Low-molecular-weight protein tyrosine phosphatase and human disease: In search of biochemical mechanisms

Archivum Immunologiae et Therapiae Experimentalis

Volumn 50, Issue 2, 2002, Pages 95-104

  Bottini, Nunzio ^a   Bottini, Egidio ^b   Gloria Bottini, Fulvia ^b   Mustelin, Tomas ^a  

^a BURNHAM INSTITUTE   (United States)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

Allergy; Asthma; Genetic polymorphisms; Obesity; Tyrosine phosphatase

Indexed keywords

ACP1 PROTEIN, HUMAN; ISOENZYME; ONCOPROTEIN; PROTEIN TYROSINE PHOSPHATASE;

ALTERNATIVE RNA SPLICING; ALZHEIMER DISEASE; ASTHMA; BRAIN; CARDIOMEGALY; DIABETES MELLITUS; ENTERITIS; ENZYMOLOGY; FAVISM; FEMALE; GENETIC POLYMORPHISM; GENETICS; HUMAN; HYPERSENSITIVITY; MALARIA; METABOLISM; OBESITY; PHYSIOLOGY; PREGNANCY; PRENATAL DEVELOPMENT; REVIEW; RHEUMATOID ARTHRITIS;

ALTERNATIVE SPLICING; ALZHEIMER DISEASE; ARTHRITIS, RHEUMATOID; ASTHMA; BRAIN; CARDIOMEGALY; DIABETES MELLITUS; EMBRYONIC AND FETAL DEVELOPMENT; FAVISM; FEMALE; HUMANS; HYPERSENSITIVITY; INFLAMMATORY BOWEL DISEASES; ISOENZYMES; MALARIA; OBESITY; POLYMORPHISM, GENETIC; PREGNANCY; PROTEIN-TYROSINE-PHOSPHATASE; PROTO-ONCOGENE PROTEINS;

EID: 0036367267     PISSN: 0004069X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (80)

