The Localization of Alkaline Phosphatase during the Post-embryonic Development of Drosophila melanogaster

1950 ◽  
Vol s3-91 (13) ◽  
pp. 89-105
Author(s):  
T. YAO
Keyword(s):  
Alkaline Phosphatase ◽  
Drosophila Melanogaster ◽  
Embryonic Development ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Larval Instar ◽  
Morphological Evidence ◽  
Simultaneous Increase ◽  
Endocrine Organs ◽  
Pericardial Cells

1. The localization of alkaline phosphatase during the post-embryonic development of Drosophila melanogaster has been described. 2. In the larvae, nuclear phosphatase is always demonstrable, but cytoplasmic phosphatase shows a more restricted distribution. Salivary glands, mid-gut, Malpighian tubes, and pericardial cells are richest in cytoplasmic phosphatase. 3. The larva prior to puparium formation is characterized by a decrease of alkaline phosphatase in the internal organs with a simultaneous increase in the hypodermis. 4. The phosphatase data support the view that the prepupa is actually an intrapuparial larval instar. 5. Pupation is accompanied, by a very noticeable increase of alkaline phosphatase which is mainly confined to the cytoplasm. The high enzyme activity is maintained for the first day and a half after head eversion: there is a subsequent decline until at the time of emergence most organs are inactive. However, certain organs retain their alkaline phosphatase activity. 6. As in embryogenesis, alkaline phosphatase seems to be more concerned with histo-differentiation than with chemo-differentiation. 7. Alkaline phosphatase (and also acid phosphatase) actively participates in the process of histolysis or cellular degeneration. 8. The alkaline phosphatase activity of the pericardial cells, together with other morphological evidence, indicates that these cells are endocrine organs which play important roles in Drosophila metamorphosis. 9. Cytochemical evidence suggests that alkaline phosphatase in Drosophila is probably playing a part in the carriage of organic substances across the membrane barrier.

Identification of intracellular sites of superoxide production in stimulated neutrophils

1998 ◽  
Vol 111 (1) ◽  
pp. 81-91 ◽  
Author(s):  
T. Kobayashi ◽  
J.M. Robinson ◽  
H. Seguchi
Keyword(s):  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Time Course ◽  
Superoxide Production ◽  
Human Neutrophils ◽  
Morphological Evidence ◽  
Marker Enzyme ◽  
Intracellular Compartments

In this study, we show that superoxide production is carried out within intracellular compartments of human neutrophils and not at the plasma membrane following stimulation with phorbol myristate acetate. Oxidant production was not observed in unstimulated cells. Stimulated cells exhibited superoxide production in two distinct types of intracellular organelles. Initially, activity was detected in slender rod-shaped granules and in spherical or elliptical granules. The oxidant-producing granules fused directly with the plasma membrane or fused to form larger intracellular vesicles which then became associated with the plasma membrane. Longer periods of stimulation with PMA resulted in a decrease in the number of vesicles containing oxidant reaction product only, and an increase in structures containing both the oxidant-reaction product and ferritin particles; the latter was used herein as a marker for endocytosis. Thus a complex pattern of intracellular vesicular trafficking occurs in stimulated neutrophils. Alkaline phosphatase activity, a marker enzyme for a type of intracellular neutrophil granule was co-localized in the oxidant reaction-positive intracellular compartments. The time course of up-regulation of alkaline phosphatase activity to the cell surface parallelled the release of superoxide from stimulated cells. Results from this study demonstrate for the first time cytochemical and morphological evidence that superoxide is released from stimulated neutrophils through exocytosis of an oxidant-producing intracellular granule.

PHOSPHOMONOESTERASE ACTIVITY IN THE LIFE-CYCLE STAGES OF SCHISTOCERCA GREGARIA

1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
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.

LEUCOCYTE METABOLISM IN PREGNANCY

1960 ◽  
Vol XXXV (IV) ◽  
pp. 575-584 ◽  
Author(s):  
C. Borel ◽  
J. Frei ◽  
A. Vannotti
Keyword(s):  
Alkaline Phosphatase ◽  
Oxygen Consumption ◽  
Pregnant Women ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Lactate Production ◽  
Glucose Consumption ◽  
In Pregnancy

ABSTRACT Enzymatic studies, on leucocytes of pregnant women, show an increase of the alkaline phosphatase activity and a decrease of the glucose consumption and lactate production, as well as of proteolysis. The oxygen consumption, with succinate as substrate, does not vary.

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