메뉴 건너뛰기




Volumn 216, Issue 1, 2014, Pages 1-8

The lipid raft-bound alkaline phosphatase activity increases and the level of transcripts remains unaffected in liver of merosin-deficient LAMA2dy mouse

Author keywords

Glycosylation; Heat deactivation; Hypophosphatasia; Muscular dystrophy; Oligomerization

Indexed keywords

ALKALINE PHOSPHATASE; FLOTILLIN 2; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOSYLTRANSFERASE; MEROSIN; MESSENGER RNA; TRANSFERRIN RECEPTOR;

EID: 84902976710     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2014.03.008     Document Type: Article
Times cited : (3)

References (46)
  • 1
    • 0025139287 scopus 로고
    • Purified tetrameric alkaline phosphatase: The effect of treatments with phosphatidylinositol phospholipase C and sodium dodecyl sulfate
    • DOI 10.1016/0009-8981(90)90037-S
    • K. Hawrylak, L. Kihn, D. Rutkowski, and R.A. Stinson Purified tetrameric alkaline phosphatase: the effect of treatments with phosphatidylinositol phospholipase C and sodium dodecyl sulfate Clin. Chim. Acta 186 1990 197 201 (Pubitemid 20037753)
    • (1990) Clinica Chimica Acta , vol.186 , Issue.2 , pp. 197-201
    • Hawrylak, K.1    Kihn, L.2    Rutkowski, D.3    Stinson, R.A.4
  • 2
    • 84882799443 scopus 로고    scopus 로고
    • A novel hypothesis for an alkaline phosphatase 'rescue' mechanism in the hepatic acute phase immune response
    • A.F. Pike, N.I. Kramer, B.J. Blaauboer, W. Seinen, and R. Brands A novel hypothesis for an alkaline phosphatase 'rescue' mechanism in the hepatic acute phase immune response Biochim. Biophys. Acta 1832 2013 2044 2056
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 2044-2056
    • Pike, A.F.1    Kramer, N.I.2    Blaauboer, B.J.3    Seinen, W.4    Brands, R.5
  • 3
    • 84861529229 scopus 로고    scopus 로고
    • Cellular function and molecular structure of ecto-nucleotidases
    • H. Zimmermann, M. Zebisch, and N. Strater Cellular function and molecular structure of ecto-nucleotidases Purinergic Signalling 8 2012 437 502
    • (2012) Purinergic Signalling , vol.8 , pp. 437-502
    • Zimmermann, H.1    Zebisch, M.2    Strater, N.3
  • 4
    • 33747475602 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment
    • DOI 10.1021/bi052471+
    • M.F. Hoylaerts, L. Ding, S. Narisawa, K.S. Van, and J.L. Millan Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment Biochemistry 45 2006 9756 9766 (Pubitemid 44257423)
    • (2006) Biochemistry , vol.45 , Issue.32 , pp. 9756-9766
    • Hoylaerts, M.F.1    Ding, L.2    Narisawa, S.3    Van Kerckhoven, S.4    Millan, J.L.5
  • 5
    • 34250160114 scopus 로고    scopus 로고
    • Alkaline phosphatases: Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
    • J.L. Millán Alkaline phosphatases: structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes Purinergic Signalling 2 2006 335 341
    • (2006) Purinergic Signalling , vol.2 , pp. 335-341
    • Millán, J.L.1
  • 6
    • 46749091223 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase (CD73) -mediated extracellular adenosine production plays a critical role in hepatic fibrosis
    • DOI 10.1096/fj.07-100685
