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The Clinical Biochemistry of 5'-Nucleotidase*

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The Clinical Biochemistry of 5'-Nucleotidase* ANNALS OF CLINICAL AND LABORATORY SCIENCE, Vol. 20, No. 2 Copyright © 1990, Institute for Clinical Science, Inc. The Clinical Biochemistry of 5'-Nucleotidase* F. WILLIAM SUNDERMAN JR., M.D. Departments of Laboratory Medicine and Pharmacology, University of Connecticut Medical School, Farmington, CT 06032 ABSTRACT This review delineates the subcellular distribution, biochemical charac­ teristics, and metabolic functions of 5'-nucleotidase (5'NT), summarizes the analytical biochemistry of 5'NT, and assesses the clinical significance of5'NT determinations in body fluids, cells, and tissues. Salient aspects of the clinical biochemistry of 5'NT, discussed herein, are as follows: (A) Serum 5'NT activity is generally elevated in hepatobiliary diseases, espe­ cially with intrahepatic obstruction, but, unlike serum alkaline phospha­ tase, serum 5'NT activity is not increased in infancy, childhood, preg­ nancy, or osteoblastic disorders. (B) In cancer patients, elevated serum 5'NT activity does not always indicate hepatobiliary involvement; in some cases, 5'NT may be released into serum from the primary tumor or local metastases. (C) Genetic deficiency of erythrocyte pyrimidine 5'NT activity is a common cause of hereditary non-spherocytic hemolytic anemia. (D) Acquired deficiency of erythrocyte pyrimidine 5'NT activity occurs in patients with P-thalassemia and lead poisoning. (E) 5'NT activity is low in circulating monocytes, increases markedly upon their differentiation to tissue macrophages, and subsequently diminishes during macrophage activation. (F) Lymphocyte ecto-5'NT activity, a plasma membrane marker of cell maturation, is generally low in immunodeficiency states, and undergoes characteristic changes in patients with certain lymphomas and leukemias. Introduction ribonucleosides and inorganic phos­ phate. Reis’s enzyme, now commonly In 1934, Reis1 0 9 reported that muscle termed ‘5'-nucleotidase’ (‘5'NT’) and for­ homogenates contain an enzyme activity mally designated as ‘5'-ribonucleotide that specifically hydrolyzes various phosphohydrolase’ (EC 3.1.3.5), com­ ribonucleoside-5 ' -monophosphates at prises a group of related enzymes that neutral pH to yield the corresponding are widely distributed in prokaryotic and eukaryotic organisms. Determinations of 5'NT activity in human serum, erythro­ * Presented at the Fortieth Anniversary Meeting of the Association of Clinical Scientists in Philadel­ cytes, leukocytes, and tissues have phia, PA, November 1989. become diagnostically important in cer­ 123 0091-7370/90/0300-0123 $02.00 © Institute for Clinical Science, Inc. 1 2 4 SUNDERMAN JR. tain hepatobiliary, hematological, immu­ myocyte ecto-5'NT . 1 2 7 In rat kidney, nological, and neoplastic disorders. The ecto-5'NT activity is located in the brush voluminous literature, prior to approxi­ border of proximal tubular cells and in mately 1970, on the clinical enzymology plasma membranes of cortical interstitial of 5'NT was reviewed by Bodansky and fibroblasts . 8 1 Based on the segregation S ch w artz , 2 3 Drummond and Yama­ pattern of ecto-5'NT activity in panels of moto , 4 9 and van der Slik et al. ; 1 4 8 more human/rodent hybrid cells, the genetic recent publications have been surveyed locus of ecto-5'NT resides on human by Belfield 1 1 and Ellis . 5 3 The goals of the chromosome 6 in the region from ql4 to present paper are (a) to summarize the q 2 1 . 2 8 , 2 9 distribution, properties, and functions of 5'NT; (b) to review the analytical bio­ P r o p e r t ie s chemistry of 5'NT; and (c) to delineate the clinical significance of measurements Since chelators generally inhibit 5'NT of 5'NT activities in body fluids, cells, activity and various divalent metal ions and tissues. restore the activity, 5'NT is probably a metalloprotein; the native constituent Distribution, Properties, and Functions metal has not been identified, but zinc is a likely candidate . 6 1 , 8 6 Based on studies SUBCELLULAR DISTRIBUTION AND of lymphocytes, myocytes, and renal G e n e t ic L o c u s cells, ecto-5'NT is a homodimeric or tetrameric glycoprotein, comprising two Activity of 5'NT is predominantly or four subunits of 6 8 to 70 kD .80,84,127 located in the plasma membrane of The pH optimum of 5'-NT activity mammalian cells . 7 , 6 0 5'-Nucleotidases ranges from 6.5 to 8.4, depending upon are also present, although in less abun­ the specific isoenzymes, substrates, dance, in mitochondria , 6 5 m icro - buffers, and reaction condi­ somes, 5 6 , 1 1 7 Golgi apparatus , 5 6 and cyto­ tions .68,120,122,129,160 The relative specific so l .143,146,158 Studies of hepatocytes, activities of 5'-adenososine monophos­ lymphocytes, and placental cells indicate phate (5'-AMP), 5'-uridine monophos­ that the ectoenzyme, ‘ecto-5'NT’, is phate (5'-UMP), 5'-guanosine mono­ anchored to the plasma membrane by a phosphate (5'-GMP), 5'-cytidine C-terminal glycolipid moiety that con­ monophosphate (5'-CMP), and 5'-ino- tains glycosyl phosphotidylinosi- sine monophosphate (5'-IMP) as sub­ to l .85,135,136,158,159 In rat hepatocytes, strates for ecto-5'NT of rat hepatocytes ecto-5'NT is a short-stalked integral are reported to be 100:81:63:63:59, membrane protein; the catalytic site respectively . 