1. AMANTE A., GLORIA-BOTTINI F. and BOTTINI E. (1990): Intrauterine growth: association with acid phosphatase genetic polymorphism. J. Perinat. Med., 18, 275-282.
2. BERTI A., RICACCI S., RAUGEI G., DEGL'INNOCENTI D. and RAMPONI G. (1994): Inhibition of cellular response to platelet-derived growth factor by low Mr phosphotyrosine protein phosphatase overexpression. FEBS Lett., 349, 7-12.
3. BOIVIN P. and GALAND C. (1986): The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3. Bioehem. Biophys. Res. Commun., 134, 557-564.
4. BOTTINI E. (1999): Association between cytosolic low molecular weight phosphotyrosine-phosphatase and malaria -a possible mechanism. Am. J. Phys. Anthropol., 108, 241-244.
5. BOTTINI E., CRAPELLA E., SCACCHI R., LUCARINI N., GLORIA-BOTTINI F., PASCONE R., BONCI E. and MAGGIONI G. (1985): Serum haptoglobin appearance during neonatal period is associated with acid phosphatase (ACP1) phenotvpe. Early Hum. Dev., 10, 237-243.
6. BOTTINI E., COSMI E., NICOTRA M., SANTEUSANIO G., LA TORRE M., BOTTINI N. and LUCARINI N. (1998): The genetics of signal transduction and the feto-maternal relationship. A study of cytosolic low molecular weight phosphotyrosine phosphatase. Dis. Markers, 14, 143-150.
7. BOTTINI E., GLORIA-BOTTINI F. and BORGIANI P. (1995): ACP1 and human adaptability. 1. Association with common diseases: a case-control study. Hum. Genet., 96, 629-637.
8. BOTTINI E., GLORIA-BOTTINI F., BORGIANI P. and BUSINCO L. (1997): Association between ACP1 and favism: a possible biochemical mechanism. Blood, 89, 2613-2615.
9. BOTTINI E., LUCARELLI P., AGOSTINO R., PALMARINO R., BUSINCO L. and ANTOGNONI G. (1971): Favism: association with erythrocyte acid phosphatase phenotype. Science, 171, 409-411.
10. BOTTINI E., LUCARINI N., GERLINI G., FINOCCHI G., SCIRE G. and GLORIA-BOTTINI F. (1990): Enzyme polymorphism and clinical variability of diseases: study of acid phosphatase locus 1 (ACP1) in obese subjects. Hum. Biol., 62, 403.
11. BOTTINI E., PALMARINO R., LUCARELLI P., LISTA R. and BOTTINI N. (2001): ACP1 and human adaptability: association with past malarial morbidity in the Sardinian population. Am. J. Hum. Biol., 13, 753-760.
12. BOTTINI N., GLORIA-BOTTINI F., LUCARINI N., RONCHETTI P. G. and FONTANA L. (2000): Inflammatory bowel disease: Are there gender differences in the genetics of signal transduction? A preliminary study of cytosolic low molecular weight protein tyrosine phosphatase. Dis. Markers, 16, 163-166.
13. BOTTINI N., MACMURRAY J., PETERS W., RHOSTAMKANI M. and COMINGS D, E. (2001): Association of the acid phosphate (ACP1) gene with triglyceride levels in obese post-menopausal women: potential relevance to the development of the metabolic syndrome (submitted).
14. BOTTINI N., MAO X. Q., BORGIANI P., SACCUCCI P., STEFANINI L., GRECO E., FONTANA L., SHIRAKAWA T. and HOPKIN J. M. (2001): Low molecular weight PTP - IL-4RA interaction in atopy predisposition. Eur. J. Allerg. Clin. Immunol. (in press).
15. BOTTINI N., MELONI G. F., BORGIANI P., GIORGINI A., BUZZETTI R., POZZILLI P., LUCARELLI P. and GLORIA-BOTTINI F. (2001): Genotypes of cytosolic low molecular weight protein tyrosine phosphatase (cLMWPTP or ACP1) correlate with age at onset of type 1 diabetes in sex specific manner (submitted).
16. BOTTINI N., STEFANINI L., WILLIAMS S., ALONSO A., MERLO J., JASCUR T., COUTURE C. and MUSTELIN T. (2001): Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP) (submitted).
17. BRYSON G. L., MASSA H., TRASK B. J. and VAN ETTEN R. L. (1995): Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1. Genomics, 30, 133-140.
18. CHERNOFF J. and LI H. C. (1985): A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase. Arch. Biochem. Biophys., 240, 135-145.
19. CHIARUGI P., CIRRI P., MARRA F., RAUGIE G., CAMICI G., MANAO G. and RAMPONI G. (1997): LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signaling. Biochem. Biophys. Res. Commun., 238, 676-682.