    • Z. Peng, P. Fernandez, T. Wilder, H. Yee, L. Chiriboga, E.S.L. Chan, and B.N. Cronstein Ecto-5′-nucleotidase (CD73)-mediated extracellular adenosine production plays a critical role in hepatic fibrosis FASEB J. 22 2008 2263 2272 (Pubitemid 351948645)
    • (2008) FASEB Journal , vol.22 , Issue.7 , pp. 2263-2272
    • Peng, Z.1    Fernandez, P.2    Wilder, T.3    Yee, H.4    Chiriboga, L.5    Chan, E.S.L.6    Cronstein, B.N.7
  • 8
    • 84874213726 scopus 로고    scopus 로고
    • Dynamic evolution of the LPS-detoxifying enzyme intestinal alkaline phosphatase in zebrafish and other vertebrates
    • Y. Yang, A.M. Wandler, J.H. Postlethwait, and K. Guillemin Dynamic evolution of the LPS-detoxifying enzyme intestinal alkaline phosphatase in zebrafish and other vertebrates Front. Immunol. 3 2012 314
    • (2012) Front. Immunol. , vol.3 , pp. 314
    • Yang, Y.1    Wandler, A.M.2    Postlethwait, J.H.3    Guillemin, K.4
  • 9
    • 84881087204 scopus 로고    scopus 로고
    • Multisystemic functions of alkaline phosphatases
    • R. Buchet, J.L. Millan, and D. Magne Multisystemic functions of alkaline phosphatases Methods Mol. Biol. 1053 2013 27 51
    • (2013) Methods Mol. Biol. , vol.1053 , pp. 27-51
    • Buchet, R.1    Millan, J.L.2    Magne, D.3
  • 10
    • 77950665927 scopus 로고    scopus 로고
    • Physiological role of alkaline phosphatase explored in hypophosphatasia
    • M.P. Whyte Physiological role of alkaline phosphatase explored in hypophosphatasia Ann. N. Y. Acad. Sci. 1192 2010 190 200
    • (2010) Ann. N. Y. Acad. Sci. , vol.1192 , pp. 190-200
    • Whyte, M.P.1
  • 11
    • 84856485352 scopus 로고    scopus 로고
    • Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia
    • Y. Satou, H.A. Al-Shawafi, S. Sultana, S. Makita, M. Sohda, and K. Oda Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia Biochim. Biophys. Acta 1822 2012 581 588
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 581-588
    • Satou, Y.1    Al-Shawafi, H.A.2    Sultana, S.3    Makita, S.4    Sohda, M.5    Oda, K.6
  • 12
    • 76249113874 scopus 로고    scopus 로고
    • The mechanism of mineralization and the role of alkaline phosphatase in health and disease
    • H. Orimo The mechanism of mineralization and the role of alkaline phosphatase in health and disease J. Nippon Med. Sch. 77 2010 4 12
    • (2010) J. Nippon Med. Sch. , vol.77 , pp. 4-12
    • Orimo, H.1
  • 14
    • 77954956652 scopus 로고    scopus 로고
    • The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency
    • M.T. Moral-Naranjo, M.F. Montenegro, E. Muñoz-Delgado, F.J. Campoy, and C.J. Vidal The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency Biochim. Biophys. Acta 1802 2010 754 764
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 754-764
    • Moral-Naranjo, M.T.1    Montenegro, M.F.2    Muñoz-Delgado, E.3    Campoy, F.J.4    Vidal, C.J.5
  • 15
    • 79851479445 scopus 로고    scopus 로고
    • Reggie/flotillin and the targeted delivery of cargo
    • C.A. Stuermer Reggie/flotillin and the targeted delivery of cargo J. Neurochem. 116 2011 708 713
    • (2011) J. Neurochem. , vol.116 , pp. 708-713
    • Stuermer, C.A.1
  • 16
    • 46849102138 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol anchor: A complex membrane-anchoring structure for proteins
    • DOI 10.1021/bi8006324
