Proteasomal activities in the claw muscle tissue of European lobster, Homarus gammarus, during larval development

Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology

Volumn 181, Issue 7, 2011, Pages 861-871

  Götze, Sandra ^a,b   Saborowski, Reinhard ^a  

^a ALFRED WEGENER INSTITUTE FOR POLAR AND MARINE RESEARCH   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

20S and 26S proteasome; Claws; Lobster larvae; Molt; Muscle atrophy

Indexed keywords

ATP DEPENDENT 26S PROTEASE; PROTEASOME;

ANIMAL; ARTICLE; ENZYMOLOGY; GROWTH, DEVELOPMENT AND AGING; LARVA; METABOLISM; MUSCLE; MUSCLE ATROPHY; MUSCLE DEVELOPMENT; NEPHROPIDAE; PHYSIOLOGY; SKELETAL MUSCLE;

ANIMALS; LARVA; MUSCLE DEVELOPMENT; MUSCLE FIBERS, SKELETAL; MUSCLES; MUSCULAR ATROPHY; NEPHROPIDAE; PROTEASOME ENDOPEPTIDASE COMPLEX;

ANIMALIA; CRUSTACEA; HOMARUS GAMMARUS; LOBSTER;

EID: 80052959771     PISSN: 01741578     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00360-011-0574-2     Document Type: Article

References (52)