20. CIRRI P., CHIARUGI P., CAMICI G., MANAO G., RAUGIE G., CAPPUGI G. and RAMPONI G. (1993): The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase. Eur. J. Biochem., 214, 647-657.
21. CIRRI P., FIASCHI T., CHIARUGI P., CAMICI G., MANAO G., RAUGEI G. and RAMPONI G. (1996): The molecular basis of the differing kinetic behavior of the two low molecular mass phosphotyrosine protein phosphatase isoforms. J. Biol. Chem., 271, 2604-2607.
22. COMINGS D., ROSTAMKANI M., BOTTINI N. and MACMURRAY J. (2001): Association between the acid phosphatase (ACP1) gene and Alzheimer's disease (submitted).
23. DISSING J. (1987): Immunochemical characterization of human red cell acid phosphatase isozymes. Biochem. Genet., 25, 901-918.
24. DISSING J. and JOHNSEN A. H. (1992): Human red cell acid phosphatase (ACP1): The primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles. Biochim. Biophys. Acta, 1121, 261-268.
25. DISSING J., JOHNSEN A. H. and SENSABAUGH G. F. (1991): Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele. J. Biol. Chem., 266, 20619-20625.
26. DISSING J., RANGAARD B. and CHRISTENSEN U. (1993): Activity modulation of the fast and slow isozymes of human cytosolic low-molecular-weight acid phosphatase (ACP1) by purines. Biochim. Biophys. Acta, 1162, 275-282.
27. DISSING J. and SVENSMARK O. (1990): Human red cell acid phosphatase: purification and properties of the A, B, and C isozymes. Biochim. Biophys. Acta, 1041, 232-242.
28. FUCHS K. R., SHEKELS L. L. and BERNLOHR D. A. (1992): Analysis of the ACP1 gene product: classification as an FMN phosphatase. Biochem. Biophys. Res. Commun., 189, 1598-1605.
29. GLORIA-BOTTINI F., GERLINI G., LUCARINI N., BORGIANI P., AMANTE A., LA TORRE M., ANTONACCI E. and BOTTINI E. (1996): Phosphotyrosine phosphatases and diabetic pregnancy: and association between low molecular weight acid phosphatase and degree of glycemic control. Experimentia, 52, 340-343.
30. GLORIA-BOTTINI F., LUCARINI N. and LA TORRE M. (1996): ...meanwhile, elsewhere in Italy. Nature, 379, 395.
31. GLORIA-BOTTINI F., LUCARINI N., PALMARINO R., LA TORRE M., AMANTE A. and BOTTINI E. (1997): ACP1 and human adaptability. 2. Association with season of conception. Hum. Genet., 101, 158-164.
32. GLORIA-BOTTINI F., NICOTRA M., LUCARINI N., BORGIANI P., LA TORRE M., AMANTE A., GIMELFARB A. and BOTTINI E. (1996): Phosphotyrosine-protein-phosphatases and human reproduction: an association between low molecular weight acid phosphatase (ACP1) and spontaneous abortion. Dis. Markers, 12, 261-269.
33. GRANGEASSE C., DOUBLET P., VINCENT C., VAGANAY E., RIBERTY M., DUCLOS B. and COZZONE A. J. (1998): Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii. J. Mol. Biol., 278, 339-347.
34. HARRISON M. L., RATHINAVELU P., ARESE P., GEAHLEN R. L. and Low P. S. (1991): Role of band 3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis. J. Biol. Chem., 266, 4106-4111.
35. HEINRIKSON R. L. (1969): Purification and characterization of a low molecular weight acid phosphatase from bovine liver. J. Biol. Chem., 244, 299-307.
36. HOPKINSON D. A., SPENCER N. and HARRIS H. (1963): Red cell acid phosphatase variants: a new human polymorphism. Nature, 199, 969-971.
37. HUANG L., SANKAR S., LIN C., KONTOS C. D., SCHROFF A. D., CHA E. H., FENG S. M., LI S. F., YU Z., VAN ETTEN R. L., BLANAR M. A. and PETERS K. G. (1999): HCPTPA, a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor-mediated signal transduction and biological activity. J. Biol. Chem., 274, 38183-38188.
38. LAZARUK K. D., DISSING J. and SENSABAUGH G. F. (1993): Exon structure at the human ACP1 locus supports alternative splicing model for f and s isozyme generation. Biochem. Biophys. Res. Commun., 196, 440-446.
39. LOW P. S., ALLEN D. P., ZIONCHECK T. F., CHARI, P., WILLARDSON B. M., GEAHLEN R. L. and HARRISON M. L. (1987): Tyrosine phosphorylation of band 3 inhibits peripheral protein binding. J. Biol. Chem., 262, 4592-4596.