    • M.G. Paulick, and C.R. Bertozzi The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins Biochemistry 47 2008 6991 7000 (Pubitemid 351956348)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 6991-7000
    • Paulick, M.G.1    Bertozzi, C.R.2
  • 17
    • 82655189982 scopus 로고    scopus 로고
    • N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells
    • N.S. Imjeti, S. Lebreton, S. Paladino, E. de la Fuente, A. Gonzalez, and C. Zurzolo N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells Mol. Biol. Cell 22 2011 4621 4634
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4621-4634
    • Imjeti, N.S.1    Lebreton, S.2    Paladino, S.3    De La Fuente, E.4    Gonzalez, A.5    Zurzolo, C.6
  • 19
    • 36849014328 scopus 로고    scopus 로고
    • Acute liver failure following therapeutic paracetamol administration in patients with muscular dystrophies
    • DOI 10.1111/j.1365-2044.2007.05340.x
    • B. Pearce, and I.S. Grant Acute liver failure following therapeutic paracetamol administration in patients with muscular dystrophy Anaesthesia 63 2008 89 91 (Pubitemid 350233217)
    • (2008) Anaesthesia , vol.63 , Issue.1 , pp. 89-91
    • Pearce, B.1    Grant, I.S.2
  • 21
    • 33645851346 scopus 로고    scopus 로고
    • The increased ecto-5′-nucleotidase activity in muscle, heart and liver of laminin α2-deficient mice is not caused by an elevation in the mRNA content
    • J.C. Morote-García, L.F. Sánchez del Campo, F.J. Campoy, C.J. Vidal, and E. Muñoz-Delgado The increased ecto-5′-nucleotidase activity in muscle, heart and liver of laminin α2-deficient mice is not caused by an elevation in the mRNA content Int. J. Biochem. Cell Biol. 38 2006 1092 1101
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1092-1101
    • Morote-García, J.C.1    Sánchez Del Campo, L.F.2    Campoy, F.J.3    Vidal, C.J.4    Muñoz-Delgado, E.5
  • 22
    • 28244492010 scopus 로고    scopus 로고
    • Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice
    • DOI 10.1111/j.1471-4159.2005.03433.x
    • S. Nieto-Cerón, L.F. Sánchez del Campo, E. Muñoz-Delgado, C.J. Vidal, and F.J. Campoy Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice J. Neurochem. 95 2005 1035 1046 (Pubitemid 41713488)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.4 , pp. 1035-1046
    • Nieto-Ceron, S.1    Del Campo, L.F.S.2    Munoz-Delgado, E.3    Vidal, C.J.4    Campoy, F.J.5
  • 23
    • 13644267779 scopus 로고    scopus 로고
    • Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells
    • DOI 10.1007/s00223-004-0023-2
    • J.R. Farley, and P. Magnusson Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells Calcif. Tissue Int. 76 2005 63 74 (Pubitemid 40228476)
    • (2005) Calcified Tissue International , vol.76 , Issue.1 , pp. 63-74
    • Farley, J.R.1    Magnusson, P.2
  • 24
    • 70349432183 scopus 로고    scopus 로고
    • Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms
    • L.C. Halling, S. Narisawa, J.L. Millan, and P. Magnusson Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms Bone 45 2009 987 993
    • (2009) Bone , vol.45 , pp. 987-993
    • Halling, L.C.1    Narisawa, S.2    Millan, J.L.3    Magnusson, P.4
  • 25
    • 0018980970 scopus 로고
    • Sugar-lectin interactions: How does wheat-germ agglutinin bind sialoglycoconjugates?
