Histochemical identification of the vascular endothelial isoenzyme of alkaline phosphatase.

Alkaline phosphatase (AP) is a widely studied membrane bound ecto-enzyme with an extensive distribution in nature. Three major human isoenzymes have been defined and can be distinguished on the basis of their differential sensitivity to specific inhibitors. Despite the voluminous literature describing AP, the physiological role of this enzyme is unclear. Microvascular endothelium is strongly AP positive and may provide a convenient model for study of the role of AP in vitro. This report describes the use of freeze-substitution and high-resolution plastic embedding techniques to identify the isoenzyme of endothelial AP by quantitative analysis of the relative inhibition by specific inhibitors of AP, using human gingival tissues and a number of rat tissues. Endothelial AP is found to be the liver/bone/kidney isoenzyme, indicating kidney as a credible source of enzyme for further experimental work investigating the role of AP.

[1]  R. Stinson,et al.  The solubilization of tetrameric alkaline phosphatase from human liver and its conversion into various forms by phosphatidylinositol phospholipase C or proteolysis. , 1988, The Journal of biological chemistry.

[2]  H. Harris,et al.  A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[3]  H. Harris,et al.  Structure of the human liver/bone/kidney alkaline phosphatase gene. , 1988, The Journal of biological chemistry.

[4]  C. Slaughter,et al.  Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[5]  W. Rutter,et al.  Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[6]  D. W. Moss,et al.  Modification of alkaline phosphatases by treatment with glycosidases. , 1985, Enzyme.

[7]  R. Lev,et al.  Colonic and small intestinal alkaline phosphatase. A histochemical and biochemical study. , 1982, Gastroenterology.

[8]  H. Harris Multilocus enzyme systems and the evolution of gene expression: the alkaline phosphatases as a model example. , 1980, Harvey lectures.

[9]  S. Posen,et al.  Clinical Utilization of Alkaline Phosphatase Measurements , 1979 .

[10]  B. Schofield,et al.  Histochemical demonstration of enzyme activities in plastic and paraffin embedded tissue sections. , 1979, Stain technology.

[11]  R. Mulivor,et al.  Differential inhibition of the products of the human alkaline phosphatase loci , 1978, Annals of human genetics.

[12]  M. Borgers THE CYTOCHEMICAL APPLICATION OF NEW POTENT INHIBITORS OF ALKALINE PHOSPHATASES , 1973, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[13]  J. Ahlqvist Freeze-substitution. A method applicable to routine surgical biopsies. , 2009, Acta pathologica et microbiologica Scandinavica. Section A, Pathology.

[14]  Dean J. Champion,et al.  Basic Statistics for Social Research , 1970 .

[15]  S. Posen,et al.  The action of EDTA on human alkaline phosphatases. , 1967, Biochimica et biophysica acta.

[16]  R. H. Eaton,et al.  Inhibition of the orthophosphatase and pyrophosphatase activities of human alkaline-phosphatase preparations. , 1967, The Biochemical journal.

[17]  W. Aldridge,et al.  The inhibition of enzymes by beryllium. , 1966, The Biochemical journal.

[18]  E. J. Knight,et al.  The route of re-circulation of lymphocytes in the rat , 1964, Proceedings of the Royal Society of London. Series B. Biological Sciences.

[19]  O. Bodansky The inhibitory effects of DL-alanine, L-glutamic acid, L-lysine, and L-histidine on the activity of intestinal, bone, and kidney phosphatases. , 1948, The Journal of biological chemistry.