Batten Disease and mitochondrial pathways of proteolysis

Biochemical and Molecular Medicine

Volumn 57, Issue 1, 1996, Pages 1-9

  Tanner, Allison J ^a   Dice, J Fred ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SUBUNIT;

CHROMOSOME 12; DEGENERATIVE DISEASE; DRUG ACCUMULATION; ENZYME DEGRADATION; FIBROBLAST; GENE MAPPING; HUMAN; LYSOSOME; MITOCHONDRIAL RESPIRATION; NERVE DEGENERATION; NEURONAL CEROID LIPOFUSCINOSIS; OXIDATIVE PHOSPHORYLATION; PROTEIN DEGRADATION; SHORT SURVEY;

EID: 0029925415     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1996.0001     Document Type: Article

References (63)

1. Gobel HH Neuronal ceroid-lipofuscinoses: The current status. Brain Dev 14:203-211, 1992.
2. Boustany R, Alroy J, Kolodny EH. Clinical classification of the neuronal ceroid lipofuscinosis subtypes. Am J Genet 5:47-58, 1982.
3. Jolly RD, Martinus RDJ, Palmer DN. Sheep and other animals with ceroid-lipofuscinoses: Their relevance to Batten Disease. Am J Med Genet 42:609-614, 1992.
4. Hall NA, Lake BD, Dewji NN, Patrick AD. Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis). Biochem J 275:269-272, 1991.
5. Kominami EK, Ezaki J, Muno D, Ishido K, Ueno T, Wolfe LS. Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's Disease). J Biochem 111:278-282, 1992.
6. Tyynela J, Palmer DN, Baumann M, Haltia M. Storage of saposins A and D in infantile neuronal ceroid lipofuscinosis. FEES Lett 330:8-12, 1993.
7. Palmer DN, Fearnley IM, Walker JE, Hall NA, Lake BD, Wolfe LS, Haltia M, Martinus RD, Jolly RD. Mitochondrial ATP synthase subunit c storage in the ceroid-lipofuscinoses (Batten Disease) Am J Med Genet 45:561-567, 1992.
8. Ezaki J, Wolfe LS, Higuti T, Ishido K, Kominami E. Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten Disease) J Neurochem 64:733-741, 1995.
9. Jarvela I, Schleutker J, Haataja L, Santavuori P, Puhakka L, Manninen T, Palotie A, Sandkuiji LA, Renlund M, White R, Aula P, Peltonen L. Infantile form of neuronal ceroid lipofuscinosis (CLN1) maps to the short arm of chromosome 1. Genomics 9:170-173, 1991.
10. Mitchison HM, Thompson AD, Mulley JC, Kozman HM, Richards Rl, Gallen DF, Stallings RL, Doggett NA, Attwood J, McKay TR, Sutherland GR, Gardiner RM. Fine genetic mapping of the Batten Disease locus (CLN3) by haplotype analysis and demonstration of allelic association with chromosome 16p microsatellite loci. Genomics 16:455-460, 1993.
11. Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature 376:584-587, 1995.
12. Medd SM, Walker JE, Jolly RD. Characterization of the expressed genes for subunit c of mitochondrial ATP synthase in sheep with ceroid lipofuscinosis. Biochem J 793:65-73, 1993.
13. Bronson RT, Lake BD, Cook S, Taylor S, Davisson MT. Motor neuron degeneration of mice is a model of neuronal ceroid lipofuscinosis (Battens Disease) Ann Neurol 33:381-385, 1993.
14. Pederson PL, Amzel LM. ATP synthases. J Biol Chem 268:9937-9940, 1993.
15. Attardi G. Biogenesis of mitochondria. Annu Rev Cell Biol 4:289-333, 1988.
16. Johnson LV, Waish ML, Chen LB. Localization of mitochondria in living cells with rhodamine 123. Proc Natl Acad Sci USA 77:990-994, 1980.
17. Hayashi JI, Takemitsu M, Goto Y, Nonaka I. Human mitochondria and mitochondrial genome function as a single dynamic cellular unit. J Cell Biol 125:43-50, 1994.
18. Glover LA, Lindsay JG. Targeting proteins to mitochondria: A current overview. Biochem J 284:609-620, 1992.
