scholarly journals Semi-Automatic Rating Method for Neutrophil Alkaline Phosphatase Activity

2016 ◽  
Vol 31 (1) ◽  
pp. e22022 ◽  
Author(s):  
Kanae Sugano ◽  
Kotomi Hashi ◽  
Misaki Goto ◽  
Kiyotaka Nishi ◽  
Rie Maeda ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Rating Method ◽  
Neutrophil Alkaline Phosphatase

scholarly journals Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia

Blood ◽  
1975 ◽  
Vol 45 (3) ◽  
pp. 335-343
Author(s):  
D Rosenblum ◽  
SJ Petzold
Keyword(s):  
Alkaline Phosphatase ◽  
Polycythemia Vera ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Normal Subjects ◽  
Myelogenous Leukemia ◽  
Precipitin Line ◽  
Neutrophil Alkaline Phosphatase ◽  
Sepharose 4B

To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from patients with CML with that of normal subjects and patients with polycythemia vera (PRV). Antisera prepared in rabbits against granule alkaline phosphatase purified from the neutrophils of a patient with PRV produced a single precipitin line of antigenic identity when reacted with extracts of normal, PRV, and CML neutrophil granules. A histochemical stain for alkaline phosphatase activity (alpha-naphthyl acid phosphate coupled with Fast Blue RR) specifically stained the precipitin line. A variety of quantitative precipitin techniques failed to produce satisfactory precipitation of alkaline phosphatase activity. Comparative analyses were therefore performed by affinity chromatography using goat antirabbit-gammaglobulin linked to Sepharose 4B to adsorb alkaline phosphatase complexed with rabbit gamma globulin. With this method, 100% of CML, normal, and PRV alkaline phosphatase could be adsorbed. Using limiting concentrations of antibody, a proportionally smaller fraction of enzyme activity was absorbed as the concentration of PRV alkaline phosphatase or normal alkaline phosphatase was increased. Extracts of CML granules containing comparable amounts of protein but 200-fold less alkaline phosphatase activity per milligram did not specifically reduce adsorption. Thus, in CML, we found no evidence that the granulocytes contained a large amount of antigenically normal but enzymatically defective alkaline phosphatase. Examination of electron micrographs revealed no significant differences in the number or distribution of granules in the granulocytes of normal subjects or patients with PRV or CML. This suggests that the low level of neutrophil alkaline phosphatase in CML granulocytes is the result of decreased enzyme content and not a consequence of synthesis of catalytically defective enzyme.

scholarly journals Absent or Extremely Low Neutrophil Alkaline Phosphatase Activity Levels in Patients with Myelodysplastic Syndromes

2013 ◽  
Vol 52 (4) ◽  
pp. 479-482 ◽  
Author(s):  
Yataro Yoshida ◽  
Tatsuya Katsurada ◽  
Shigeru Oguma ◽  
Yukiharu Nakabo ◽  
Noriyoshi Yoshinaga ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Myelodysplastic Syndromes ◽  
Activity Levels ◽  
Neutrophil Alkaline Phosphatase

scholarly journals Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia

Blood ◽  
1975 ◽  
Vol 45 (3) ◽  
pp. 335-343 ◽  
Author(s):  
D Rosenblum ◽  
SJ Petzold
Keyword(s):  
Alkaline Phosphatase ◽  
Polycythemia Vera ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Normal Subjects ◽  
Myelogenous Leukemia ◽  
Precipitin Line ◽  
Neutrophil Alkaline Phosphatase ◽  
Sepharose 4B

Abstract To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from patients with CML with that of normal subjects and patients with polycythemia vera (PRV). Antisera prepared in rabbits against granule alkaline phosphatase purified from the neutrophils of a patient with PRV produced a single precipitin line of antigenic identity when reacted with extracts of normal, PRV, and CML neutrophil granules. A histochemical stain for alkaline phosphatase activity (alpha-naphthyl acid phosphate coupled with Fast Blue RR) specifically stained the precipitin line. A variety of quantitative precipitin techniques failed to produce satisfactory precipitation of alkaline phosphatase activity. Comparative analyses were therefore performed by affinity chromatography using goat antirabbit-gammaglobulin linked to Sepharose 4B to adsorb alkaline phosphatase complexed with rabbit gamma globulin. With this method, 100% of CML, normal, and PRV alkaline phosphatase could be adsorbed. Using limiting concentrations of antibody, a proportionally smaller fraction of enzyme activity was absorbed as the concentration of PRV alkaline phosphatase or normal alkaline phosphatase was increased. Extracts of CML granules containing comparable amounts of protein but 200-fold less alkaline phosphatase activity per milligram did not specifically reduce adsorption. Thus, in CML, we found no evidence that the granulocytes contained a large amount of antigenically normal but enzymatically defective alkaline phosphatase. Examination of electron micrographs revealed no significant differences in the number or distribution of granules in the granulocytes of normal subjects or patients with PRV or CML. This suggests that the low level of neutrophil alkaline phosphatase in CML granulocytes is the result of decreased enzyme content and not a consequence of synthesis of catalytically defective enzyme.

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.

Discordant neutrophil alkaline phosphatase activity and cytogenetic response in chronic myeloid leukemia treated with α-interferon

Pathology ◽  
1993 ◽  
Vol 25 (4) ◽  
pp. 363-366
Author(s):  
Debra L. Taylor ◽  
Anne-Marie Kerwick ◽  
Suzanne L. Elliott ◽  
Robyn L. Rodwell ◽  
Susan J. Wright ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Chronic Myeloid Leukemia ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Myeloid Leukemia ◽  
Cytogenetic Response ◽  
Neutrophil Alkaline Phosphatase
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