3 3 The relative specific activ­ faces the extracellular medium and little, ities of 5'-AMP, 5'-CMP, 5'-IMP, and if any, of the enzyme molecule extends 5'-GMP as substrates for ecto-5'NT of to the cytoplasmic surface of the plasma porcine lymphocytes are reported to be m em brane . 7 In contrast, in murine plas­ 100:65:50:45, respectively . 4 7 The 5'N T macytoma cells, ecto-5'NT is a trans­ activity of blood serum and plasma membrane protein . 1 5 6 In chicken gizzard membranes of lymphocytes, mammary myocytes, ecto-5'NT activity is stimu­ cells, glioma cells, and plasmacytoma lated by laminin and inhibited by fibro- cells is strongly inhibited by concanava- n ectin . 4 3 , 1 2 7 These two components of lin A (‘con A ’),32,37,82,126,160 but the cyto­ the extracellular matrix evidently inter­ plasmic 5'NT activity of plasmacytoma act with different binding sites of the cells and erythrocytes is unaffected by CLINICAL BIOCHEMISTRY OF 5'-NUCLEOTIDASE 1 2 5 con A . 1 1 2 , 1 6 0 Since con A binds to puri­ sine production by the 5'NT activity of fied ecto-5'NT in vitro, ecto-5'N T is interstitial fibroblasts helps to regulate believed to be a plasma membrane renal hemodynamics, glomerular filtra­ receptor for con A . 4 6 -4 7 -8 2 ’ 1 2 3 tion rate, and the release of renin and Human erythrocytes contain at least erythropoietin . 8 1 The microvillous two cytosolic 5'NT activities: First, there plasma membrane of syncytiotrophoblast is a cytosolic purine 5'NT that avidly in the human placenta is rich in hydrolyzes 5'-IMP and 5'-GMP, but ecto-5'NT activity, which may help to hydrolyzes 5'-AMP and other nucleoside modulate the feto-placental-maternal 5'-monophosphates at much lower microcirculation . 8 9 Human placental ra te s . 2 5 This p u rin e 5'N T activity is ecto-5'NT has FAD-pyrophosphatase inhibited by inorganic phosphate and activity that hydrolyzes flavin adenine strongly stimulated by adenosine tri­ dinucleotide (FAD) to riboflavin phos­ phosphate (ATP) and 2,3-diphosphoglyc- phate; whether or not ecto-5'nucleoti­ erate (2,3-DPG); the activity is higher in dases of other tissues hydrolyze FAD fresh erythrocytes than in outdated remains to be established . 7 9 In hum an c e lls . 2 5 Second, there is a cytosolic erythrocytes, cytosolic purine 5'NT is pyrimidine 5'NT that avidly hydrolyzes secondarily involved in the catabolism of 5'-UMP and 5'-CMP, but is inactive on 5'-AMP, which proceeds initially via purine 5'-ribonucleotides . 1 3 0 , 1 4 4 This deamination by adenosine deaminase to pyrimidine 5'NT activity is deficient in 5'-IMP, which is a preferred substrate patients with a common form of heredi­ for erythrocyte purine 5'NT . 2 5 , 1 4 6 In tary non-spherocytic hemolytic ane­ human erythrocytes, cytosolic pyrimi­ m ia , 1 7 1 4 4 and is inhibited in patients dine 5'NT dephosphorylates pyrimidine with (i-thalassemia4 0 ’ 1 5 1 and lead poison­ and deoxypyrimidine nucleotides . 1 4 4 in g .30,98’99’145 §everal isoenzymes of Pyrimidine 5'NT activity is high in retic­ erythrocyte pyrimidine 5'NT have been ulocytes, which contain abundant pyrim­ identified and characterized .35’36,97’130 idine nucleotides; pyrimidine 5'NT activity diminishes abruptly after F u n c t io n s nascent erythrocytes are released from the bone marrow . 2 0 , 2 1 As discussed sub­ The primary function of ecto-5'NT is sequently, pathological reduction of the conversion of extracellular nucleo­ erythrocyte pyrimidine 5'NT activity, as tides (e.g., 5'-AMP), to which cells are a consequence of hereditary enzyme generally impermeable, to the corre­ deficiency, (3-thalassemia, or lead poi­ sponding nucleosides (e.g., adenosine), soning, results in hemolytic anemia, which can readily enter most basophilic stippling, and elevated eryth­ cells .55,132,150 The half-life of adenosine in rocyte concentrations of 5'-CMP, 5'- plasma is brief; adenosine modulates cor­ UMP, and glutathione (GSH). onary, cerebral, and skeletal blood flow, affects neuronal activity and immune Analytical Biochemistry responses, and influences the metabolic of 5'-Nucleotidase effects of catecholamines . 9 5 , 1 2 5 In lym­ phocytes, 5'NT activity supplies nucleo­ C lassification o f 5 '-NT A ssays sides for cellular metabolism and nucleic acid synthesis under conditions where Techniques for the assay of 5'NT activ­ intracellular de novo synthesis of nucleo­ ity may be classified in eight major cate­ tides is lim ited .
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