Identification and primary characterization of specific proteases in the digestive juice of Archachatina ventricosa

Guionie, Olivier; Moallic, Claire; Niamké, Sebastien; Placier, Gaël; Sine, Jean Pierre; Colas, Bernard

doi:10.1016/s1096-4959(03)00115-5

Cited by 10 publications

(4 citation statements)

References 26 publications

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“…1D) is an enzyme involved in both gluconeogenesis and glycogenolysis and has two members on Hsa 17 and one on Hsa 2 [70]. Due to lack of sequences from Ciona and Branchiostoma floridae , the time window when the expansion of this family took place is wide.…”

Section: Resultsmentioning

confidence: 99%

Phylogenetic and chromosomal analyses of multiple gene families syntenic with vertebrate Hox clusters

2008

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BackgroundEver since the theory about two rounds of genome duplication (2R) in the vertebrate lineage was proposed, the Hox gene clusters have served as the prime example of quadruplicate paralogy in mammalian genomes. In teleost fishes, the observation of additional Hox clusters absent in other vertebrate lineages suggested a third tetraploidization (3R). Because the Hox clusters occupy a quite limited part of each chromosome, and are special in having position-dependent regulation within the multi-gene cluster, studies of syntenic gene families are needed to determine the extent of the duplicated chromosome segments. We have analyzed in detail 14 gene families that are syntenic with the Hox clusters to see if their phylogenies are compatible with the Hox duplications and the 2R/3R scenario. Our starting point was the gene family for the NPY family of peptides located near the Hox clusters in the pufferfish Takifugu rubripes, the zebrafish Danio rerio, and human.ResultsSeven of the gene families have members on at least three of the human Hox chromosomes and two families are present on all four. Using both neighbor-joining and quartet-puzzling maximum likelihood methods we found that 13 families have a phylogeny that supports duplications coinciding with the Hox cluster duplications. One additional family also has a topology consistent with 2R but due to lack of urochordate or cephalocordate sequences the time window when these duplications could have occurred is wider. All but two gene families also show teleost-specific duplicates.ConclusionBased on this analysis we conclude that the Hox cluster duplications involved a large number of adjacent gene families, supporting expansion of these families in the 2R, as well as in the teleost 3R tetraploidization. The gene duplicates presumably provided raw material in early vertebrate evolution for neofunctionalization and subfunctionalization.

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Section: Resultsmentioning

confidence: 99%

Phylogenetic and chromosomal analyses of multiple gene families syntenic with vertebrate Hox clusters

2008

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“…Proteolytic enzymes have been studied in vetigastropods (genera Haliotis and Megathura [9], [10]), stylommatophoran pulmonates (genera Helix , Elona , Archachatina, Arion and Dermoceras [11], [12], [13], [14]), opistobranchs (genera Hermissenda and Aeolidia , [15]) and in an architaenioglossan (genus Viviparus [16]), but lack of proteases has been reported in the ampullariids Pila virens [17] and Pomacea canaliculata [4], the species which is studied here.…”

Section: Introductionmentioning

confidence: 99%

Endosymbiotic and Host Proteases in the Digestive Tract of the Invasive Snail Pomacea canaliculata: Diversity, Origin and Characterization

2013

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Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands and their apparent molecular weights were identified in both tissue extracts and luminal contents by gel zymography: (1) a 125 kDa protease in salivary gland extracts and in the crop content; (2) a 30 kDa protease throughout all studied luminal contents and in extracts of the midgut gland and of the endosymbionts isolated from this gland; (3) two proteases of 145 and 198 kDa in the coiled gut content. All these proteases were inhibited by aprotinin, a serine-protease inhibitor, and showed maximum activity between 30°C and 35°C and pH between 8.5 and 9.5. Tissue L-alanine-N-aminopeptidase activity was determined in the wall of the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Our findings show that protein digestion in P. canaliculata is carried out through a battery of diverse proteases originated from the salivary glands and the endosymbionts lodged in the midgut gland and by proteases of uncertain origin that occur in the coiled gut lumen.

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“…On the basis of their comparison, a conclusion is drawn on the preference of certain amino acids in the P1 position for this enzyme [2][3][4]. This method requires a good synthetic basis and long kinetic work.…”

Section: Introductionmentioning

confidence: 99%

Theoretical possibilities and limitations of protease primary specificity determination by statistical analysis of MALDI mass-spectra of proteolysis products

2012

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Possibilities and limitations of the method of examination of proteolytic enzymes' primary spec ificity by statistical analysis of MALDI (matrix assisted laser desorption/ionization) mass spectra of products obtained by protein substrate proteolysis, without direct determination of their amino acid sequences, were investigated theoretically. The optimum range given by the measurement errors of the peptides' masses for obtaining a statistical set of the events, and the form of statistical data presentation, were chosen. It was shown that the proposed method can be applied only for proteases with a relatively narrow primary specificity (two or three amino acids). The influence of protein substrate molecular weight and amino acid composition on the efficiency of specifics for a particular protease amino acid, revealed under statistical treatment of the set of proteolysis product masses, was studied on the model of trypsin, chymotrypsin, glutamylendopeptidase, pepsin (pH 1.3).

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Identification and primary characterization of specific proteases in the digestive juice of Archachatina ventricosa

Cited by 10 publications

References 26 publications

Phylogenetic and chromosomal analyses of multiple gene families syntenic with vertebrate Hox clusters

Phylogenetic and chromosomal analyses of multiple gene families syntenic with vertebrate Hox clusters

Endosymbiotic and Host Proteases in the Digestive Tract of the Invasive Snail Pomacea canaliculata: Diversity, Origin and Characterization

Theoretical possibilities and limitations of protease primary specificity determination by statistical analysis of MALDI mass-spectra of proteolysis products

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