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Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells by Qi Yan; Matt Weaver; Nikole Perdue; E. Helene Sage is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The matricellular glycoprotein, secreted protein acidic and rich in cysteine (SPARC), has complex biological activities and is important for lens epithelial cell function and regulation of cataract formation. To understand how SPARC influences lens epithelial cell activity and homeostasis, we have studied the subcellular distribution of SPARC in murine lens epithelial cells in vitro. We demonstrate that endogenous SPARC is located in the cytoplasm of either quiescent or dividing lens epithelial cells in culture. However, cytoplasmic SPARC was translocated into the nuclei of immortalized lens epithelial cells upon a significant reduction of intracellular SPARC in these cells. Recombinant human (rh) SPARC added to the culture media was quickly and efficiently internalized into the cytosol of SPARC‐null lens epithelial cells. Moreover, cytoplasmic rhSPARC was also translocated into the nucleus after exogenous rhSPARC was removed from the culture media. The translocation of SPARC into the nucleus was therefore triggered by the reduction of SPARC protein normally available to the cells. A mouse SPARC–EGFP chimeric fusion protein (70 kDa) was expressed in lens epithelial cell

Who reads Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells?

Author

Qi Yan; Matt Weaver; Nikole Perdue; E. Helene Sage

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0021-9541)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)