    • M. Monsigny, A.C. Roche, C. Sene, R. Maget-Dana, and F. Delmotte Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? Eur. J. Biochem. 104 1980 147 153
    • (1980) Eur. J. Biochem. , vol.104 , pp. 147-153
    • Monsigny, M.1    Roche, A.C.2    Sene, C.3    Maget-Dana, R.4    Delmotte, F.5
  • 26
    • 0034962796 scopus 로고    scopus 로고
    • Expression of binding properties of Gal/GalNAc reactive lectins by mammalian glycotopes
    • A.M. Wu Expression of binding properties of Gal/GalNAc reactive lectins by mammalian glycotopes (an updated report) Adv. Exp. Med. Biol. 491 2001 55 64 (Pubitemid 32595116)
    • (2001) Advances in Experimental Medicine and Biology , vol.491 , pp. 55-64
    • Wu, A.M.1
  • 28
    • 33644503593 scopus 로고    scopus 로고
    • Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes
    • A. Mazzone, P. Tietz, J. Jefferson, R. Pagano, and N.F. LaRusso Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes Hepatology 43 2006 287 296
    • (2006) Hepatology , vol.43 , pp. 287-296
    • Mazzone, A.1    Tietz, P.2    Jefferson, J.3    Pagano, R.4    Larusso, N.F.5
  • 29
    • 34250333029 scopus 로고    scopus 로고
    • Cell polarity development and protein trafficking in hepatocytes lacking E-cadherin/β-catenin-based adherens junctions
    • DOI 10.1091/mbc.E06-11-1040
    • D. Théard, M. Steiner, D. Kalicharan, D. Hoekstra, and S.C.D. van Ijzendoorn Cell polarity development and protein trafficking in hepatocytes lacking E-cadherin/beta-catenin-based adherens junctions Mol. Biol. Cell 18 2007 2313 2321 (Pubitemid 46911381)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.6 , pp. 2313-2321
    • Theard, D.1    Steiner, M.2    Kalicharan, D.3    Hoekstra, D.4    Van Ijzendoorn, S.C.D.5
  • 30
    • 43949101050 scopus 로고    scopus 로고
    • Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking
    • DOI 10.1002/hep.22014
    • R.A. Joseph, B.D. Shepard, G.T. Kannarkat, T. Rutledge, D.J. Tuma, and P.L. Tuma Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking Hepatology 47 2008 1745 1753 (Pubitemid 351702756)
    • (2008) Hepatology , vol.47 , Issue.5 , pp. 1745-1753
    • Joseph, R.A.1    Shepard, B.D.2    Kannarkat, G.T.3    Rutledge, T.M.4    Tuma, D.J.5    Tuma, P.L.6
  • 31
    • 84862176451 scopus 로고    scopus 로고
    • Muscle membrane repair and inflammatory attack in dysferlinopathy
    • R. Han Muscle membrane repair and inflammatory attack in dysferlinopathy Skelet. Muscle 1 2011 10
    • (2011) Skelet. Muscle , vol.1 , pp. 10
    • Han, R.1
  • 32
    • 0037931325 scopus 로고    scopus 로고
    • Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution
    • DOI 10.1074/jbc.M301105200
    • R.R. Boulanger Jr., and E.R. Kantrowitz Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution J. Biol. Chem. 278 2003 23497 23501 (Pubitemid 36830167)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23497-23501
    • Boulanger Jr., R.R.1    Kantrowitz, E.R.2
  • 34
    • 43549100025 scopus 로고    scopus 로고
    • Molecular basis of perinatal hypophosphatasia with tissue-nonspecific alkaline phosphatase bearing a conservative replacement of valine by alanine at position 406: Structural importance of the crown domain
    • DOI 10.1111/j.1742-4658.2008.06414.x
    • N. Numa, Y. Ishida, M. Nasu, M. Sohda, Y. Misumi, T. Noda, and K. Oda Molecular basis of perinatal hypophosphatasia with tissue-nonspecific alkaline phosphatase bearing a conservative replacement of valine by alanine at position 406. Structural importance of the crown domain FEBS J. 275 2008 2727 2737 (Pubitemid 351678661)
    • (2008) FEBS Journal , vol.275 , Issue.11 , pp. 2727-2737
    • Numa, N.1    Ishida, Y.2    Nasu, M.3    Sohda, M.4    Misumi, Y.5    Noda, T.6    Oda, K.7
  • 35
    • 0032738447 scopus 로고    scopus 로고