1. Ádám G, Gausz J, Noselli S, Kurucz E, Andó I, Udvardy A (2004) Tissue and developmental stage-dependent changes in the subcellular localization of the 26S proteasome in the ovary of Drosophila melanogaster. Gene Expr Patterns 4: 329-333.
2. Ahn JY, Hong SO, Kwak KB, Kang SS, Tanaka K, Ichihara A, Ha DB, Chung CH (1991) Developmental regulation of proteolytic activities and subunit pattern of 20S proteasome in chick embryonic muscle. J Biol Chem 266: 15746-15749.
3. Asher G, Reuven N, Shaul Y (2006) 20S proteasome and protein degradation "by default". BioEssays 28: 844-849.
4. Baumeister W, Walz J, Zühl F, Seemüller E (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92: 367-380.
5. Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-256.
6. Cardozo C, Eleuteri AM, Orlowski M (1995) Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung and liver. J Biol Chem 270: 22645-22651.
7. Charmantier G, Charmantier-Daures M, Aiken DE (1991) Metamorphosis in the lobster Homarus (Decapoda): a review. J Crust Biol 11: 481-495.
8. Coux O, Tanaka K, Goldberg AL (1996) Structure and function of the 20S and the 26S proteasomes. Annu Rev Biochem 65: 801-847.
9. Covi JA, Bader BD, Chang ES, Mykles DL (2010) Molt cycle regulation of protein synthesis in skeletal muscle of the blackback land crab, Gecarcinus lateralis, and the differential expression of a myostatin-like factor during atrophy induced by molting or unweighting. J Exp Biol 213: 172-183.
10. Dahlmann B, Ruppert T, Kuehn LO, Merforth S, Kloetzel PM (2000) Different proteasome subtypes in a single tissue exhibit different enzymatic properties. J Mol Biol 303: 643-653.
11. Davies KJA (2001) Degradation of oxidized proteins by the 20S proteasome. Biochimie 83: 301-310.
12. De Diego JL, Katz JM, Marshall P, Gutierrez B, Manning JE, Nussenzweig V, Gondalez J (2001) The ubiquitin-proteasome pathway plays an essential role in proteolysis during Trypanosoma cruzi remodeling. Biochemistry 40: 1053-1062.
13. De Mot R, Nagy I, Walz J, Baumeister W (1999) Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol 7: 88-92.
14. Drews O, Wildgruber R, Zong C, Sukop U, Nissum M, Weber G, Gomes AV, Ping P (2007) Mammalian proteasome subpopulations with distinct molecular compositions and proteolytic activities. Mol Cell Proteomics 6: 2021-2031.
15. El Haj A, Clarke S, Harrison P, Chang E (1996) In vivo muscle protein synthesis rates in the American lobster Homarus americanus during the molt cycle and in response to 20-hydroxyecdysone. J Exp Biol 199: 579-585.
16. Frisan F, Levitsky V, Polack A, Masucci MG (1998) Phenotype-dependent differences in proteasome subunit composition and cleavage specificity in B cell lines. J Immunol 160: 3281-3289.
17. Galastegui N, Groll M (2010) The 26S proteasome: assembly and function of a destructive machine. Trends Biochem Sci 35: 634-642.
18. Gomes AV, Young GW, Wang Y, Zong C, Eghbali M, Drews O, Lu H, Stefani E, Ping P (2009) Contrasting proteome biology and functional heterogeneity of the 20S proteasome complexes in mammalian tissues. Mol Cell Proteomics 8: 302-315.
19. Götze S, Saborowski R (2011) NanoDrop fluorometry adopted for microassays of proteasomal enzyme activities. Anal Biochem 413: 203-205. doi: 10. 1016/j. ab. 2011. 02. 023.
20. Grune T, Merker K, Sandig G, Davies KJA (2003) Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Comm 305: 709-718.
21. Haass C, Kloetzel PM (1989) The drosophila proteasome undergoes changes in its subunit pattern during development. Exp Cell Res 180: 243-252.
22. Hochstrasser M (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Op Cell Biol 7: 215-223.
23. Hong SO, Ahn JY, Lee CS, Kang MS, Ha DB, Tanaka K, Chung CH (1994) Tissue-specific expression of the subunits of chick 20S proteasomes. Biochem Mol Biol Int 32: 723-729.
24. Husom AD, Peters EA, Kolling EA, Fugere NA, Thompson LV, Ferrington DA (2003) Altered proteasome function and subunit composition in aged muscle. Arch Biochem Biophys 421: 67-76.
25. Ismail SZM, Mykles DL (1992) Differential molt-induced atrophy in the dimorphic claws of the male fiddler crabs, Uca pugnax. J Exp Zool 263: 18-31.
26. Jariel-Encontre I, Bossis G, Piechaczyk M (2008) Ubiquitin independent degradation of proteins by the proteasome. Biochem Biophys Acta Rec Cancer 1786: 153-177.
27. Kisselev AF, Goldberg AL (2001) Proteasome inhibitors: from research tools to drug candidates. Chem Biol 8: 739-758.
28. Kisselev AF, Akopian TN, Castillo V, Goldberg AL (1999) Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell 4: 395-402.
29. Kisselev AF, Kaganowich D, Goldberg AL (2002) Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20S proteasomes. Evidence for peptide-induced channel opening in the α-rings. J Biol Chem 277: 22260-22270.
30. Kisselev AF, Garcia-Calvo M, Overkleeeft HS, Peterson E, Pennington MW, Ploegh HL, Thornberry NA, Goldberg AL (2003) The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites. J Biol Chem 278: 35869-35877.
31. Kisselev A, Callard A, Goldberg AL (2006) Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J Biol Chem 281: 8582-8590.
32. Klein U, Gernold M, Kloetzel P-M (1990) Cell-specific accumulation of Drosophila proteasome (MCP) during early development. Journal Cell Biol 111: 2275-2282.
33. Koenders A, Yu X, Chang ES, Mykles DL (2002) Ubiquitin and actin expression in claw muscles of land crab, Gecarcinus lateralis, and American lobster, Homarus americanus: differential expression of ubiquitin in two slow muscle fiber types during molt-induced atrophy. J Exp Zool 292: 618-632.
34. Liu C-W, Corboy MJ, DeMartino GN, Thomas PJ (2003) Endoproteolytic activity of the proteasome. Science 299: 408-411.
35. Meng L, Mohan R, Kwork BHB, Elofsson M, Sin N, Crews CM (1999) Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity. Proc Natl Acad Sci USA 96: 10403-10408.
36. Mykles DL (1990) Calcium-dependent proteolysis in crustacean claw closer muscle maintained in vitro. J Exp Zool 256: 16-30.
37. Mykles DL (1996) Differential effects of bovine PA28 on six peptidase activities of the lobster muscle proteasome (MCP). Arch Biochem Biophys 325: 77-81.
38. Mykles DL (1997) Biochemical properties of insect and crustacean proteasomes. Mol Biol Rep 24: 133-138.
39. Mykles DL (1998) Intracellular proteinases of invertebrates: calcium-dependent and proteasome/ubiquitin-dependent systems. Int Rev Cytol 184: 157-289.
40. Mykles DL (1999a) Proteolytic processes underlying molt-induced claw muscle atrophy in decapod crustaceans. Am Zool 39: 541-551.
41. Mykles DL (1999b) Structure and functions of arthropod proteasomes. Mol Biol Rep 26: 103-111.
42. Mykles DL, Haire MF (1991) Sodium dodecyl sulfate and heat induce two distinct forms of lobster muscle multicatalytic proteinase: the heat-activated form degrades myofibrillar proteins. Arch Biochem Biophys 288: 543-551.
43. Mykles DL, Skinner DM (1981) Preferential loss of thin filaments during molt-induced atrophy in crab claw muscle. J Ultrastruc Res 75: 314-325.
44. Naujokat C, Hoffmann S (2002) Role and function of the 26S proteasome in proliferation and apoptosis. Lab Invest 82: 965-980.
45. Orlowski M, Wilk S (2003) Ubiquitin-independent proteolytic function of the proteasome. Arch Biochem Biophys 415: 1-5.
46. Pelletier S, Schuurman KG, Berkers CR, Ovaa H, Heck AJR, Raijmakers R (2010) Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry. Mol BioSyst 6: 1450-1453.
47. Richter-Ruoff B, Wolf DH (1993) Proteasome and cell cycle: evidence for a regulatory role of the proteasome on mitotic cyclins in yeast. FEBS Lett 336: 34-36.
48. Schmalenbach I, Fanke HD (2010) Potential impact of climate warming on the recruitment of an economically and ecologically species, the European lobster (Homarus gammarus) at Helgoland, North Sea. Mar Biol 157: 1127-1135.
49. Shean BS, Mykles DL (1995) Polyubiquitin in crustacean striated muscle: increased expression and conjugation during molt-induced claw muscle atrophy. Biochim Biophys Acta 1264: 312-322.
50. Skinner DM (1966) Macromolecular changes associated with the growth of crustacean tissues. Am Zool 6: 235-242.
51. Verras M, Gourzi P, Kalosaka K, Zacharopoulou A, Mintzas AC (2008) cDNA cloning, characterization, and developmental expression of the 20S proteasome α5 subunit in the Mediterranean fruit fly Ceratitis capitata. Arch Insect Biochem Physiol 67: 120-129.
52. Voges D, Zwickel P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. An Rev Biochem 68: 1015-1068.