scholarly journals Effect of Excessive Vitamin A on Alkaline Phosphatase Activity and Concentrations of Calcium-binding Protein and Bone Gla-protein in Culture Medium and CaBP mRNA Expression in Osteoblasts of Broiler Chickens

2010 ◽  
Vol 24 (2) ◽  
pp. 239-245 ◽  
Author(s):  
Xiaoyu Guo ◽  
Sumei Yan ◽  
Binlin Shi ◽  
Yongmiao Feng
Keyword(s):  
Alkaline Phosphatase ◽  
Vitamin A ◽  
Mrna Expression ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Calcium Binding ◽  
Broiler Chickens ◽  
Culture Medium ◽  
Calcium Binding Protein ◽  
Bone Gla Protein

Alkaline phosphatase activity in bovine oocytes and preimplantation embryos as affected by removal of the zona pellucida and culture medium constituents

2003 ◽  
Vol 15 (5) ◽  
pp. 285 ◽  
Author(s):  
J. L. Edwards ◽  
A. M. Powell ◽  
C. E. Rexroad Jr
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Zona Pellucida ◽  
Bovine Serum ◽  
Culture Medium ◽  
Preimplantation Embryos ◽  
Perivitelline Space ◽  
Mechanical Removal ◽  
Bovine Oocytes

The aims of the present study were: (1) to characterize alkaline phosphatase (AP) activity in bovine oocytes and embryos with intact or removed zona pellucida (ZP); and (2) to evaluate the effect of culture medium constituents on AP activity. Alkaline phosphatase activity in non-matured and matured oocytes was most evident nearest the plasma membrane and perivitelline space. In more than 90% of two- to 16-cell embryos, AP activity was observed in the perivitelline space and at blastomere contacts. In blastocysts, AP activity was localized to the trophectoderm. Only after immunodissection was AP activity detected in the inner cell mass. Removal of the ZP by pronase or mechanical means reduced AP activity. Alkaline phosphatase activity was detected in evacuated ZP after mechanical removal. Specific constituents comprising the embryo culture medium altered AP activity. Alkaline phosphatase activity was reduced in eight- to 16-cell embryos and evacuated ZP cultured in CR1aa + 0.4% bovine serum albumin compared with embryos cultured in CR1aa alone or embryos co-cultured on a monolayer of Buffalo rat liver cells in the presence of 10% fetal bovine serum. The presence of AP activity at blastomere contacts and in evacuated ZP limits its usefulness as a marker for the differentiation of embryonic cells comprising the early cleavage-stage embryo.

scholarly journals In vitro modulation of alkaline phosphatase activity in neutrophils from patients with chronic myelogenous leukemia by monocyte-derived activity

Blood ◽  
1986 ◽  
Vol 67 (2) ◽  
pp. 492-497 ◽  
Author(s):  
T Matsuo
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Culture Medium ◽  
Underlying Mechanism ◽  
Myelogenous Leukemia ◽  
Neutrophil Alkaline Phosphatase

Abstract To clarify the underlying mechanism of low neutrophil alkaline phosphatase (NAP) activity in chronic myelogenous leukemia (CML), CML neutrophils were cultured in liquid medium with different numbers of monocytes. Alkaline phosphatase activity in CML neutrophils, assessed cytochemically, increased with the numbers of monocytes. NAP activity was not induced by the interaction between neutrophils and monocytes, but by the presence of a monocyte-derived soluble activity. NAP activity in normal neutrophils was also lowered by depletion of monocytes from culture medium. Under such monocyte-depleted conditions, both CML and normal neutrophils proliferated and differentiated to produce mature neutrophils. Thus induction of NAP activity can be modified in vitro by changing the amount of NAP-inducing activity released from monocytes. However, whether a reduction of NAP-inducing activity in CML neutrophil is the cause of low NAP activity in vivo remains uncertain.

scholarly journals A new fluorescence method for alkaline phosphatase histochemistry.

1992 ◽  
Vol 40 (12) ◽  
pp. 1971-1974 ◽  
Author(s):  
G I Murray ◽  
S W Ewen
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Calcium Binding ◽  
Human Liver ◽  
Xylenol Orange ◽  
Single Step ◽  
Fluorescence Method ◽  
Step Procedure ◽  
Calcein Blue

We have developed a new fluorescence method for the histochemical localization of alkaline phosphatase activity. Calcium phosphate deposited at the sites of alkaline phosphatase activity in a Gomori-type reaction are identified by calcium binding fluorochromes. The calcium binding fluorochromes calcein, calcein blue, and xylenol orange were investigated, with each fluorochrome being included in the alkaline phosphatase incubating medium and used in a single-step procedure. Alkaline phosphatase activity was studied in freeze-substituted, resin-embedded human liver and jejunal biopsies, and each fluorochrome produced intense fluorescence of different colors at sites of alkaline phosphatase activity. Calcein, calcein blue, and xylenol orange produced green, blue, and red fluorescence, respectively. Sites of enzyme activity were accurately localized without evidence of diffusion, and there was an absence of non-enzyme-catalyzed binding of any of the fluorochromes to tissue. This fluorescence method, which is particularly suited to investigating the localization and distribution of the activity of different enzymes in the same section, was used to investigate the distribution and co-localization of alkaline phosphatase and aminopeptidase M in human liver and jejunum.

scholarly journals In vitro modulation of alkaline phosphatase activity in neutrophils from patients with chronic myelogenous leukemia by monocyte-derived activity

Blood ◽  
1986 ◽  
Vol 67 (2) ◽  
pp. 492-497
Author(s):  
T Matsuo
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Culture Medium ◽  
Underlying Mechanism ◽  
Myelogenous Leukemia ◽  
Neutrophil Alkaline Phosphatase

To clarify the underlying mechanism of low neutrophil alkaline phosphatase (NAP) activity in chronic myelogenous leukemia (CML), CML neutrophils were cultured in liquid medium with different numbers of monocytes. Alkaline phosphatase activity in CML neutrophils, assessed cytochemically, increased with the numbers of monocytes. NAP activity was not induced by the interaction between neutrophils and monocytes, but by the presence of a monocyte-derived soluble activity. NAP activity in normal neutrophils was also lowered by depletion of monocytes from culture medium. Under such monocyte-depleted conditions, both CML and normal neutrophils proliferated and differentiated to produce mature neutrophils. Thus induction of NAP activity can be modified in vitro by changing the amount of NAP-inducing activity released from monocytes. However, whether a reduction of NAP-inducing activity in CML neutrophil is the cause of low NAP activity in vivo remains uncertain.

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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