beta-Glucuronidase and hexosaminidase are marker enzymes for different compartments of the endo-lysosomal system in mussel digestive cells

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dc.contributor.author Izagirre, U.
dc.contributor.author Angulo, E.
dc.contributor.author ap Gwynn, Iolo A.
dc.contributor.author Wade, Stephen
dc.contributor.author Marigomez, I.
dc.date.accessioned 2010-03-16T09:15:23Z
dc.date.available 2010-03-16T09:15:23Z
dc.date.issued 2009-02-01
dc.identifier.citation Izagirre , U , Angulo , E , ap Gwynn , I A , Wade , S & Marigomez , I 2009 , ' beta-Glucuronidase and hexosaminidase are marker enzymes for different compartments of the endo-lysosomal system in mussel digestive cells ' Cell and Tissue Research , vol 335 , no. 2 , pp. 441-454 . en
dc.identifier.issn 1432-0878
dc.identifier.other PURE: 148768
dc.identifier.other dspace: 2160/4437
dc.identifier.uri http://hdl.handle.net/2160/4437
dc.description Izagirre, U., Angulo, E., Wade, S., ap Gwynn, I., Marigomez, I. (2009). beta-Glucuronidase and hexosaminidase are marker enzymes for different compartments of the endo-lysosomal system in mussel digestive cells. Cell and Tissue Research, 335, (2), 441-454. IMPF: 02.31 en
dc.description.abstract In environmental toxicology, the most commonly used techniques used to visualise lysosomes in order to determine their responses to pollutants (LSC test: lysosomal structural changes test; LMS test: lysosomal membrane stability test) are based on the histochemical application of lysosomal marker enzymes. In mussel digestive cells, the marker enzymes used are β-glucuronidase (β-Gus) and hexosaminidase (Hex). The present work has been aimed at determining the distribution of these lysosomal marker enzymes in the various compartments of the endo-lysosomal system (ELS) of mussel digestive cells and at exploring whether intercellular transfer of lysosomal enzymes occurs between digestive and basophilic cells. Immunogold cytochemistry has allowed us to conclude that β-Gus is present in every compartment of the digestive cell ELS, whereas Hex is not so widely distributed. Moreover, Hex is intimately linked to the lysosomal membrane, whereas β-Gus appears to be not necessarily membrane-bound. Therefore, two populations of heterolysosomes with different enzyme load and membrane stability have been distinguished in the digestive cell. In addition, heterolysosomes of different electron density have been commonly observed merging together by contact; we suggest that some might act as storage granules for lysosomal enzymes. On the other hand, β-Gus seems to be released to the digestive alveolar lumen in secretory lysosomes produced by basophilic cells and endocytosed by digestive cells. Regarding the implications of the present study on the interpretation of lysosomal biomarkers, we conclude that β-Gus, but not Hex, histochemistry provides an appropriate marker for the LSC test and that, although both lysosomal marker enzymes can be employed in the LMS test, different values would be obtained depending on the marker enzyme employed. en
dc.format.extent 14 en
dc.language.iso eng
dc.relation.ispartof Cell and Tissue Research en
dc.title beta-Glucuronidase and hexosaminidase are marker enzymes for different compartments of the endo-lysosomal system in mussel digestive cells en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1007/s00441-008-0693-6
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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