Evidence that alkaline phosphatase from human neutrophils is the same gene product as the liver/kidney/bone isoenzyme

Gainer, Anita L.; Stinson, Robert A.

doi:10.1016/0009-8981(82)90107-3

Cited by 45 publications

(18 citation statements)

References 12 publications

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“…The rate of solubilization of enzymes is higher in cytoplasm than in membrane prep aration [22]. It is difficult to assess the com plete recovery of membrane-linked compo nents with Triton X-100 alone; the yield is about 70-80% [14].…”

Section: Isoenzyme Types Found In Pmnmentioning

confidence: 99%

“…Recently, Gainer and Stinson [14] have analyzed the inhibition pattern of normal NAP in man. They postulated that NAP is identical to liver AP.…”

Section: Isoenzyme Types Found In Pmnmentioning

confidence: 99%

“…The AP isoen published [1, 6, 11, 14, 17, 18, 23-25, 29, 30], In the various papers quoted the AP isoenzymes were essentially identified using electrophoretic methods. Except in the work of Gainer and Stinson [14] dealing exclu sively with some inhibitory pattern, the nu merous investigations on the isoenzymes of granulocyte AP have shown contradictory re sults on the basis of electrophoretic studies. Close examination reveals obvious discrep ancies between the zymograms reported, the number of isoenzymes detected ranging from 1 to 4 [17,24,25,28].…”

Section: Introductionmentioning

confidence: 99%

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Liver- and Placenta-Like Alkaline Phosphatases (EC 3.1.3.1) Isoenzymes in Normal Human Neutrophils

Vergnes¹,

Grozdea²,

Corberand³

1984

Enzyme

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Alkaline phosphatase (AP) has been characterized in the neutrophil polymorphonuclear leukocytes (PMN) from 14 healthy adults. The biochemical properties of the isoenzymes were analyzed by the following methods: enzyme assays, slab gel electrophoresis, thermostability, inhibition pattern using four chemical inhibitors, and immunological specificity. In normal PMNs, two types of AP have been found: a thermolabile isoenzyme identical to the liver/bone/kidney type and a thermostable isoenzyme with respect to its electrophoretic properties, its level of thermostability, its immunological specificity, the thermostable isoenzyme resembles the placental form more closely than the intestinal form. These results are consistent with the proposal that granulocyte AP is a heterogeneous enzyme. Two enzyme forms appear to be expressed in this blood cell.

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Section: Isoenzyme Types Found In Pmnmentioning

confidence: 99%

“…Recently, Gainer and Stinson [14] have analyzed the inhibition pattern of normal NAP in man. They postulated that NAP is identical to liver AP.…”

Section: Isoenzyme Types Found In Pmnmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Liver- and Placenta-Like Alkaline Phosphatases (EC 3.1.3.1) Isoenzymes in Normal Human Neutrophils

Vergnes¹,

Grozdea²,

Corberand³

1984

Enzyme

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“…The ALP from tissues which express the tis sue-nonspecific enzyme (e.g. liver, bone, kid ney) all show indistinguishable patterns of inhibition with the inhibitors homoarginine, phenylglycylglycine, and phenylalanine [22,23], The inhibitor profile for the ALP from the lymphoma cells was also indistinguishable from the tissue-nonspecific isoenzyme (ta ble 2), but different from the isoenzymes of intestine and placenta.…”

Section: Discussionmentioning

confidence: 89%

Characterization of the Alkaline Phosphatase Expressed on the Surface of a Hodgkin's Lymphoma Cell Line