40. LUCARINI N., ANTONACCI E., BOTTINI N., BORGIANI P., FAGGIONI G. and GLORIA-BOITINI F. (1998): Phosphotyrosine-protein-phosphatase and diabetic disorders. Further studies on the relationship between low molecular weight acid phosphatase genotype and degree of glycemic control. Dis. Markers, 14, 121-125.
41. LUCARINI N., ANTONACCI E., BOTTINI N. and GLORIA-BOTTINI F. (1997): Low-molecular-weight acid phosphatase (ACP1), obesity, and blood lipid levels in subjects with non-insulin-dependent diabetes mellitus. Hum. Biol., 69, 509-515.
42. LUCARINI N., BOTTINI N., ANTONACCI E., BORGIANI P., FAGGIONI G. and GLORIA-BOTTINI F. (1997). Diabetic complications and the genetics of signal transduction. A study of retinopathy in NIDDM. Dis. Markers, 13, 169-176.
43. LUCARINI N., FINOCCHI G., GLORIA-BOTTINI F., MACIOCE M., BORGIANI P., AMANTE A. and BOTTINI E. (1990): A possible genetic component of obesity in childhood. Observations on acid phosphatase polymorphism. Experientia, 46, 90-91.
44. MACCARI A. M., BOTTINI N., CANU G., CICHI A., BORZI M. and FONTANA L. (2001): LMPTP: a modifier gene in HCM? (submitted).
45. MARIAN A. J. (2000): Pathogenesis of diverse clinical and pathological phenotypes in hypertrophic cardiomyopathy. Lancet, 355, 58-60.
46. MARON B. J. (1997): Hypertrophic cardiomyopathy. Lancet, 350, 127-133.
47. MARRACCINI P., IANTOMASI T., RIGACCI S., PACINI S., RUGGIERO M., VINCENZINI M. T. and RAMPONI G. (1994): Effect of phosphotyrosine phosphatase over-expression on glutathione metabolism in normal and oncogene-transformed cells. FEBS Lett., 344, 157-160.
48. MILLER D. T., READ R., RUSCONI J. and CAGAN R. L. (2000): The Drosophila primo locus encodes two low-molecular-weight tyrosine phosphatases. Gene, 243, 1-9.
49. MODESTI A., MARZOCCHINI R., RAUGEI G., CHITI F., SERENI A., MAGHERINI F. and RAMPONI G. (1998): Cloning and characterization of a new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing. FEBS Lett., 431, 111-115.
50. MOHRENWEISER H. W. and NOVOTNY J. E. (1982): ACP1GUA-1 - a low-activity variant of human erythrocyte acid phosphatase: association with increased glutathione reductase activity. Am. J. Hum. Genet., 34, 425-433.
51. MONDESERT O., MORENO S. and RUSSELL P. (1994): Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man. J. Biol. Chem., 269, 27996-27999.
52. MUSTELIN T. (2001): Keeping the T cell immune response in balance; Role of protein tyrosine phosphatases in autoimmunity. In: ALTMAN A. (ed.) Current directions on autoimmunity. Karger Press Basel, 5, 176-190.
53. MUSTELIN T. and BOTTINI N. (2001): Protein tyrosine phosphatases in autoimmunity. Eur. J. Allerg. Clin. Immunol. (in press).
54. MUSTELIN T., FENG G.-S., BOTT NI N., ALONSO A., KHOLOD N., BIRLE D., MERLO J. and HUYNH H. (2001): Protein tyrosine phosphatases. Frontiers Biosci., 7, 85-142.
55. OH S. S., CHISHTI A. H., PALEK J. and LIU S. C. (1997): Erythrocyte membrane alterations in Plasmodium falciparum malaria sequestration. Curr. Opin. Hematol., 4, 148-154.
56. OSTANIN K., POKALSKY C., WANG S. and VAN ETTEN R. L. (1995): Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase. J. Biol. Chem., 270, 18491-18499.
57. PAGGI A., BORGIANI P., GLORIA-BOTTINI F., Russo S., SAPPONARA I., BANCI M., AMANTE A., LUCARINI N. and BOTTINI E. (1991): Further studies on acid phosphatase in obese subjects. Dis. Markers, 9, 1-7.
58. PALMARINO R., AGOSTINO R., GLORIA F., LUCARELLI P., BUSINCO L., ANTOGNONI G., MAGG ONI G., WORKMAN P. L. and BOTTINI E. (1975): Red cell acid phosphatase: another polymorphism correlated with Malaria? Am. J. Phys. Anthropol., 43, 177-186.
59. PEI J. J., GONG C. X., IQBAL K., GRUNDKE-IQBAL I., WU Q. L., WINBLAD B. and COWBURN R. F. (1998): Subcellular distribution of protein, phosphatases and abnormally phosphorylated tau in the temporal cortex from Alzheimer's disease and control brains. J. Neural. Transm., 105, 69-83.
60. RAMPONI G. (1994): The low Mr cytosolic phosphotyrosine protein phosphatase. Adv. Prot. Phosphatases, 8, 1-25.
61. RAMPONI G., MANAO G., CAMICI G., CAPPUGI G., RUGGIERO M. and BOTTARO D. P. (1989): The 18 kDa cytosolic acid phosphatase from bovine liver has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor. FEBS Lett., 250, 469-473.