19. Kiebler M, Becker K, Pfanner N, Neupert W. Mitochondrial protein import: Specific recognition and membrane translocation of preproteins. J Membr Biol 135:191-207, 1993.
20. Kalousek F, Neupert W, Omura T, Schatz G, Schmitz U. Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins. Trends Biochem Sci 18:249, 1993.
21. Lipsky NG, Pederson PL. Mitochondrial turnover in animal cells. J Biol Chem 265:8652-8657, 1981.
22. Hare JF, Hodges R. Turnover of mitochondrial inner membrane proteins in hepatoma monolayer cultures. J Biol Chem 257:3575-3580, 1982.
23. Dunn WA. Studies on the mechanism of autophagy: Formation of the autophagic vacuole. J Cell Biol 110:1923-1933, 1990.
24. Ueno T, Muno D, Kominami E. Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes from leupeptin-administered rat liver. J Biol Chem 266:18995-18999, 1991.
25. Seglen PO, Gordon PB, Holen I. Nonselective autophagy. Semin Cell Biol 1:441-448, 1990.
26. Pösö AR, Mortimore GE. Requirement for alanine in the amino acid control of deprivation-induced proteolysis in rat liver. Proc Natl Acad Sci USA 81:4270-4274, 1984.
27. Knecht E, Hernandez-Yago J, Grisolia S. Regulation of lysosomal autophagy in transformed and nontransformed mouse fibroblasts under several growth conditions. Exp Cell Res 154:224-232, 1984.
28. Cockle SM, Dean RT. The regulation of proteolysis in normal fibroblasts as they approach confluence: Evidence for the participation of the lysosomal system. Biochem J 208:243-249, 1982.
29. Grisola S, Hernandez-Yago J, Knecht E. Regulation of mitochondrial protein concentration: a plausible model which may permit assessing protein turnover. Curr Topics Cell Regul 27:387-396, 1985.
30. Rapoport S, Schmidt J, Prehn S. Maturation of rabbit reticulocytes: Susceptibility of mitochondria to ATP-dependent proteolysis is determined by the maturational state of reticulocyte. FEBS Lett 183:370-374, 1985.
31. Goldberg AL. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur J Biochem 203:9-23, 1992.
32. Gottesman S, Maurizi MR. Regulation by proteolysis: Energy-dependent proteases and their targets. Microbiol Rev 56:592-621, 1992.
33. Suzuki CK, Suda K, Wang N, Schatz G. Requirement for the yeast gene lon in intramitochondrial proteolysis and main-tenance of respiration. Science 264:273-276, 1994.
34. Wagner I, Arlt H, vanDyke L, Langer T, Neupert W. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13:5135-5145, 1994.
35. Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc Natl Acad Sci USA 90:11247-11251, 1993.
36. Amerik AY, Petukhova G, Grigorenko VG, Lykov IP, Yarovoi SV, Lipkin VM, Gorbalenya AE. Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases. FEES Lett 340:25-28, 1994.
37. Wang N, Maurizi MR, Emmert-Buck L, Gottesman MM. Synthesis, processing, and localization of human Lon protease. J Biol Chem 269:29308-29313, 1994.
38. Desautels M, Goldberg AL. Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J Biol Chem 257:11673-11679, 1982.
39. Watabe S, Kimura T. Adrenal cortex mitochondrial enzyme with ATP-dependent protease and protein-dependent ATPase activities. J Biol Chem 260:14498-14504, 1985.
40. Maurizi MR. ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli. Biochem Soc Trans 19:719-723, 1991.
41. Singh SK, Maurizi MR. Mutational analysis demonstrates different functional roles for the two ATP-binding sites in Clp AP protease from Escherichia coli. J Biol Chem 269:29537-29545, 1994.