Belland

Visser²,

Poppema³

et al. 1993

Enzyme Protein

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Alkaline phosphatase solubilized from a human Hodgkin’s lymphoma cell line (L428) was compared with purified amphiphilic and hydrophilic forms of the enzyme from human liver, and with the enzyme solubilized from a cultured osteosarcoma cell line (Saos-2). Purified hydrophilic alkaline phosphatases from human placenta and intestine were also compared in some experiments. Alkaline phosphatase was released from the plasma membrane of intact lymphocytes by phosphatidylinositol phospholipase C and thus is anchored to the outside of the plasma membrane by covalently attached phosphatidylinositol. Enzyme released in this way was hydrophilic and that solubilized with Triton X-100 was amphiphilic, as assessed by adsorption to octyl-Sepharose. Lymphocyte alkaline phosphatase, when released from the membrane by phosphatidylinositol phospholipase C or solubilized by Triton X-100, had apparent M(r) values on gradient gel electrophoresis of 227 and 494 kDa, respectively. These values were consistently higher than equivalent ones obtained with enzymes purified from human liver, but were similar to those of cultured osteosarcoma cells. Isoenzyme-specific inhibitors of alkaline phosphatase showed similar patterns of inhibition between the enzyme from L428 cells and the tissue-nonspecific (liver/kidney/bone) isoenzyme from human liver. Heat stabilities were similar for the enzymes from L428 and Saos-2 (bone isoform) cell lines, but differed significantly from those of liver, intestine and placenta. We conclude that the alkaline phosphatase expressed in this lymphoma cell line (L428) has properties that most closely resemble those of the tissue-nonspecific isoenzyme found normally in osteoblasts of bone (bone isoform).

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“…Informed written consent was obtained from each individual. [ 10] procedure, kept in Krebs-Ringer buffer, were lysed by sonication (three bursts at 50 W for 30 s) and NAP was solubilized with 2% Triton X-100 and 20% n-butanol. After centrifugation at 6,000# for 15 min, the alcoholic phase was discarded and the aqueous layer recovered.…”

Section: Subjectsmentioning

confidence: 99%

Changes in Immunological Properties of Neutrophil Alkaline Phosphatase in Trisomy 21 Pregnancies

Grozdea

Vergnes

et al. 1994

Acta Haematol

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Immunoreactivity, cytochemical, immunocytochemical characteristics and subcellular distribution of neutrophil alkaline phosphatase (NAP) were investigated in blood and/or smear samples from 18 women aged 23-46 years (mean 32.5 years) with trisomy 21 fetuses (17-21 weeks) and 28 women aged 20-42 years (mean 31 years) with normal fetuses (17-22 weeks). Immunochemical NAP investigations were carried out in 8 pathological and 8 normal pregnancies; cytochemical and immunocytochemical procedures were carried out in 18 pregnant women with trisomy 21 fetuses and 28 controls. NAP from women with trisomy 21 fetuses is characterized by: (1) a significant decrease in reactivity with anti-liver-type alkaline phosphatase (AP) and anti-NAP antisera;(2)low or very slight reactivity with antiplacental or anti-intestinal antibodies;(3)marked dispersion of NAP lead citrate reaction products or anti-NAP antibody colloidal gold-labelling in neutrophil cytoplasms, as detected by electron microscopy. This subcellular AP distribution (extramembranous) is different from that of normal NAP sites associated with plasma membrane, nuclear membrane and secretory vesicles. The NAP immunochemical and cytochemical characteristics suggest that neutrophils of a woman with a trisomy 21 fetus contain two AP isoenzymes: the liver/bone type and an atypical AP.

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Evidence that alkaline phosphatase from human neutrophils is the same gene product as the liver/kidney/bone isoenzyme

Cited by 45 publications

References 12 publications

Liver- and Placenta-Like Alkaline Phosphatases (EC 3.1.3.1) Isoenzymes in Normal Human Neutrophils

Liver- and Placenta-Like Alkaline Phosphatases (EC 3.1.3.1) Isoenzymes in Normal Human Neutrophils

Characterization of the Alkaline Phosphatase Expressed on the Surface of a Hodgkin's Lymphoma Cell Line

Changes in Immunological Properties of Neutrophil Alkaline Phosphatase in Trisomy 21 Pregnancies

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