Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)

Komai, Tsuyoshi; Kawabata, Choko; Amano, Mitsuyo; Lee, Byung Rho; Ichishima, Eiji

doi:10.1016/j.cbpc.2004.01.006

Cited by 21 publications

(26 citation statements)

References 30 publications

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“…Human preprocathepsin, procathepsin and cathepsin D differ from their equivalents isolated from the mammalian tissue in a number of particulars concerning the amino acid sequence, posttranslatory modifications and conformatory structure [169]. Due to the differences, human anti-cathepsin D antibodies do not react with cathepsin D of other species [170].…”

Section: Final Commentsmentioning

confidence: 99%

Human cathepsin D.

Minarowska

Gacko²,

Karwowska³

et al. 2008

Folia Histochem Cytobiol.

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Section: Final Commentsmentioning

confidence: 99%

Human cathepsin D.

Minarowska

Gacko²,

Karwowska³

et al. 2008

Folia Histochem Cytobiol.

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“…3.4.22.1, 3.4.22.15, and 3.4.23.5, respectively) in EC group 3. Among these cathepsins, the cathepsin D of Japanese common squid Todarodes pacificus has been already purified from the liver and characterized [11]. Cathepsin belongs to the aspartic proteinase group.…”

Section: Resultsmentioning

confidence: 99%

“…Squid liver has been known to concentrate essential and non-essential elements and has, therefore, been used as a bioindicator to monitor for the presence of pollutants in the ocean [5,6]. In studies aimed at further developing the applications of the squid liver, a number of enzymes have been purified from the squid liver [7][8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Identification of enzyme genes in the liver of the Bleeker’s squid Loligo bleekeri by expressed sequence tag analysis

et al. 2009

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Expressed sequence tag (EST) analyses were performed with the aim of identifying enzyme genes in the liver of the Bleeker's squid Loligo bleekeri. Of the 768 ESTs identified and sequenced, 669 were grouped into 324 clusters. Of these clusters, 123 comprising 245 ESTs were found to be homologous to genes reported to date. Among these, 43 clusters were annotated as enzymes according to the Enzyme Commission (EC) numbering system. Two EC groups, oxidoreductases and hydrolases, possessed a large number of ESTs. A cluster homologous to the glutathione peroxidase, an enzyme in the oxidoreductase group, contained 16 ESTs, which accounted for 2.4% of the total ESTs sequenced. There are three serine proteases, three cathepsins, two triacylgricerol lipases, and two chitinases among the clusters homologous to the enzymes in the hydrolase group. Since the squid liver functions in the digestive process, these enzymes would be involved in food digestion. Our data provide information on the various types of enzymes expressed in the squid liver and may provide a useful basis for further characterization of these enzymes.

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“…However, in this study we deduced that one of the cleavage sites shared by all three aspartic acid peptidases, VIF↓FRL was highly similar to a sequence in a commercially available fluorescent substrate, mca-GKPILFFRLK(dnp). Komei and colleagues have determined that cathepsin D from the hepatopancreas of Todarodes pacificus (Japanese common squid) cleaves this fluorescent substrate between the two Phe residues (Komai et al 2004). We deduced that designing a new fluorescent substrate that would be robustly cleaved by all three aspartic peptidases was not required and therefore this general aspartic acid substrate was used for subsequent biochemical studies.…”

Section: Sequence and Specificity Comparison Of H Americanus Cathepsmentioning

confidence: 99%

Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion

et al. 2015

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Crustaceans are a diverse group, distributed in widely variable environmental conditions for which they show an equally extensive range of biochemical adaptations. Some digestive enzymes have been studied by purification/characterization approaches. However, global analysis is crucial to understand how digestive enzymes interplay. Here we present the first proteomic analysis of the digestive fluid from a crustacean (Homarus americanus) and identify glycosidases and peptidases as the most abundant classes of hydrolytic enzymes. The digestion pathway of complex carbohydrates was predicted by comparing the lobster enzymes to similar enzymes from other crustaceans.A novel and unbiased substrate profiling approach was used to uncover the global proteolytic specificity of gastric juice and determine the contribution of cysteine and aspartic acid peptidases. These enzymes were separated by gel electrophoresis and their individual substrate specificities uncovered from the resulting gel bands. This new technique is called zymoMSP. Each cysteine peptidase cleaves a set of unique peptide bonds and the S2 pocket determines their substrate specificity. Finally, affinity chromatography was used to enrich for a digestive cathepsin D1 to compare its substrate specificity and cold-adapted enzymatic properties to mammalian enzymes. We conclude that the H.americanus digestive peptidases may have useful therapeutic applications, due to their cold-adaptation properties and ability to hydrolyze collagen.

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Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)

Cited by 21 publications

References 30 publications

Human cathepsin D.

Human cathepsin D.

Identification of enzyme genes in the liver of the Bleeker’s squid Loligo bleekeri by expressed sequence tag analysis

Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion

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