Post-transcriptional regulation of human cathepsin L expression
-
Shivani Mittal
Abstract
The expression of cathepsin L, a lysosomal protease, is known to be elevated in cancer and other pathologies. Multiple splice variants of human cathepsin L with variable 5′UTRs exist, which encode for the same protein. Previously we have observed that variant hCATL A (bearing the longest 5′UTR) was translated in vitro with significantly lower efficiency than variant hCATL AIII (bearing the shortest 5′UTR). Contrary to these findings, results of the present study reveal that in cancer cells, hCATL A mRNA exhibits higher translatability in spite of having lower stability than AIII. This is the first report demonstrating a highly contrasting trend in translation efficiencies of hCATL variants in rabbit reticulocytes and live cells. Expression from chimeric mRNAs containing 5′UTRs of A or AIII upstream to luciferase reporter cDNA established the A UTR to be the sole determinant for this effect. Transient transfections of bicistronic plasmids and mRNAs confirmed the presence of a functional Internal Ribosome Entry Site in this UTR. Our data suggest that differential stability and translation initiation modes mediated by the 5′UTRs of human cathepsin L variants are involved in regulating its expression.
©2011 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Review
- Recent insights into regulation of transcription by RNA polymerase III and the cellular functions of its transcripts
- Genes and Nucleic Acids
- Post-transcriptional regulation of human cathepsin L expression
- Protein Structure and Function
- In vitro conversion and seeded fibrillization of posttranslationally modified prion protein
- Synthesis of recombinant high density lipoprotein with apolipoprotein A-I and apolipoprotein A-V
- Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1
- Molecular Medicine
- Inhibition of AP-1 suppresses cervical cancer cell proliferation and is associated with p21 expression
- STAT3 controls matrix metalloproteinase-1 expression in colon carcinoma cells by both direct and AP-1-mediated interaction with the MMP-1 promoter
- Cell Biology and Signaling
- TGFβ1 suppresses vascular smooth muscle cell motility by expression of N-cadherin
- Renal pro-apoptotic proteins are reduced by growth hormone resistance but not by visceral fat removal
- Proteolysis
- Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence
Articles in the same Issue
- Review
- Recent insights into regulation of transcription by RNA polymerase III and the cellular functions of its transcripts
- Genes and Nucleic Acids
- Post-transcriptional regulation of human cathepsin L expression
- Protein Structure and Function
- In vitro conversion and seeded fibrillization of posttranslationally modified prion protein
- Synthesis of recombinant high density lipoprotein with apolipoprotein A-I and apolipoprotein A-V
- Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1
- Molecular Medicine
- Inhibition of AP-1 suppresses cervical cancer cell proliferation and is associated with p21 expression
- STAT3 controls matrix metalloproteinase-1 expression in colon carcinoma cells by both direct and AP-1-mediated interaction with the MMP-1 promoter
- Cell Biology and Signaling
- TGFβ1 suppresses vascular smooth muscle cell motility by expression of N-cadherin
- Renal pro-apoptotic proteins are reduced by growth hormone resistance but not by visceral fat removal
- Proteolysis
- Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence
