, Volume 212, Issue 3, pp 124-133

Evolutionary conservation and association of SPARC with the basal lamina in Drosophila

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SPARC (secreted protein, acidic, rich in cysteine, also called BM40 and osteonectin) is a multifunctional calcium-binding glycoprotein whose modular organization has been highly conserved between invertebrates and vertebrates, indicating a conservation of function during metazoan evolution. Genome analysis has revealed a single copy of the Drosophila SPARC (dSPARC) gene. As a first step towards investigating the function of SPARC in Drosophila, we examined its spatiotemporal distribution during development. During embryogenesis, dSPARC mRNA transcripts are restricted to mesoderm derivatives, hemocytes, and the fat body. Immunostaining with anti-Drosophila SPARC antibodies indicates that dSPARC secreted by the hemocytes and fat body cells is concentrated in basal laminae surrounding internal organs. During oogenesis, dSPARC transcripts are restricted to the somatic cells of the germarium and follicles. Consistent with embryonic development, the resultant protein is concentrated in basal laminae. Mutations in type IV collagen are associated with a dramatic decrease in dSPARC protein immunostaining in hemocytes. The data suggest that the production and assembly of dSPARC in the basal lamina is dependent on type IV collagen, and raise the possibility that dSPARC and type IV collagen interactions are a prerequisite to the assembly and structural integrity of basal laminae in Drosophila.

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