Expression profiling of dipeptidyl peptidase 8 and 9 in breast and ovarian carcinoma cell lines.
Proteases, particularly serine proteases like dipeptidyl peptidase 4 (DP4)             and fibroblast activation protein (FAP), play an important role in cancer invasion             and angiogenesis. Aberrant expression of DP4 and FAP is associated with numerous             cancers, including breast and epithelial ovarian carcinoma. We investigated the             mRNA levels, protein expression and enzyme activity of the structural homologs             DP8 and DP9, in addition to DP4 and FAP, in three breast carcinoma (MDA-MB-231,             MDA-MB-453, MCF-7), three epithelial ovarian carcinoma (EOC) (OVCA-432, OVCA-429,             SKOV3), 293T and HeLa cell lines. In addition, DP2 and prolyl endopeptidase (PEP)             mRNA and enzyme levels were measured and compared in each cell line. Ubiquitous             but differential expression of DP8 and DP9 mRNA and protein was observed across             all cell lines. Relative to EOC, DP8 protein was lower in the breast carcinoma             cell lines (p=0.057), suggesting that DP8 may play differing roles in different             cancer cell types. A strong, negative, non-reciprocal relationship was identified             between DP9 protein and DP4 mRNA (r=-0.903, p=0.002) and protein (r=-0.810, p=0.015).             This suggests that DP4 expression plays an important role in the post-transcriptional             regulation of DP9 in breast and ovarian cancer cell lines. Overall, this study             suggests a potential role for DP8 and DP9 in breast and ovarian cancer and further             investigations in this area are required.
School of Biological Sciences, Flinders University, Adelaide, South Australia, Australia. claire.wilson2@health.sa.gov.au
Claire H
CH
Wilson
Catherine A
CA
Abbott
D001943:Breast Neoplasms / Q000201:enzymology* / Q000235:genetics; D045744:Cell Line, Tumor; D004150:Dipeptidases / Q000096:biosynthesis / Q000235:genetics*; D018819:Dipeptidyl Peptidase 4 / Q000096:biosynthesis / Q000235:genetics; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000096:biosynthesis / Q000235:genetics*; D010450:Endopeptidases; D005260:Female; D018093:Gelatinases / Q000096:biosynthesis / Q000235:genetics; D020869:Gene Expression Profiling; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics; D010051:Ovarian Neoplasms / Q000201:enzymology* / Q000235:genetics; D034622:RNA Interference; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D034741:RNA, Small Interfering; D012697:Serine Endopeptidases / Q000096:biosynthesis / Q000235:genetics; D000099167:Fibroblast Activation Protein Alpha
D004150:Dipeptidases; D018819:Dipeptidyl Peptidase 4; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D010450:Endopeptidases; D018093:Gelatinases; D008565:Membrane Proteins; D012333:RNA, Messenger; D034741:RNA, Small Interfering; D012697:Serine Endopeptidases; D000099167:Fibroblast Activation Protein Alpha; C471241:DPP9 protein, human; C042807:DPP4 protein, human; C487997:DPP8 protein, human