62. RAMPONI G., RUGGIERO M., RAUGEI G., BERTI A., MODESTI A., DEGL'INNOCENTI D., MAGNELLI L., PAZZAGLI C., CHIARUGI V. P. and CAMICI G. (1992): Overexpression of a synthetic phosphotyrosine protein phosphatase gene inhibits normal and transformed cell growth. Int. J. Cancer, 51, 652-656.
63. v-src phosphorylates and activates low molecular weight phosphotyrosine-piotein phosphatase. J. Biol. Chem., 271, 1278-1281.
64. RUDBECK L., DISSING J., LAZARUK K. D. and SENSABAUGH G. (2000): Human 18 kDa phosphotyrosine protein phosphatase (ACP1) polymorphism: studies of rare variants provide evidence that substitutions within or near alternatively spliced exons affect splicing result. Ann. Hum. Genet., 64, 107-116.
65. RUGGIERO M., PAZZAGLI C., RIGACCI S., MAGNELLI L., RAUGIE G., BERTI A., CHIARUGI V. P., PIERCE J. H., CAMICI G. and RAMPONI G. (1993): Negative growth control by a novel low Mr phosphotyrosine protein phosphatase in normal and transformed cells. FEBS Lett., 326, 294-298.
66. SENSABAUGH G. F. and LAZARUK K. A. (1993): A TaqI site identifies the *A allele at the ACP1 locus. Hum. Mol. Genet., 2, 1079.
67. SHEKELS L. L., SMITH A. J., VAN ETTEN R. L. and BERNLOHR D. A. (1992): Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase. Prot. Sci., 1, 710-721.
68. SHIMOHAMA S., FUJIMOTO S., CHACHIN M., TANIGUCHI T., PERRY G., WHITEHOUSE P. J. and KIMURA J. (1995): Alterations of low molecular weight acid phosphatase protein level in Alzheimer's disease. Brain Res., 699, 125-129.
69. SHIMOHAMA S., FUJIMOTO S., TANIGUCHI T., KAMEYAMA M. and KIMURA J. (1993): Reduction of low-molecular-weight acid phosphatase activity in Alzheimer brains. Ann. Neurol., 33, 616-621.
70. SHIMOHAMA S., FUJIMOTO S., TANIGUCHI T. and KIMURA J. (1994): The endogenous substrate of low molecular weight acid phosphatase in the brain is an epidermal growth factor receptor. Brain Res., 662, 185-188.
71. STEFANI M., CASELLI A., BUCCIANTINI M., PAZZAGLI L., DOLFI F., CAMICI G., MANAO G. and RAMPONI G. (1993): Dephosphorylation of tyrosine phosphorylated synthetic peptides by rat liver phosphotyrosine protein phosphatase isoenzymes. FEBS Lett., 326, 131-134.
72. STEIN E., LANE A. A., CERRETTI D. P., SCHOECKLMANN H. O., SCHROFF A. D., VAN ETFEN R. L. and DANIEL T. O. (1998): Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev., 12, 667-678.
73. SU X.-D., TADDEI N., MASSIMO S., RAMPONI G. and NORDLUND P. (1994): The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature, 370, 575-578.
74. TAILOR P., GILMAN J., WILLIAMS S. and MUSTELIN T. (1999): A novel isoform of the low molecular weight protein tyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing. Eur. J. Biochem., 262, 277-282.
75. TAILOR P., WILLIAMS S., GILMAN J., COUTURE C. and MUSTELIN T. (1997): Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132. J. Biol. Chem., 272, 5371-5376.
76. TANINO H., YOSHIDA J., YAMAMOTO R., KOBAYASHI Y., SHIMOHAMA S. and FUJIMOTO S. (1999): Abundance of low molecular weight phosphotyrosine protein phosphatase in the nerve-ending fraction in the brain. Biol. Pharm. Bull., 22, 794-798.
77. WO Y.-Y. P., MCCORMACK A. L., SHABANOWITZ J., HUNT D. F., DAVIS J. P., MITCHELL G. L. and VAN ETTEN R. L. (1992): Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. J. Biol. Chem., 267, 10856-10865.
78. ZHANG M., STAUFFACHER C. V., LIN D. and VAN ETTEN R. L. (1998): Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. J. Biol. Chem., 273, 21714-21720.
79. ZHANG M., STAUFFACHER C. V. and VAN ETTEN R. L. (1995): The three dimensional structure, chemical mechanism and function of the low molecular weight protein tyrosine phosphatases. Adv. Prot. Phosphatases, 9, 1-23.
80. ZHANG Z.-Y. and VAN EITEN R. L. (1990): Purification and characterization of a low-molecular-weight acid phosphatase -a phosphotyrosyl-protein phosphatase from bovine heart. Arch. Biochem. Biophys., 282, 39-49.