Genomic organisation and polymorphism of a Crustacean trypsin multi-gene family

Klein, B.; Sellos, Daniel; Wormhoudt, Alain Van

doi:10.1016/s0378-1119(98)00331-x

Cited by 31 publications

(26 citation statements)

References 34 publications

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“…4). This is consistent with the presence of multigene trypsin families in other arthropods (Klein et al 1996(Klein et al , 1998Gaines et al 1999). It may also account for some of the trypsin isoforms reported here.…”

Section: Resultssupporting

confidence: 92%

“…The signal peptide as mentioned previously has little amino acid similarity to the vertebrate signal peptides (see Roach et al 1997). Furthermore, the signal peptides of the L. salmonis trypsins are not similar to the signal peptides of P. leniusculus and L. vannamei (Table 1; Klein et al 1998;Herna´ndez-Corte´s et al 1999).…”

Section: Resultsmentioning

confidence: 91%

“…2. All of the trypsin types have identical amino terminal sequences (Ile-Val-Gly-Gly) which are shared with other crustacean and vertebrate trypsins (Table 1; Klein et al 1998). The sequences of the L. salmonis trypsins encode for mature proteins (active enzymes) of 223 amino acids with calculated molecular weights ranging from 23.6 to 23.7 kDa.…”

Section: Resultsmentioning

confidence: 99%

“…Five trypsin cDNAs, which belong to two trypsin families, have been reported for the shrimp Litopenaeus vannamei (formerly Penaeus vannamei) (Klein et al 1996). Further, study of trypsin genes from L. vannamei resulted in the sequencing of three trypsin genes belonging to distinct trypsin families (Klein et al 1998). A cDNA sequence encoding the synthesized trypsin zymogen from crayfish Pacifastacus leniusculus hepatopancreas has also been determined (Herna´ndez-Corte´s et al 1999).…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning of trypsin cDNAs and trypsin gene expression in the salmon louse Lepeophtheirus salmonis (Copepoda: Caligidae)

Johnson

Ewart

Osborne

et al. 2002

Parasitology Research

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The salmon louse, Lepeophtheirus salmonis, is a marine ectoparasitic copepod that infects salmonid fishes. We are studying the interactions between this parasite and its salmonid hosts, as it is a common cause of disease in both wild and farmed stocks of salmon. In this paper, we report on the cloning and sequencing of seven trypsin-like enzymes from a cDNA library prepared from whole body preadult female and male L. salmonis. The predicted trypsin activation peptides are 23 or 24 residues in length, considerably longer than previously reported activation peptides of other animals. Differences in the putative signal and activation peptide sequences of the trypsin isoforms suggest that these forms differ in their regulation and function. The calculated molecular weights of the trypsins range from 23.6 to 23.7 kDa. There are eight cysteine residues, which suggest the presence of four disulfide bridges. These trypsins are very similar (>or=46% aa identity) to other crustacean trypsins and insect hypodermins. Using in situ hybridization techniques trypsinogen expression could be identified in all three cell types of the midgut.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular cloning of trypsin cDNAs and trypsin gene expression in the salmon louse Lepeophtheirus salmonis (Copepoda: Caligidae)

Johnson

Ewart

Osborne

et al. 2002

Parasitology Research

View full text Add to dashboard Cite

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“…Many of these processes are also known to involve serine proteases in arthropods (Klein et al 1998;Benjamin et al 2001;Cooper et al 2002;Cerenius and Söderhäll 2004). The extent of these processes provides little information about the possible function of OET-03.…”

Section: Introductionmentioning

confidence: 99%

Olfactory specific chymotrypsin-like serine protease from the aesthetasc tegumental gland of the lobster, Homarus americanus

2005

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Numerous proteases and protease inhibitors are expressed in the lobster olfactory organ. One of these proteases, olfactory enriched transcript 03 (OET-03), is particularly interesting because its mRNA is expressed only in one cell type of the olfactory organ of the American lobster, Homarus americanus. We have obtained a full-length cDNA clone of OET-03. The predicted amino acid sequence is equally divided between a novel N-terminal domain and a conserved serine protease catalytic domain at the C-terminus. Heterologous expression in HEK293 cells allowed protease assays demonstrating that OET-03 cleaved a specific serine protease substrate, N-alpha benzoyl-L-arginine p-nitroanilide, but did not cleave a substrate of metalloproteases and cysteine proteases. OET-03 protease activity was significantly inhibited by the chymotrypsin-like protease inhibitor, tosyl-L-phenylalanine chloromethyl ketone, but not by the general protease inhibitor, phenylmethylsulfonyl fluoride. Immunoreactivity for OET-03 was detected only in the cells previously shown to contain OET-03 mRNA. The cytoplasm of these cells was filled with enlarged smooth endoplasmic reticulum (a characteristic of secretory cells) that appeared to expand into large electron-translucent areas at the ventral end of the cell. The ventral ends of these secretory cells were apposed to phalloidin-labeled triangular structures reminiscent of the beginnings of the ducts of crustacean tegumental glands. This putative gland was found only in association with the aesthetasc sensory units of the olfactory organ, hence the name, aesthetasc tegumental gland.

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Invertebrate trypsins: a review

Sánchez‐Paz²,

2008

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Food protein hydrolysis, a crucial step in digestion, is catalyzed by trypsin enzymes from the digestive apparatus of invertebrates. Trypsin appeared early in evolution and occurs in all phyla and, in the digestive systems of invertebrates, it became the most abundant proteinase. As in vertebrates, invertebrate trypsin is also present in several forms (isoenzymes). Its physiological importance in food protein digestion in several invertebrate species has emerged with compelling evidence; and several other physiological functions, such as regulation of digestive functions, are now settled. Recent advances in the knowledge of invertebrate trypsin synthesis, regulation, genetics, catalytic characteristics; structure, evolution, as well as inhibition, especially in non-Drosophilidae insects and in some crustaceans are reviewed. Most of the existing information is largely based on the use of several tools, including molecular techniques, to answer many still open questions and solve medical, agricultural, and food quality problems.

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Genomic organisation and polymorphism of a Crustacean trypsin multi-gene family

Cited by 31 publications

References 34 publications

Molecular cloning of trypsin cDNAs and trypsin gene expression in the salmon louse Lepeophtheirus salmonis (Copepoda: Caligidae)

Molecular cloning of trypsin cDNAs and trypsin gene expression in the salmon louse Lepeophtheirus salmonis (Copepoda: Caligidae)

Olfactory specific chymotrypsin-like serine protease from the aesthetasc tegumental gland of the lobster, Homarus americanus

Invertebrate trypsins: a review

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