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Localization and functional role of a 41 kDa collagenase/gelatinase activity expressed in the sea urchin embryo
Author(s) -
Mayne Janice,
Robinson John J.
Publication year - 2002
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1046/j.1440-169x.2002.00645.x
Subject(s) - blastula , immunogold labelling , gelatinase , cytoplasm , biology , microbiology and biotechnology , extracellular , compartment (ship) , collagenase , organelle , yolk , antiserum , embryo , amyloplast , immunolabeling , biochemistry , sea urchin , ultrastructure , embryogenesis , matrix metalloproteinase , anatomy , gastrulation , antibody , enzyme , chloroplast , immunology , immunohistochemistry , gene , ecology , oceanography , plastid , geology
The egg storage compartment of the sea urchin embryo was investigated for a protein destined for export to the extracellular matrices. Using an antiserum prepared against a 41 kDa collagenase/gelatinase localized to the extraembryonic matrices (the hyaline layer and basal lamina), the egg storage compartment was mapped for this antigen. Indirect immunofluorescence analysis revealed the 41 kDa collagenase/gelatinase in the cortical granules as well as a second compartment which was dispersed throughout the egg cytoplasm. High resolution immunogold labeling defined this cytoplasmic compartment as the yolk granule organelle. Gelatin substrate gel zymography revealed the presence of a 41 kDa gelatin cleavage activity in purified yolk granules. These results suggest a role for yolk granules in regulated protein export and challenge the traditional view of this organelle as a benign storage compartment for nutrients. In additional experiments, embryos grown in the presence of the 41 kDa cleavage activity or the anti‐41 kDa antiserum had severely delayed gut formation and spicule elongation. These results demonstrate a requirement for defined levels of the 41 kDa activity in the extracellular matrices of the developing embryo.