    • Role of metal ions on the secondary and quaternary structure of alkaline phosphatase from bovine intestinal mucosa
    • DOI 10.1002/(SICI)1097-0134(19991101)37:2<310::AID-PROT16>3.0.CO;2- B
    • M. Bortolato, F. Besson, and B. Roux Role of metal ions on the secondary and quaternary structure of alkaline phosphatase from bovine intestinal mucosa Proteins 37 1999 310 318 (Pubitemid 29503012)
    • (1999) Proteins: Structure, Function and Genetics , vol.37 , Issue.2 , pp. 310-318
    • Bortolato, M.1    Besson, F.2    Roux, B.3
  • 36
    • 0031036060 scopus 로고    scopus 로고
    • Human tissue non-specific alkaline phosphatases: Sugar-moiety-induced enzymic and antigenic modulations and genetic aspects
    • O. Nosjean, I. Koyama, M. Goseki, B. Roux, and T. Komoda Human tissue non-specific alkaline phosphatases: sugar-moiety-induced enzymic and antigenic modulations and genetic aspects Biochem. J. 321 1997 297 303 (Pubitemid 27056472)
    • (1997) Biochemical Journal , vol.321 , Issue.2 , pp. 297-303
    • Nosjean, O.1    Koyama, I.2    Goseki, M.3    Roux, B.4    Komoda, T.5
  • 37
    • 0030833450 scopus 로고    scopus 로고
    • Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2(dy) mouse muscle
    • J. Cabezas-Herrera, M.T. Moral-Naranjo, F.J. Campoy, and C.J. Vidal Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle J. Neurochem. 69 1997 1964 1974 (Pubitemid 27452743)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.5 , pp. 1964-1974
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 38
    • 0037131559 scopus 로고    scopus 로고
    • Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice
    • M.T. Moral-Naranjo, J. Cabezas-Herrera, C.J. Vidal, and F.J. Campoy Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice Neurosci. Lett. 331 2002 155 158
    • (2002) Neurosci. Lett. , vol.331 , pp. 155-158
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3    Campoy, F.J.4
  • 41
    • 84873734964 scopus 로고    scopus 로고
    • Dynamics fingerprint and inherent asymmetric flexibility of a cold-adapted homodimeric enzyme. A case study of the Vibrio alkaline phosphatase
    • E. Papaleo, G. Renzetti, G. Invernizzi, and B. Asgeirsson Dynamics fingerprint and inherent asymmetric flexibility of a cold-adapted homodimeric enzyme. A case study of the Vibrio alkaline phosphatase Biochim. Biophys. Acta 1830 2013 2970 2980
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 2970-2980
    • Papaleo, E.1    Renzetti, G.2    Invernizzi, G.3    Asgeirsson, B.4
  • 42
    • 0015413741 scopus 로고
    • Alkaline phosphatase in normal and diseased human muscle
    • N.C. Kar, and C.M. Pearson Alkaline phosphatase in normal and diseased human muscle Proc. Soc. Exp. Biol. Med. 141 1972 4 6
    • (1972) Proc. Soc. Exp. Biol. Med. , vol.141 , pp. 4-6
    • Kar, N.C.1    Pearson, C.M.2
  • 43
    • 70449514551 scopus 로고    scopus 로고
    • Inhibition of extracellular matrix assembly induces the expression of osteogenic markers in skeletal muscle cells by a BMP-2 independent mechanism
    • N. Osses, J.C. Casar, and E. Brandan Inhibition of extracellular matrix assembly induces the expression of osteogenic markers in skeletal muscle cells by a BMP-2 independent mechanism BMC Cell Biol. 10 2009 73
    • (2009) BMC Cell Biol. , vol.10 , pp. 73
    • Osses, N.1    Casar, J.C.2    Brandan, E.3
  • 44
    • 0033769980 scopus 로고    scopus 로고
    • Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver of Lama2dy mice
    • J.L. Gómez, M.S. García-Ayllón, F.J. Campoy, and C.J. Vidal Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver of Lama2dy mice J. Neurosci. Res. 62 2000 134 145
    • (2000) J. Neurosci. Res. , vol.62 , pp. 134-145
    • Gómez, J.L.1    García-Ayllón, M.S.2    Campoy, F.J.3    Vidal, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.