42. Wickner S, Gottesman S, Skowyra D, Hoskins J, McKenney K, Maurizi MR. A molecular chaperone, Clp A, functions like DnaK and Dna J. Proc Natl Acad Sci USA 91:12218-12222, 1994.
43. Mian SI. Sequence similarities between cell regulation factors, heat shock proteins and RNA helicases. Trends Biochem Sci 18:125-127, 1993.
44. Dubiel W, Ferrell K, Pratt G, Rechsteiner M. Subunit 4 of the 26S protease Is a member of a novel eukaryotic ATPase family. J Biol Chem 267:22699-22702, 1992.
45. Leonhardt SA, Fearon K, Danese PN, Mason TL. Hsp78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13:6304-6313, 1993.
46. Klausner RD, Sitia R. Protein degradation in the endoplasmic reticulum. Cell 62:611-614, 1990.
47. Warner JR. In the absence of ribosomal RNA synthesis, the ribosomal proteins of Hela cells are synthesized normally and degraded rapidly. J Mol Biol 115:315-333, 1977.
48. Pajic A, Tauer R, Feldmann H, Neupert W, Langer T. Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett 353:201-206, 1994.
49. Tzagoloff A, Yue J, Jang J, Paul MF. A new member of a family of ATPases is essential for assembly of mitochondrial respiratory chain and ATP synthetase complexes in Saccharomyces cerevisiae. J Biol Chem 269:26144-26151, 1994.
50. Buchler M, Tisljar U, Wolf DH. Proteinase yscD (oligopeptidase yscD). Eur J Biochem 219:627-639, 1994.
51. Hawlitschek G, Schneider H, Schmidt B, Tropschug M, Hartl FU, Neupert W. Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein. Cell 53:795-806, 1988.
52. Yang M, Jensen RE, Yaffe MP, Opplinger W, Schatz G. Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes. EMBO J 7:3857-3862, 1988.
53. Ou WJ, Ito A, Okazaki H, Omura T. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J 8:2605-2612, 1989.
54. Emmermann M, Braun HP, Schmitz UK. The mitochondrial processing peptide from potato: a self-processing enzyme encoded by two differentially expressed genes. Mol Gen Genet 245:237-245, 1994.
55. Braun HP, Emmermann M, Kruft V, Schmitz UK. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J 11:3219-3227, 1992.
56. Schmidt B, Wachter E, Sebald W, Neupert W. Processing peptidase of Neurospora mitochondria. Eur J Biochem 144:581-588, 1984.
57. Kalousek F, Isaya G, Rosenberg LE. Rat liver mitochondrial intermediate peptidase (MIP): Purification and initial characterization. EMBO J 11:2803-2809, 1992.
58. Schneider A, Behrens M, Scherer P, Pratje E, Michaelis G, Schatz G. Inner membrane protease 1, an enzyme mediating intramitochondrial protein sorting in yeast. EMBO J 10:247-254, 1991.
59. Behrens M, Michaelis G, Pratje E. Mitochondrial inner membrane protease 1 of Saccharomyces cerevisiae shows sequence similarity to Escherichia coli leader peptidase. Mol Gen Genet 228:167-176, 1991.
60. Ezaki J, Wolfe LS, Ishodoh K, Kominami E. Abnormal degradation pathway of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten Disease). Am J Med Genet 57:254-259, 1995.
61. Faust JR, Rodman JS, Daniel PF, Dice JF, Bronson RT. Two related proteolipids and dolichol-linked oligosaccharides accumulate in motor neuron degeneration mice (mnd/mnd, a model for neuronal ceroid lipofuscinosis. J Biol Chem 269:10150-10155, 1994.
62. Hare JF. Mechanisms of membrane protein turnover. Biochim Biophys Acta 1031:71-90, 1990.
63. Luzikov VN. Proteolytic control over topogenesis of membrane proteins. FEBS Lett 200:259-264, 1986.