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Volumn 27, Issue 1, 2006, Pages 83-92

Immunohistochemical analysis of human skeletal muscle AMP deaminase deficiency. Evidence of a correlation between the muscle HPRG content and the level of the residual AMP deaminase activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE MONOPHOSPHATE DEAMINASE; ISOPROTEIN; POLYPEPTIDE;

EID: 33746089545     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-006-9059-4     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 31744452211 scopus 로고    scopus 로고
    • Basic reactions of muscle
    • Engel AG and Franzini-Armstrong C (eds). Mc Graw-Hill, New York
    • Banker BQ and Engel AG (2004) Basic reactions of muscle. In: Engel AG and Franzini-Armstrong C (eds) Myology: Basic and Clinical 3rd edn. (pp. 691-747). Mc Graw-Hill, New York.
    • (2004) Myology: Basic and Clinical 3rd Edn. , pp. 691-747
    • Banker, B.Q.1    Engel, A.G.2
  • 3
    • 0031906409 scopus 로고    scopus 로고
    • Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria
    • Bruno C, Minetti C., Shanske S, Morreale G, Bado M, Cordone G and DiMauro S (1998) Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria. Neurology 50: 296-298.
    • (1998) Neurology , vol.50 , pp. 296-298
    • Bruno, C.1    Minetti, C.2    Shanske, S.3    Morreale, G.4    Bado, M.5    Cordone, G.6    DiMauro, S.7
  • 4
    • 0015738302 scopus 로고
    • Stabilization of adenylate energy charge by the adenylate deaminase reaction
    • Chapman AG and Atkinson DE (1973) Stabilization of adenylate energy charge by the adenylate deaminase reaction. J Biol Chem 248: 8309-8312.
    • (1973) J Biol Chem , vol.248 , pp. 8309-8312
    • Chapman, A.G.1    Atkinson, D.E.2
  • 6
    • 0018200117 scopus 로고
    • Myoadenylate deaminase deficiency: A new disease of muscle
    • Fishbein WN, Armbrustmacher VW and Griffin JL (1978) Myoadenylate deaminase deficiency: a new disease of muscle. Science 200: 545-548.
    • (1978) Science , vol.200 , pp. 545-548
    • Fishbein, W.N.1    Armbrustmacher, V.W.2    Griffin, J.L.3
  • 8
    • 0021948917 scopus 로고
    • Myoadenylate deaminase deficiency: Inherited and acquired forms
    • Fishbein WN (1985) Myoadenylate deaminase deficiency: inherited and acquired forms. Biochem Med 33: 158-169.
    • (1985) Biochem Med , vol.33 , pp. 158-169
    • Fishbein, W.N.1
  • 9
    • 0027462632 scopus 로고
    • Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle
    • Fishbein WN, Sabina RL, Ogasawara N and Holmes EW (1993) Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle. Biochim Biophys Acta 1163: 97-104.
    • (1993) Biochim Biophys Acta , vol.1163 , pp. 97-104
    • Fishbein, W.N.1    Sabina, R.L.2    Ogasawara, N.3    Holmes, E.W.4
  • 10
    • 0030178727 scopus 로고    scopus 로고
    • Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle
    • Fortuin FD, Morisaki T and Holmes EW (1996) Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. Proc Assoc Am Physicians 108: 329-333.
    • (1996) Proc Assoc Am Physicians , vol.108 , pp. 329-333
    • Fortuin, F.D.1    Morisaki, T.2    Holmes, E.W.3
  • 11
    • 0020062835 scopus 로고
    • Myoadenylate deaminase deficiency or not? Observations on two brothers with exercise-induced muscle pain
    • Hayes DJ, Summers BA and Morgan-Hughes JA (1982) Myoadenylate deaminase deficiency or not? Observations on two brothers with exercise-induced muscle pain. J Neurol Sci 53: 125-136.
    • (1982) J Neurol Sci , vol.53 , pp. 125-136
    • Hayes, D.J.1    Summers, B.A.2    Morgan-Hughes, J.A.3
  • 12
    • 0021154683 scopus 로고
    • Circulatory clearance, internalization and degradation of muscle AMP aminohydrolase
    • Husic DH and Suelter CH (1984) Circulatory clearance, internalization and degradation of muscle AMP aminohydrolase. J Biol Chem 259: 4359-4364.
