Expression patterns of ubiquitin, heat shock protein 70, α-actin and β-actin over the molt cycle in the abdominal muscle of marine shrimp Litopenaeus vannamei

Molecular Reproduction and Development

Volumn 74, Issue 5, 2007, Pages 554-559

  Cesar, Jose Renato O ^a   Yang, Jinzeng ^a,b  

^a UNIVERSITY OF HAWAII   (United States)

^b NONE   (United States)

Author keywords

Actin; Hsp70; L. vannamei; mRNA expression; Muscle; Shrimp; Ubiquitin

Indexed keywords

ALPHA ACTIN; BETA ACTIN; ELONGATION FACTOR 1ALPHA; HEAT SHOCK PROTEIN 70; MESSENGER RNA; UBIQUITIN;

ABDOMINAL WALL MUSCULATURE; ALPHA ACTIN GENE; ANIMAL TISSUE; ARTICLE; BETA ACTIN GENE; CONTROLLED STUDY; DEVELOPMENTAL STAGE; GENE; GENE EXPRESSION REGULATION; HSP 70 GENE; MOLTING; MULTIPLEX POLYMERASE CHAIN REACTION; MUSCLE GROWTH; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA ANALYSIS; SHRIMP; UBIQUITIN GENE;

ABDOMINAL MUSCLES; ACTINS; ANIMALS; GENE EXPRESSION; HSP70 HEAT-SHOCK PROTEINS; MOLTING; PENAEIDAE; PEPTIDE ELONGATION FACTOR 1; RNA, MESSENGER; UBIQUITIN;

ANIMALIA; CRUSTACEA; DECAPODA (CRUSTACEA); LITOPENAEUS VANNAMEI;

EID: 33947708813     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20605     Document Type: Article

References (27)

1. Chan SM, Rankin SM, Keeley LL. 1988. Characterization of the molt stages in Penaeus vannamei: Setogenesis and hemolymph levels of total protein, ecdysteroids and glucose. Biol Bull 175:185-192.
2. Chrysis D, Underwood LE. 1999. Regulation of components of the ubiquitin system by insulin-like growth factor I and growth hormone in skeletal muscle of rats made catabolic with dexamethasone. Endocrinology 140:5635-5641.
3. Dhar AK, Roux MM, Klimpel KR. 2001. Detection and quantification of infectious hypodermal and hematopoietic necrosis virus and white spot virus in shrimp using real-time quantitative PCR and SYBR green chemistry. J Clin Microbiol 39:2835-2845.
4. El Haj AJ. 1996. Crustacean genes involved in growth. In: Ennion S, Goldspink G, editors. Gene regulation in aquatic organisms. SEB Seminar Series. Cambridge: Cambridge University Press. pp 94-112.
5. El Haj AJ, Clarke S, Harrison P, Chang ES. 1996. In vivo muscle synthesis rates in the American lobster Homarus americanis, during the molt cycle and in response to 20-hydroxyecdysone. J Exp Biol 199:579-585.
6. Fang CH, Li BG, Sun XY, Hasselgren PO. 2000. Insulin-like growth factor I reduces ubiquitin and ubiquitin-conjugating enzyme gene expression but does not inhibit muscle proteolysis in septic rats. Endocrinology 141:743-2751.
7. Haas AL, Baboshina O, Williams B, Schwartz LM. 1995. Coordinated induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle. J Biol Chem 270:9407-9412.
8. Harrison P, El Haj AJ. 1994. Actin mRNA levels and myofibrillar growth in leg muscles of the European lobster (H. gammarus) in response to passive stretch. Mol Mar Biol Biotech 3:35-42.
9. Houlihan DF, El Haj AJ. 1985. An analysis of muscle growth. In: Wenner AM, editor. Factors in adult growth. Amsterdam: A. A. Blaskema Press. p 362.
10. Kang WK, Naya Y. 1993. Sequence of the cDNA encoding an actin homolog in the crayfish Procambarus clarkii. Gene 133:303-304.
11. Kim IC, Kim YJ, Song SJ, Lee JS, Lee W. 2003. The intertidal harpacticoid copepod Tigriopus japonicus (Crustacea: Copepoda) beta actin gene: Cloning, sequence and intraspecies variation. DNA Seq 14:279-284.
12. Koenders A, Yu X, Chang ES, Mykles DL. 2002. Ubiquitin and actin expression in claw muscles of land crab, Geocarcinus 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.
13. Macias MT, Sastre L. 1990. Molecular cloning and expression of four actin isoforms during Artemia development. Nucleic Acids Res 18:5219-5225.
14. Moss SM. 2002. Marine shrimp farming in the western hemisphere: Past problems, present solutions, and future visions. Rev Fisheries Sci 10:601-620.
15. Mykles DL. 1997. Crustacean muscle plasticity: Molecular mechanisms determining mass and contractile properties. Comp Biochem Physiol B Biochem Mol Biol 117:367-378.
16. Mykles DL. 1998. Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems. Int Rev Cytol 184:157-289.
17. Mykles DL, Skinner DM. 1990. Atrophy of crustacean somatic muscle and the proteinases that do the job: A review. J Crust Biol 10: 577-594.
18. Pickart CM, Summers RG, Shim H, Kasperek EM. 1991. Dynamics of ubiquitin pools in developing sea urchin embryos. Dev Growth Differ 33:587-598.
19. Pollard TD. 1990. Actin. Curr Opin Cell Biol 2:33-40.
20. Schiaffino S, Reggiani C. 1996. Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiol Rev 76:371-423.
21. 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.
22. Spees JL, Chang SA, Mykles DL, Snyder MJ, Chang ES. 2003. Molt cycle-dependent molecular chaperone and polyubiquitin gene expression in lobster. Cell Stress Chaperones 3:258-264.
23. Whiteley NM, El Haj AJ. 1997. Regulation of muscle gene expression over the moult in crustacea. Comp Biochem Physiol B Biochem Mol Biol 117B:323-331.
24. Whiteley NM, Taylor EW, El Haj AJ. 1992. Actin gene expression during muscle growth in Carcinus maenas. J Exp Biol 167: 277-284.
25. Wing SS, Goldberg AL. 1993. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am J Physiol 264:E668-E676.
26. Yang J, Ratovitski T, Brady JP, Solomon MB, Wells KD, Wall RJ. 2001. Expression of myostatin pro domain results in muscular transgenic mice. Mol Repr Dev 60:351-361.
27. Zhu XJ, Dai ZM, Liu J, Yang WJ. 2005. Actin gene in prawn, Macrobrachium rosenbergii: Characteristics and differential expression during embryonic development. Comp Biochem Physiol B Biochem Mol Biol 140:599-605.