesterase and ribonuclease I after 30 min at 42 °C, and phosphoglucose isomerase after 60 min at 42 °C; at 30 °C the rate of release of cyclic phosphodiesterase and ribonuclease I is relatively slower. After 60 min at 42 °C in nutrient broth, growth of these strains has either slowed down or stopped. In L-broth, which permits the growth of the heptose-deficient strain (SA1377) at 42 °C, leakage of cyclic phosphodiesterase and phosphoglucose isomerase occurs, whereas there is no detectable leakage of these enzymes from the isogenic smooth strain (SA 1355). Thus, leakage of the periplasmic enzymes from the heptose-deficient strain occurs with or without growth. Mg2+ (0.75 mM), sodium chloride (50 mM), and sucrose (100 mM) in nutrient broth at 42 °C prevent the leakage of these enzymes. The shedding of LPS from the heptose-deficient as well as the smooth strains is enhanced by high temperature (42 °C), whereas considerable leakage of protein occurs only in the heptose-deficient strain at 42 °C and not in the smooth strain. The smooth and heptose-deficient strains are equally sensitive to osmotic shock although a significant proportion of acid phosphatase and cyclic phosphodiesterase activities from the heptose-deficient cells grown at 42 °C comes off in the Tris-NaCl wash step suggesting a rather loose attachment of these enzymes onto the cell surface.

scholarly journals Equine Glucose-6-phosphate Dehydrogenase Deficiency

1994 ◽  
Vol 31 (5) ◽  
pp. 518-527 ◽  
Author(s):  
S. L. Stockham ◽  
J. W. Harvey ◽  
D. A. Kinden
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
G6pd Deficiency ◽  
Dehydrogenase Deficiency ◽  
Reduced Glutathione ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Electron Microscopic ◽  
Transmission Electron ◽  
Transmission Electron Microscopic ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Glucose 6 Phosphate Dehydrogenase

Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a well-characterized X-linked inherited disorder in humans but has not been reported in horses. We describe a persistent hemolytic anemia and hyperbilirubinemia due to a severe G6PD deficiency in an American Saddlebred colt. Other abnormalities in the colt's erythrocytes as compared with those of healthy horses ( n = 22–35) included increased activities of hexokinase and pyruvate kinase, decreased concentrations of reduced glutathione and reduced nicotinamide adenine dinucleotide phosphate (NADP), and increased concentration of oxidized NADP. Morphologic abnormalities included eccentrocytosis, pyknocytosis, anisocytosis, macrocytosis, and increased number of Howell-Jolly bodies. Scanning and transmission electron microscopic examinations revealed that eccentrocytes had contracted to spherical regions and thin collapsed regions. Eccentrocytes were more electron dense than were normal erythrocytes when examined by transmission electron microscopy. When exposed to acetylphenylhydrazine, erythrocytes from the G6PD-deficient colt produced more and smaller Heinz bodies than did erythrocytes from normal horses. Abnormalities in the colt's dam included presence of eccentrocytes and pyknocytes; her average erythrocyte G6PD activity was slightly below the range of reference values.

scholarly journals HYDROLYTIC ENZYMES DURING SPERMATOGENESIS IN RAT AN ELECTRON MICROSCOPIC AND HISTOCHEMICAL STUDY

1968 ◽  
Vol 16 (4) ◽  
pp. 249-262 ◽  
Author(s):  
ZOLTAN POSALAKI ◽  
DEZSÖ SZABÓ ◽  
ERNÖ BÁCSI ◽  
ISTVÁN ÖKRÖS
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Sertoli Cells ◽  
Hydrolytic Enzymes ◽  
Appreciable Amount ◽  
Second Phase ◽  
Nonspecific Esterase ◽  
Electron Microscopic ◽  
Two Phases

The localization of lipids and the activities of nonspecific esterase, aryl sulfatase and acid phosphatase were studied in different stages of spermatogenesis in rats. In addition, the distribution of acid phosphatase activity was demonstrated electron histochemically. The spermatogenetic cycle was divided into two phases—corresponding to the first and the last four stages of Roosen-Runge-Giesel (RG) classification. Spermatids in the first phase contained abundant endoplasmic reticulum with rosette formation and well developed Golgi apparatus with numerous vesicles. They displayed high activity of hydrolytic enzymes but contained no appreciable amount of lipids. The Sertoli cells contained large lipid granules but showed minimal enzyme activity. During the second phase reduction of the cytoplasm of spermatids with fragmentation of the endoplasmic reticulum and Golgi lamellae, accumulation of lipids, aggregation of ribonucleo-protein particles, formation of residual bodies and marked decrease of enzyme activity were seen. The Sertoli cells contained large mitochondria, well developed endoplasmic reticulum and numerous dense bodies and revealed high activities of hydrolytic enzymes and rapid depletion of lipids. These ultrastructural and histochemical findings suggested an interaction between the Sertoli cells and the developing spermatids which probably contributed to the regulation of spermatogenesis.

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