Literature DB >> 21533820

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

Sandra Götze1, Reinhard Saborowski.   

Abstract

Decapod crustaceans grow discontinuously and gain size through complex molt processes. The molt comprises the loss of the old cuticle and, moreover, substantial reduction and re-organization of muscles and connective tissues. In adult lobsters, the muscle tissue of the massive claws undergoes significant atrophy of 40-75% before ecdysis. The degradation of this tissue is facilitated by calcium-dependent proteases and by the proteasome, an intra-cellular proteolytic multi-enzyme complex. In contrast to the adults, the involvement of the proteasome during the larval development is yet not validated. Therefore, we developed micro-methods to measure the 20S and the 26S proteasomal activities within mg- and sub-mg-quantities of the larval claw tissue of the European lobster, Homarus gammarus. Within the three larval stages (Z1-3) we distinguished between sub-stages of freshly molted/hatched (post-molt), inter-molt, and ready to molt (pre-molt) larvae. Juveniles were analyzed in the post-molt and in the inter-molt stage. The trypsin-like, the chymotrypsin-like, and the peptidyl-glutamyl peptide hydrolase activity (PGPH) of the 20S proteasome increased distinctly from freshly hatched larvae to pre-molt Z1. During the Z2 stage, the activities were highest in the post-molt animals, decreased in the inter-molt animals and increased again in the pre-molt animals. A similar but less distinct trend was evident in the Z3 stages. In the juveniles, the proteasomal activities decreased toward the lowest values. A similar pattern was present for the chymotrypsin-like activity of the 26S proteasome. The results show that the proteasome plays a significant role during the larval development of lobsters. This is not only reflected by the elevated activities, but also by the continuous change of the trypsin/chymotrypsin-ratio which may indicate a shift in the subunit composition of the proteasome and, thus, a biochemical adjustment to better cope with elevated protein turnover rates during larval development.

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Year:  2011        PMID: 21533820     DOI: 10.1007/s00360-011-0574-2

Source DB:  PubMed          Journal:  J Comp Physiol B        ISSN: 0174-1578            Impact factor:   2.200


  47 in total

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Authors:  K J Davies
Journal:  Biochimie       Date:  2001 Mar-Apr       Impact factor: 4.079

2.  Different proteasome subtypes in a single tissue exhibit different enzymatic properties.

Authors:  B Dahlmann; T Ruppert; L Kuehn; S Merforth; P M Kloetzel
Journal:  J Mol Biol       Date:  2000-11-10       Impact factor: 5.469

Review 3.  The 26S proteasome: a molecular machine designed for controlled proteolysis.

Authors:  D Voges; P Zwickl; W Baumeister
Journal:  Annu Rev Biochem       Date:  1999       Impact factor: 23.643

4.  Mammalian proteasome subpopulations with distinct molecular compositions and proteolytic activities.

Authors:  Oliver Drews; Robert Wildgruber; Chenggong Zong; Ute Sukop; Mikkel Nissum; Gerhard Weber; Aldrin V Gomes; Peipei Ping
Journal:  Mol Cell Proteomics       Date:  2007-07-27       Impact factor: 5.911

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Authors:  O Coux; K Tanaka; A L Goldberg
Journal:  Annu Rev Biochem       Date:  1996       Impact factor: 23.643

6.  NanoDrop fluorometry adopted for microassays of proteasomal enzyme activities.

Authors:  Sandra Götze; Reinhard Saborowski
Journal:  Anal Biochem       Date:  2011-02-20       Impact factor: 3.365

7.  Tissue-specific expression of the subunits of chick 20S proteasomes.

Authors:  S O Hong; J Y Ahn; C S Lee; M S Kang; D B Ha; K Tanaka; C H Chung
Journal:  Biochem Mol Biol Int       Date:  1994-03

Review 8.  Intracellular proteinases of invertebrates: calcium-dependent and proteasome/ubiquitin-dependent systems.

Authors:  D L Mykles
Journal:  Int Rev Cytol       Date:  1998

9.  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.

Authors:  Annette Koenders; Xiaoli Yu; Ernest S Chang; Donald L Mykles
Journal:  J Exp Zool       Date:  2002-06-01

10.  Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung, and liver. Changes in LMP7 and the component necessary for expression of the chymotrypsin-like activity.

Authors:  C Cardozo; A M Eleuteri; M Orlowski
Journal:  J Biol Chem       Date:  1995-09-22       Impact factor: 5.157

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