Muscle biopsy in Pompe disease

Pompe disease (PD) can be diagnosed by measuring alpha-glucosidase levels or by identifying mutations in the gene enzyme. Muscle biopsies can aid diagnosis in doubtful cases.Methods:A review of muscle biopsy from 19 cases of PD (infantile, 6 cases; childhood, 4 cases; and juvenile/adult, 9 cases).Results:Vacuoles with or without glycogen storage were found in 18 cases. All cases had increased acid phosphatase activity. The vacuole frequency varied (almost all fibers in the infantile form to only a few in the juvenile/adult form). Atrophy of type 1 and 2 fibers was frequent in all forms. Atrophic angular fibers in the NADH-tetrazolium reductase and nonspecific esterase activity were observed in 4/9 of the juvenile/adult cases.Conclusion:Increased acid phosphatase activity and vacuoles were the primary findings. Most vacuoles were filled with glycogen, and the adult form of the disease had fewer fibers with vacuoles than the infantile or childhood forms.

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Acid Phosphatase Activities in Developing Seeds of Pisum sativum L

Functional Plant Biology ◽

10.1071/pp9770843 ◽

1977 ◽

Vol 4 (6) ◽

pp. 843 ◽

Cited By ~ 18

Author(s):

DR Murray ◽

MD Collier

Keyword(s):

Acid Phosphatase ◽

Pisum Sativum ◽

Phosphatase Activity ◽

Cell Expansion ◽

Acid Phosphatase Activity ◽

Minor Components ◽

Ph Optimum ◽

Pisum Sativum L ◽

Almost All ◽

Pea Seed

The seedcoats contain almost all of the acid phosphatase activity (EC 3.1.3.2) in the pea seed in the earliest stages of expansion. The seedcoat activity is maximal by the end of the period of rapid cell expansion and declines as the embryo matures. The developing cotyledons show a later rise in acid phosphatase activity to a maximum shortly before dehydration. The activity in the embryonic axis shows a marked increase only during dehydration. The acid phosphatase activity in the seedcoats results almost entirely from an isoenzyme with high electrophoretic mobility in 5.5% polyacrylamide gels (RF 0.97). This isoenzyme has not been detected in other tissues from the plant. The phosphatase activity in the cotyledons is accounted for by one major isoenzyme at RF 0.75 and by four minor components. The partially purified enzyme from the seedcoats shows a broad pH optimum from pH 5.0 to pH 6.0. In contrast, the preparation from the cotyledons has an optimum close to pH 5.6 and is slightly more sensitive to inhibition by 0.2 mM PI.

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PHOSPHOMONOESTERASE ACTIVITY IN THE LIFE-CYCLE STAGES OF SCHISTOCERCA GREGARIA

The Canadian Entomologist ◽

10.4039/ent100649-6 ◽

1968 ◽

Vol 100 (6) ◽

pp. 649-655 ◽

Cited By ~ 3

Author(s):

S. N. H. Naqvi ◽

Shahid H. Ashrafi ◽

M. A. H. Qadri

Keyword(s):

Alkaline Phosphatase ◽

Acid Phosphatase ◽

Embryonic Development ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Acid Phosphatase Activity ◽

Schistocerca Gregaria ◽

Adult Males ◽

First Instar ◽

Almost All

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.

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G.P.11.08 Cytoplasmic body with acid phosphatase activity – Hallmark of adult-onset Pompe disease on muscle pathology

Neuromuscular Disorders ◽

10.1016/j.nmd.2008.06.268 ◽

2008 ◽

Vol 18 (9-10) ◽

pp. 802

Author(s):

I. Nishino ◽

Y. Oya ◽

K. Monma ◽

S. Noguchi ◽

Y.K. Hayashi ◽

...

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Pompe Disease ◽

Acid Phosphatase Activity ◽

Muscle Pathology ◽

Adult Onset ◽

Cytoplasmic Body

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HISTOCHEMICAL COMPARISON OF FROG AND RAT MAST CELLS

Journal of Histochemistry & Cytochemistry ◽

10.1177/19.6.369 ◽

1971 ◽

Vol 19 (6) ◽

pp. 369-375 ◽

Cited By ~ 14

Author(s):

HERBERT CHIU ◽

DAVID LAGUNOFF

Keyword(s):

Acid Phosphatase ◽

Mast Cells ◽

Phosphatase Activity ◽

Alcian Blue ◽

Toluidine Blue ◽

Acid Phosphatase Activity ◽

Proteolytic Enzymes ◽

Nonspecific Esterase ◽

Esterase Activities ◽

Rat Mast Cells

Histochemical procedures were used to compare the constituents of frog and rat mast cells. On the basis of staining with acidified toluidine blue and the Alcian Blue-safranin combination, a substance characterized as heparin in rat cells was identified in frog mast cells. In contrast to their presence in rat cells, no histamine, serotonin or catecholamines could be observed in frog mast cells with the o-phthalaldehyde and paraformaldehyde reactions. A search for activities of two proteolytic enzymes, chymotrypsin-like and trypsin-like esterases, in frog mast cells was unsuccessful. β-Glucuronidase, N-acetyl-β-d-glucosaminidase and nonspecific esterase activities were demonstrated in both frog and rat mast cells; acid phosphatase activity was detected in frog but not rat mast cells.

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Erythrophagocytosis in the Liver in Hemolytic Anemias

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100100664 ◽

1968 ◽

Vol 26 ◽

pp. 184-185

Author(s):

O. T. Minick ◽

E. Orfei ◽

F. Volini ◽

G. Kent

Keyword(s):

Acid Phosphatase ◽

Oxidative Damage ◽

Phosphatase Activity ◽

Kupffer Cells ◽

Acid Phosphatase Activity ◽

Common Type ◽

Red Cell ◽

Cell Fragments ◽

Reticulo Endothelial System ◽

Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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