High activities of cathepsins B, D, H and L in the white muscle of chum salmon in spawning migration

Yamashita, Michiaki; Konagaya, Shiro

doi:10.1016/0305-0491(90)90262-r

Cited by 47 publications

(34 citation statements)

References 9 publications

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“…The reduction in muscle protein is coupled with an increase in muscle water content and muscle softness, suggesting that the broken-down proteins are replenished with water (58). Similar patterns of muscle wastage have been described in other fish, such as sockeye salmon, Oncorhynchus nerka (50), and chum salmon, Oncorhynchus keta (51,74). These changes are consistent with a general pattern of muscle wastage, which supports using RBT as an ideal model to elucidate the molecular mechanisms of muscle catabolism in fish.…”

Section: Muscle Atrophy In Response To Vitellogenesismentioning

confidence: 52%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

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Salem M, Kenney PB, Rexroad CE 3rd, Yao J. Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model. Physiol Genomics 28: 33-45, 2006. First published August 1, 2006; doi:10.1152/physiolgenomics.00114.2006.-Muscle atrophy is a physiological response to diverse physiological and pathological conditions that trigger muscle deterioration through specific cellular mechanisms. Despite different signals, the biochemical changes in atrophying muscle share many common cascades. Muscle deterioration as a physiological response to the energetic demands of fish vitellogenesis represents a unique model for studying the mechanisms of muscle degradation in non-mammalian animals. A salmonid microarray, containing 16,006 cDNAs, was used to study the transcriptome response to atrophy of fast-switch muscles from gravid rainbow trout compared with sterile fish. Eighty-two unique transcripts were upregulated and 120 transcripts were downregulated in atrophying muscles. Transcripts having gene ontology identifiers were grouped according to their functions. Muscle deterioration was associated with elevated expression of genes involved in the catheptic and collagenase proteolytic pathways; the aerobic production, buffering, and utilization of ATP; and growth arrest; whereas atrophying muscle showed downregulation of genes encoding a serine proteinase inhibitor, enzymes of anaerobic respiration, muscle proteins as well as genes required for RNA and protein biosynthesis/processing. Therefore, gene transcription of the trout muscle atrophy changed in a manner similar to mammalian muscle atrophy. These changes result in an arrest of normal cell growth, protein degradation, and decreased glycolytic cellular respiration that is characteristic of the fast-switch muscle. For the first time, other changes/mechanisms unique to fish were discussed including genes associated with muscle atrophy. atrophy; Oncorhynchus mykiss SEVERAL PHYSIOLOGICAL and pathological conditions can cause muscle atrophy by triggering unique responses through distinct cellular stimuli. Transcriptional mechanisms of muscle wastage are well characterized at the transcriptome level in mammalian models as a response to nutritional restriction (7), fasting, severe diseases, including cancer, renal failure, diabetes (41, 42), and sepsis (42), as well as muscle disuse or denervation (4, 57). Some studies have dealt with fish muscle atrophy at the level of individual genes/mechanisms (46, 51, 58, 60 -62). The molecular basis of mammalian muscle atrophy has received considerable attention in the literature (25,30). Losing muscle mass results from elevated rate of proteolysis and decreased rate of protein synthesis. Despite the significant amount of literature (30,32,42), the specific roles of the proteolytic systems in degrading mammalian muscle still are unclear. Moreover, we recently showed that fish use different muscle degrading proteolytic strategies compared with mammals (58). The ubiquitin-proteasome pathway,...