    • (1984) J Biol Chem , vol.259 , pp. 4359-4364
    • Husic, D.H.1    Suelter, C.H.2
  • 13
    • 16344375246 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein: A novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems
    • Jones AL, Hulett MD and Parish CR (2005) Histidine-rich glycoprotein: a novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems. Immunol Cell Biol 83: 106-118.
    • (2005) Immunol Cell Biol , vol.83 , pp. 106-118
    • Jones, A.L.1    Hulett, M.D.2    Parish, C.R.3
  • 14
    • 0023664499 scopus 로고
    • Histidine-rich glycoprotein is evolutionarily related to the cystatin superfamily
    • Koide T and Odani S (1987) Histidine-rich glycoprotein is evolutionarily related to the cystatin superfamily. FEBS Lett 216: 17-21.
    • (1987) FEBS Lett , vol.216 , pp. 17-21
    • Koide, T.1    Odani, S.2
  • 15
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb AL, Torres AS, O'Halloran TV and Rosenzweig AC (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Bio 8: 751-755.
    • (2001) Nat Struct Bio , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 17
    • 0020553949 scopus 로고
    • Heparin binding properties of human histidine-rich glycoprotein
    • Lijnen HR, Hoylaerts M and Collen D (1983) Heparin binding properties of human histidine-rich glycoprotein. J Biol Chem 258: 3803-3808.
    • (1983) J Biol Chem , vol.258 , pp. 3803-3808
    • Lijnen, H.R.1    Hoylaerts, M.2    Collen, D.3
  • 18
    • 0015317149 scopus 로고
    • Ammonia production in muscle and other tissues: The purine nucleotide cycle
    • Lowenstein JM (1972) Ammonia production in muscle and other tissues: the purine nucleotide cycle. Physiol Rev 52: 382-414.
    • (1972) Physiol Rev , vol.52 , pp. 382-414
    • Lowenstein, J.M.1
  • 19
    • 0015243919 scopus 로고
    • Ammonia production in muscle: The purine nucleotide cycle
    • Lowenstein JM and Tornheim K (1971) Ammonia production in muscle: the purine nucleotide cycle. Science 171: 397-400.
    • (1971) Science , vol.171 , pp. 397-400
    • Lowenstein, J.M.1    Tornheim, K.2
  • 21
    • 0026726662 scopus 로고
    • Cloning of human AMP deaminase isoform E cDNAs
    • Mahnke-Zizelman DK and Sabina RL (1992) Cloning of human AMP deaminase isoform E cDNAs. J Biol Chem 267: 20866-20877.
    • (1992) J Biol Chem , vol.267 , pp. 20866-20877
    • Mahnke-Zizelman, D.K.1    Sabina, R.L.2
  • 22
    • 0032567534 scopus 로고    scopus 로고
    • Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
    • Mahnke-Zizelman DK, Tullson PC and Sabina RL (1998) Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms. J Biol Chem 273: 35118-35125.
    • (1998) J Biol Chem , vol.273 , pp. 35118-35125
    • Mahnke-Zizelman, D.K.1    Tullson, P.C.2    Sabina, R.L.3
  • 23
    • 0037474241 scopus 로고    scopus 로고
    • Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase
    • Mangani S, Meyer-Klaucke W, Moir AJG, Ranieri-Raggi M, Martini D and Raggi A (2003) Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase. J Biol Chem 278: 3176-3184.
    • (2003) J Biol Chem , vol.278 , pp. 3176-3184
    • Mangani, S.1    Meyer-Klaucke, W.2    Moir, A.J.G.3    Ranieri-Raggi, M.4    Martini, D.5    Raggi, A.6
  • 24
    • 5444246328 scopus 로고    scopus 로고
    • A calpain-like proteolytic activity produces the limited cleavage at the N-terminal regulatory domain of rabbit skeletal muscle AMP deaminase: Evidence of a protective molecular mechanism
    • Martini D, Montali U, Ranieri-Raggi M, Sabbatini ARM, Thorpe SJ, Moir AJG and Raggi A (2004) A calpain-like proteolytic activity produces the limited cleavage at the N-terminal regulatory domain of rabbit skeletal muscle AMP deaminase: evidence of a protective molecular mechanism. Biochim Biophys Acta 1702: 191-198.
