Abstract
Growth and differentiation factor-5 (GDF-5) has been shown to promote chondrogenesis and osteogenesis during development and tissue repair. A member of the transforming growth factor-beta (TGF-beta) superfamily, it is closely related to the bone morphogenic protein (BMP) subfamily. Like BMP-2, GDF-5 undergoes proteolytic cleavage prior to secretion of the mature peptide from the cell. Although traditionally regarded solely as an extracellular signaling protein, a yeast one-hybrid screen recently identified GDF-5 as a possible DNA-binding protein in chondrocytic cells. Upon further investigation, a putative nuclear localization signal (NLS)—homologous with that recently discovered in BMP-2—was identified. The NLS overlaps the site of proteolytic cleavage, suggesting that an uncleaved variant of GDF-5 may be localized to the nucleus. Immunohistochemical analysis of rat chondrosarcoma (RCS) cells revealed that GDF-5 is, in fact, detectable in the nuclei of some cells. Further characterization of the nuclear variant of GDF-5 is ongoing. The discovery of GDF-5 in the nuclei of RCS cells suggests a novel role for this protein in the direct regulation of transcription during cartilage differentiation. This work was supported by NIH grant #RO1-AR048839.
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