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Truncated Human Cathepsin L, Encoded by a Novel Splice Variant, Exhibits Altered Subcellular Localization and Cytotoxicity

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Abstract:

Cathepsin L (ctsl), a lysosomal cyteine protease over expressed and secreted by cancer cells, has been implicated in a number of physiological and pathological processes including tumor cell proliferation and metastasis. In the present study we demonstrate that an unknown mRNA of human origin (Gene Bank accession number AF 217997) is a splice variant of human cathepsin L mRNA (hCATL A IV) and encodes a truncated form of cathepsin L (Δctsl) containing only 151 C-terminal amino acids. This isoform is cytotoxic to the mammalian cells. Transient transfection studies revealed that unlike ctsl, upon over expression in eukaryotic cells Δctsl is not secreted in to the media. Immunogold electron microscopy revealed its localization to nuclear, perinuclear and cytosolic regions. In view of its cytotoxic property, targeted expression of Δctsl in tumor cells may prove useful in the management of cancer.





Keywords: Splice variant; cancer; immunogold electron microscopy; transfection

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986610790225932

Publication date: February 1, 2010

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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