    • (2004) Biochim Biophys Acta , vol.1702 , pp. 191-198
    • Martini, D.1    Montali, U.2    Ranieri-Raggi, M.3    Sabbatini, A.R.M.4    Thorpe, S.J.5    Moir, A.J.G.6    Raggi, A.7
  • 25
    • 0023147728 scopus 로고
    • A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid
    • McKinney MM and Parkinson A (1987) A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid. J Immunol Methods 96: 271-278.
    • (1987) J Immunol Methods , vol.96 , pp. 271-278
    • McKinney, M.M.1    Parkinson, A.2
  • 26
    • 0025310830 scopus 로고
    • Adenylate deaminase: A multigene family in humans and rats
    • Morisaki T, Sabina RL and Holmes EW (1990) Adenylate deaminase: A multigene family in humans and rats. J Biol Chem 265: 11482-11486.
    • (1990) J Biol Chem , vol.265 , pp. 11482-11486
    • Morisaki, T.1    Sabina, R.L.2    Holmes, E.W.3
  • 28
    • 0014692598 scopus 로고
    • Muscle AMP aminohydrolase. II. Distribution of AMP aminohydrolase, myokinase and creatine kinase activities in skeletal muscle
    • Raggi A, Ronca-Testoni S and Ronca G (1969) Muscle AMP aminohydrolase. II. Distribution of AMP aminohydrolase, myokinase and creatine kinase activities in skeletal muscle. Biochim Biophys Acta 178: 619-622.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 619-622
    • Raggi, A.1    Ronca-Testoni, S.2    Ronca, G.3
  • 29
    • 0016750205 scopus 로고
    • Isozymes of AMP deaminase in red and white skeletal muscles
    • Raggi A, Bergamini C and Ronca G (1975) Isozymes of AMP deaminase in red and white skeletal muscles. FEBS Lett 58: 19-23.
    • (1975) FEBS Lett , vol.58 , pp. 19-23
    • Raggi, A.1    Bergamini, C.2    Ronca, G.3
  • 30
    • 0030770482 scopus 로고    scopus 로고
    • Association of purified skeletal-muscle AMP deaminase with a histidine-proline-rich-glycoprotein-like molecole
    • Ranieri-Raggi M, Montali U, Ronca F, Sabbatini ARM, Brown PE, Moir AG and Raggi A (1997) Association of purified skeletal-muscle AMP deaminase with a histidine-proline-rich-glycoprotein-like molecole. Biochem J 326: 641-648.
    • (1997) Biochem J , vol.326 , pp. 641-648
    • Ranieri-Raggi, M.1    Montali, U.2    Ronca, F.3    Sabbatini, A.R.M.4    Brown, P.E.5    Moir, A.G.6    Raggi, A.7
  • 31
    • 0037474256 scopus 로고    scopus 로고
    • Isolation by zinc-affinity chromatography of the histidine-proline-rich glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme
    • Ranieri-Raggi M, Martini D, Sabbatini ARM, Moir AJG and Raggi A (2003) Isolation by zinc-affinity chromatography of the histidine-proline-rich glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme. Biochim Biophys Acta 1645: 81-88.
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 81-88
    • Ranieri-Raggi, M.1    Martini, D.2    Sabbatini, A.R.M.3    Moir, A.J.G.4    Raggi, A.5
  • 32
    • 0027076339 scopus 로고
    • Adaptation of rat skeletal muscle to creatine depletion: AMP deaminase and AMP deamination
    • Ren J and Holloszy O (1992) Adaptation of rat skeletal muscle to creatine depletion: AMP deaminase and AMP deamination. J Appl Physiol 73: 2713-2716.
    • (1992) J Appl Physiol , vol.73 , pp. 2713-2716
    • Ren, J.1    Holloszy, O.2
  • 33
    • 0027940313 scopus 로고
    • Evidence of a species-differentiated regulatory domain within the N-terminal region of skeletal muscle AMP deaminase
    • Ronca F, Ranieri-Raggi M, Brown PE, Moir AJG and Raggi A (1994) Evidence of a species-differentiated regulatory domain within the N-terminal region of skeletal muscle AMP deaminase. Biochim Biophys Acta 1209: 123-129.
