Éditeur(s) : HAL CCSD Histochemical Society
Résumé : International audience
The galectin-4 protein is mostly expressed in the digestive tract and is associated with lipid raft stabilization, protein apical trafficking, wound healing, and inflammation. While most mammalian species, including humans, have a single Lgals4 gene, some mice have two paralogues: Lgals4 and Lgals6. So far, their significant similarities have hindered the analysis of their respective expression and function. We took advantage of two antibodies that discriminate between the galectin-4 and galectin-6 proteins to document their patterns of expression in the normal and the dextran sodium sulfate (DSS)-damaged digestive tract in the mouse. In the normal digestive tract, their pattern of expression from tongue to colon is quite similar, which suggests functional redundancy. However, the presence of galectin-4, but not galectin-6, in the lamina propria of the DSS-damaged colon, its association with luminal colonic bacteria, and differences in subcellular localization of these proteins suggest that they also have distinct roles in the normal and the damaged mouse digestive tract. Our results provide a rare example of ancestral and derived functions evolving after tandem gene duplication.
ISSN: 0022-1554

hal-01544764
https://hal.archives-ouvertes.fr/hal-01544764
DOI : 10.1369/0022155413478612

Éditeur(s) : HAL CCSD Wiley
Résumé : International audience
Strombus gigas and Strombus pugilis are threatened species and aquaculture represents a good alternative solution to the fishing. In this study, we highlighted the intracellular digestion process in the digestive gland of two Strombidae species, S. gigas and Strombus pugilis, by the cytochemical characterization of two lysosomal enzymes: acid phosphatase and arylsulfatase. In order to check the efficiency of artificial food digestion, we onducted the characterization on freshly collected, tarved and artificially fed individuals of S. pugilis. TEM observations of digestive gland sections from freshly collected individuals of both species revealed the resence of acid phosphatase and arylsulfatase activity mostly located in the apical third of digestive cells. Both enzymes were also detected in artificially fed individuals. In response to the starvation, acid phosphatase is not produced anymore by digestive cells, while arylsulfatase is still present. To our knowledge, this is the first cytochemical validation of intracellular digestion of artificial food in Strombidae. This study highlights the intracellular digestion of artificial food developed for Strombidae aquaculture. Moreover, we have shown that the lysosomal activity could be used as a feed index.
ISSN: 1059-910X

hal-00743013
https://hal.univ-antilles.fr/hal-00743013
DOI : 10.1002/jemt.22074

Éditeur(s) : HAL CCSD American Chemical Society
Résumé : International audience
The present study is a contribution to the "neXt50 challenge", a coordinated effort across C-HPP teams to identify the SO most tractable missing proteins (MPs) on each chromosome. We report the targeted search of 38 theoretically detectable MPs from chromosomes 2 and 14 in Triton X-100 soluble and insoluble sperm fractions from a total of 15 healthy donors. A targeted mass spectrometry-based strategy consisting of the development of LC-PRM assays (with heavy labeled synthetic peptides) targeting 92 proteotypic peptides of the 38 selected MPs was used. Out of the 38 selected MPs, 12 were identified with two or more peptides and 3 with one peptide after extensive SDS-PAGE fractionation of the two samples and with overall low-intensity signals. The PRM data are available via ProteomeXchange in PASSEL (PASS01013). Further validation by immunohistochemistry on human testes sections and cytochemistry on sperm smears was performed for eight MPs with antibodies available from the Human Protein Atlas. Deep analysis of human sperm still allows the validation of MPs and therefore contributes to the C-HPP worldwide effort. We anticipate that our results will be of interest to the reproductive biology community because an in-depth analysis of these MPs may identify potential new candidates in the context of human idiopathic infertilities.
ISSN: 1535-3893

hal-01681656
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01681656
DOI : 10.1021/acs.jproteome.7b00374

Éditeur(s) : HAL CCSD Wiley
Résumé : International audience
The Caribbean bivalves Codakia orbicularis (Linnée, 1758) and C. orbiculata (Montagu, 1808) live in seagrass beds of Thalassia testudinum and harbor intracellular sulfuroxidizing gamma-proteobacteria. These bacterial symbionts fix CO2 via the Calvin Benson cycle and provide organic compounds to the bivalve. During experimentally induced starvation, no reduced sulfur compounds and no organic particle food are available; the symbionts could be considered as the sole nutrient source of the host bivalve. A previous study has shown that the intracellular bacterial population decreased considerably during starvation and that bacterial endosymbionts were not released by the bivalves. In this study, the activity of two lysosomal marker enzymes (acid phosphatase and arylsulfatase) was detected using cytochemical experiments coupled with energy-dispersive X-ray transmission electron microscopy during sulfide and organic particle starvation. The degradation of bacterial endosymbionts began after 2 weeks of starvation in C. orbiculata and after 3 weeks in C. orbicularis. Degradation processes seem to be continuous over several months and could be responsible for the disappearance of the bacterial endosymbionts within the gills during starvation. These data suggest that the host use symbionts as a nutrient source to survive a hunger crisis. The carbon transfer from the symbionts to the host could be flexible and could consist in transfer of organic matter, “milking,” under normal feeding conditions and digestion of the symbionts under starved conditions.
ISSN: 1059-910X

Droits : info:eu-repo/semantics/OpenAccess
hal-01206367
https://hal.univ-antilles.fr/hal-01206367
https://hal.univ-antilles.fr/hal-01206367/document
https://hal.univ-antilles.fr/hal-01206367/file/revised%20version%20to%20be%20submitted%20to%20the%20editor3oct.pdf
DOI : 10.1002/jemt.22458