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Section: Muscle Atrophy In Response To Vitellogenesismentioning

confidence: 52%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

View full text Add to dashboard Cite

show abstract

“…The most studied species in this respect is the chum salmon (Oncorhynchus keta). In spawning migrating chum salmon the muscle contains high activities of cathepsins B, H, L, and D (Yamashita and Konagaya 1990a). Cathepsin B and L have also been purified and characterized from the white muscle of chum salmon (Yamashita and Konagaya 1990b, c).…”

Section: Introductionmentioning

confidence: 98%

Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

Tähtinen

Weber

Günther

et al. 2002

Cell and Tissue Research

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Tissue localization of cysteine proteinases (cathepsins) and their inhibitors (salarin, salmon kininogen) was performed in tissues of the Atlantic salmon. In skin, both epidermis and dermis were strongly stained by antisera against salarin and salmon kininogen. In epidermis the intercellular space seemed to be heavily stained (salarin). In kidney, the inhibitors were mainly localized to the interstitial capillaries. Also, some epithelial cells of the tubules (salarin) and some cells of the interstitium were stained. Mostly, the staining had a diffuse cytoplasmic localization. In the liver some hepatocytes were strongly positive for salarin and salmon kininogen. Purified fish cysteine proteinase inhibitors were not found to inhibit the growth of fish pathogenic bacteria and viruses. In the trunk kidney cathepsins B and L were localized in epithelial cells of the tubules (proximal part) and in cells of the interstitium. Mostly, the staining showed a prominent lysosomal localization. In head kidney large macrophage-like cells were positively stained for cathepsin B. The staining was localized to granula/vacuoles in the cytoplasm. In the liver, some hepatocytes were strongly stained and some were less strongly positive for cathepsin B and L. Mostly, the hepatocytes showed lysosomal staining. Cathepsin L was found in some big macrophage-like cells in the spleen. Mucosal epithelial cells of the esophagus and intestine seemed to be strongly stained for cathepsin B and L. The results show that cathepsins and their inhibitors are specifically and widely distributed in the Atlantic salmon skin indicating that they perform some biologically important and specific but so far unknown functions.

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“…Assay of cathepsin L. Cathepsin L was assayed with cathepsin B using Z-Phe-Arg-MNA (21,22) substrate with the same method and under the same conditions as those used to measure the Z-A/A-ArgArg-MNA-hydrolyzing activity of cathepsin B. Since this substrate is hydrolyzed by both cathepsins B and L, this hydrolytic activity was expressed as activity of cathepsin B ϩ L.…”

Section: Methodsmentioning

confidence: 99%

Role of cysteine proteases and protease inhibitors in gastric mucosal damage induced by ethanol or ammonia in the rat.

Nagy¹,

Kusstatscher²,

Hauschka³

et al. 1996

J. Clin. Invest.

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Since recent studies suggest an imbalance between cathepsin B and its tissue protease inhibitors (PI) in the pathogenesis of acute and chronic diseases, we tested the hypothesis that release of activated cysteine proteases (P) such as cathepsins B, H, and L might play a role in the pathogenesis of gastric hemorrhagic mucosal lesions (HML) induced by ethanol (E) or ammonia (A). Anesthetized rats received 1 ml of 50% E or 1% A solution intragastrically for 1 min during in situ gastric luminal perfusion. Rapid activation and release of cathepsins B, L, and H into the luminal perfusate preceded the formation of HML quantified by planimetry. Mucosal presence and activity of cysteine PI and cathepsin B have also been investigated in the pathogenesis of chemically induced HML. We extracted and partially isolated acid and thermostable inhibitors of cathepsin B in the gastric mucosa, and found rapid inactivation of PI and activation of cathepsin B in the early phase of E-or A-induced HML. Negative correlations were found between P and PI activities by E or A solutions. Both the activation of cathepsins B, L, and H and the development of E-induced HML were prevented by pretreatment with the sulfhydryl alkylator N -ethylmaleimide. These results suggest that cysteine P may be activated in the rat stomach after E or A exposure, and cysteine P may have a role in the pathogenesis of E-or A-induced gastric HML. Endogenous PI may also participate in the mechanisms of gastric mucosal lesions and gastroprotection. ( J. Clin. Invest. 1996. 98:1047-1054.)

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High activities of cathepsins B, D, H and L in the white muscle of chum salmon in spawning migration

Cited by 47 publications

References 9 publications

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

Role of cysteine proteases and protease inhibitors in gastric mucosal damage induced by ethanol or ammonia in the rat.

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