    • (1994) Biochim Biophys Acta , vol.1209 , pp. 123-129
    • Ronca, F.1    Ranieri-Raggi, M.2    Brown, P.E.3    Moir, A.J.G.4    Raggi, A.5
  • 34
    • 0032896424 scopus 로고    scopus 로고
    • Presence in human skeletal muscle of an AMP deaminase-associated protein that reacts with an antibody to human plasma histidine-proline-rich glycoprotein
    • Sabbatini ARM, Ranieri-Raggi M, Pollina L, Viacava P, Ashby JR, Moir AJG and Raggi A (1999) Presence in human skeletal muscle of an AMP deaminase-associated protein that reacts with an antibody to human plasma histidine-proline-rich glycoprotein. J Histochem Cytochem 47: 255-260.
    • (1999) J Histochem Cytochem , vol.47 , pp. 255-260
    • Sabbatini, A.R.M.1    Ranieri-Raggi, M.2    Pollina, L.3    Viacava, P.4    Ashby, J.R.5    Moir, A.J.G.6    Raggi, A.7
  • 37
    • 0035875157 scopus 로고    scopus 로고
    • Myoadenylate deaminase deficiency does not affect muscle anaplerosis during exhaustive exercise in humans
    • Tarnopolsky MA, Parise G, Gibala MJ, Graham TE and Rush JW (2001) Myoadenylate deaminase deficiency does not affect muscle anaplerosis during exhaustive exercise in humans. J Physiol 533: 881-889.
    • (2001) J Physiol , vol.533 , pp. 881-889
    • Tarnopolsky, M.A.1    Parise, G.2    Gibala, M.J.3    Graham, T.E.4    Rush, J.W.5
  • 38
    • 0026729528 scopus 로고
    • AMP deaminase histochemical activity and immunofluorescent isozyme localisation in rat skeletal muscle
    • Thompson JL, Sabina RL, Ogasawara N and Riley DA (1992) AMP deaminase histochemical activity and immunofluorescent isozyme localisation in rat skeletal muscle. J Histochem Cytochem 40: 931-946.
    • (1992) J Histochem Cytochem , vol.40 , pp. 931-946
    • Thompson, J.L.1    Sabina, R.L.2    Ogasawara, N.3    Riley, D.A.4
  • 39
    • 0025932650 scopus 로고
    • Adenine nucleotide metabolism in contracting skeletal muscle
    • Tullson PC and Terjung RL (1991) Adenine nucleotide metabolism in contracting skeletal muscle. Exerc Sport Sci Rev 19: 507-537.
    • (1991) Exerc Sport Sci Rev , vol.19 , pp. 507-537
    • Tullson, P.C.1    Terjung, R.L.2
  • 40
    • 0028277005 scopus 로고
    • Immunolocalization of AMP-deaminase isozymes in human skeletal muscle and cultured muscle cells: Concentration of isoforms M at the neuromuscular junction
    • Van Kuppevelt TH, Veerkamp JH, Fishbein WN, Ogasawara N and Sabina RL (1994) Immunolocalization of AMP-deaminase isozymes in human skeletal muscle and cultured muscle cells: concentration of isoforms M at the neuromuscular junction. J Histochem Cytochem 42: 861-868.
    • (1994) J Histochem Cytochem , vol.42 , pp. 861-868
    • Van Kuppevelt, T.H.1    Veerkamp, J.H.2    Fishbein, W.N.3    Ogasawara, N.4    Sabina, R.L.5
  • 42
    • 0016371046 scopus 로고
    • Effects of exercise on AMP deaminase and adenylosuccinase in rat skeletal muscle
    • Winder WW, Terjung RL, Baldwin KM and Holloszy JO (1974) Effects of exercise on AMP deaminase and adenylosuccinase in rat skeletal muscle. Am J Physiol 227: 1411-1414.
    • (1974) Am J Physiol , vol.227 , pp. 1411-1414
    • Winder, W.W.1    Terjung, R.L.2    Baldwin, K.M.3    Holloszy, J.O.4
  • 43
    • 0015217630 scopus 로고
    • Rabbit muscle adenosine 5′-monophosphate aminohydrolase. Characterization as a zinc metalloenzyme
    • Zielke CL and Suelter CH (1971) Rabbit muscle adenosine 5′-monophosphate aminohydrolase. Characterization as a zinc metalloenzyme. J Biol Chem 246: 2179-2186.
    • (1971) J Biol Chem , vol.246 , pp. 2179-2186
    • Zielke, C.L.1    Suelter, C.H.2


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