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      Immunohistochemical localization of hepatopancreatic phospholipase A 2 in Hexaplex Trunculus digestive cells

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          Abstract

          Background

          Mammalian sPLA 2-IB localization cell are well characterized. In contrast, much less is known about aquatic primitive ones. The aquatic world contains a wide variety of living species and, hence represents a great potential for discovering new lipolytic enzymes and the mode of digestion of lipid food.

          Results

          The marine snail digestive phospholipase A 2 (mSDPLA 2) has been previously purified from snail hepatopancreas. The specific polyclonal antibodies were prepared and used for immunohistochimical and immunofluorescence analysis in order to determine the cellular location of mSDPLA 2. Our results showed essentially that mSDPLA 2 was detected inside in specific vesicles tentatively named (mSDPLA 2+) granules of the digestive cells. No immunolabelling was observed in secretory zymogene-like cells. This immunocytolocalization indicates that lipid digestion in the snail might occur in specific granules inside the digestive cells.

          Conclusion

          The cellular location of mSDPLA 2 suggests that intracellular phospholipids digestion, like other food components digestion of snail diet, occurs in these digestive cells. The hepatopancreas of H. trunculus has been pointed out as the main region for digestion, absorption and storage of lipids.

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          Most cited references16

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          CHLOROPLAST SYMBIOSIS IN A NON-ELYSIID MOLLUSC,COSTASIELLA LILIANAEMARCUS (HERMAEIDAE: ASCOGLOSSA (=SACOGLOSSA): EFFECTS OF TEMPERATURE, LIGHT INTENSITY, AND STARVATION ON CARBON FIXATION RATE

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            • Abstract: not found
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            Chloroplasts as symbiotic organelles in the digestive gland of Elysia viridis [Gastropoda: opisthobranchia]

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              Ultrastructure of the hepatopancreas of the Pacific white shrimp, Penaeus vannamei (Crustacea: Decapoda)

              Fourteen specimens of the hepatopancreas of the Pacific white shrimp, Penaeus vannamei , were prepared for examination with the transmission and scanning electron microscopes and with the light microscope. The histology and ultrastructure of this organ is similar to that seen in other Decapoda. At the ultrastructural level, it was observed that B-cells rupture at approximately the level of gap junctions located on the lateral plasma membranes of the cells, and discharge the contents of their large vacuoles into the intercellular space. This efflux of enzymatic material may be the mechanism by which cells are released from the wall of the tubule at the proximal end: the rupture and collapse of a B-cell may be analagous to the removal of the keystone which supports an arch. Deprived of support, and lacking structural adaptations for cohesion (there are no desmosomes or interdigitations in the epithelium) and with the intercellular material digested, the remaining intact cells collapse into the lumen of the tubule. The lysis of individual cells of all types - R-, F-, and B-cells - may contribute to the tubules’ total complement of digestive enzymes.
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                Author and article information

                Journal
                Lipids Health Dis
                Lipids in Health and Disease
                BioMed Central
                1476-511X
                2011
                1 June 2011
                : 10
                : 91
                Affiliations
                [1 ]Laboratoire de biochimie et de génie enzymatique des lipases, ENIS BPW 1173 Université de Sfax-Tunisia
                [2 ]Laboratoire de Neurobiologie Cutanée, CHU Morvan, Université de Brest, 29609 BREST cedex France
                [3 ]Laboratoire d'Histoembryologie, FMS, BPW 3029 Université de Sfax, Tunisia
                Article
                1476-511X-10-91
                10.1186/1476-511X-10-91
                3127788
                21631952
                b502c50c-fdb4-435e-b65a-e63f827b1fef
                Copyright ©2011 Zarai et al; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 25 February 2011
                : 1 June 2011
                Categories
                Research

                Biochemistry
                Biochemistry

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