Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions
<p>Abstract</p> <p>Background</p> <p>Kallikrein-related peptidase 5 (KLK5) is a secreted trypsin-like protease of the KLK family, encoded by the <it>KLK5 </it>gene. KLK5 has been found to cleave various extracellular matrix components, as well as to activate...
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BMC
2011-05-01
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Series: | Clinical Proteomics |
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Online Access: | http://www.clinicalproteomicsjournal.com/content/8/1/5 |
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author | Avgeris Margaritis Papachristopoulou Georgia Polychronis Athanasios Scorilas Andreas |
author_facet | Avgeris Margaritis Papachristopoulou Georgia Polychronis Athanasios Scorilas Andreas |
author_sort | Avgeris Margaritis |
collection | DOAJ |
description | <p>Abstract</p> <p>Background</p> <p>Kallikrein-related peptidase 5 (KLK5) is a secreted trypsin-like protease of the KLK family, encoded by the <it>KLK5 </it>gene. KLK5 has been found to cleave various extracellular matrix components, as well as to activate several other KLK proteases, triggering the stimulation of tissue microenvironment proteolytic cascades.</p> <p>Material and Methods</p> <p><it>KLK5 </it>expression levels were quantified in 102 cancerous and benign breast tissue specimens, obtained by randomly chosen patients, using RT-qPCR assay. Subsequently, advanced biostatistics were applied in order to analyze the <it>KLK5 </it>expression profile in the two patients' cohorts and also to evaluate its clinical significance for the discrimination of breast tumors.</p> <p>Results</p> <p>A statistically significant (p < 0.001) down-regulation of the <it>KLK5 </it>expression levels were observed in the malignant specimens compared to the benign ones. Logistic regression and ROC curve analysis revealed the significant (p < 0.001) and the independent (p < 0.001) value of the <it>KLK5 </it>expression quantification, for the discrimination of the malignant from the benign mammary gland biopsies. Moreover, <it>KLK5 </it>expression levels correlate with the pre-menopausal status (p < 0.005) as well as the ER-negative staining (p = 0.028) of women with breast cancer.</p> <p>Conclusions</p> <p>The quantification of <it>KLK5 </it>expression in breast tissue biopsies may be considered as a novel and independent biomarker for the differential diagnosis between malignant and benign tumors of the mammary gland.</p> |
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spelling | doaj.art-42d994b63b3441f58cb69ed35861b95f2022-12-22T01:07:56ZengBMCClinical Proteomics1559-02752011-05-0181510.1186/1559-0275-8-5Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesionsAvgeris MargaritisPapachristopoulou GeorgiaPolychronis AthanasiosScorilas Andreas<p>Abstract</p> <p>Background</p> <p>Kallikrein-related peptidase 5 (KLK5) is a secreted trypsin-like protease of the KLK family, encoded by the <it>KLK5 </it>gene. KLK5 has been found to cleave various extracellular matrix components, as well as to activate several other KLK proteases, triggering the stimulation of tissue microenvironment proteolytic cascades.</p> <p>Material and Methods</p> <p><it>KLK5 </it>expression levels were quantified in 102 cancerous and benign breast tissue specimens, obtained by randomly chosen patients, using RT-qPCR assay. Subsequently, advanced biostatistics were applied in order to analyze the <it>KLK5 </it>expression profile in the two patients' cohorts and also to evaluate its clinical significance for the discrimination of breast tumors.</p> <p>Results</p> <p>A statistically significant (p < 0.001) down-regulation of the <it>KLK5 </it>expression levels were observed in the malignant specimens compared to the benign ones. Logistic regression and ROC curve analysis revealed the significant (p < 0.001) and the independent (p < 0.001) value of the <it>KLK5 </it>expression quantification, for the discrimination of the malignant from the benign mammary gland biopsies. Moreover, <it>KLK5 </it>expression levels correlate with the pre-menopausal status (p < 0.005) as well as the ER-negative staining (p = 0.028) of women with breast cancer.</p> <p>Conclusions</p> <p>The quantification of <it>KLK5 </it>expression in breast tissue biopsies may be considered as a novel and independent biomarker for the differential diagnosis between malignant and benign tumors of the mammary gland.</p>http://www.clinicalproteomicsjournal.com/content/8/1/5KLK5Breast CancerCancer BiomarkersTumor MarkersKLKsKallikreinsSerine ProteasesProteolysis |
spellingShingle | Avgeris Margaritis Papachristopoulou Georgia Polychronis Athanasios Scorilas Andreas Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions Clinical Proteomics KLK5 Breast Cancer Cancer Biomarkers Tumor Markers KLKs Kallikreins Serine Proteases Proteolysis |
title | Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions |
title_full | Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions |
title_fullStr | Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions |
title_full_unstemmed | Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions |
title_short | Down-regulation of kallikrein-related peptidase 5 (<it>KLK5</it>) expression in breast cancer patients: a biomarker for the differential diagnosis of breast lesions |
title_sort | down regulation of kallikrein related peptidase 5 it klk5 it expression in breast cancer patients a biomarker for the differential diagnosis of breast lesions |
topic | KLK5 Breast Cancer Cancer Biomarkers Tumor Markers KLKs Kallikreins Serine Proteases Proteolysis |
url | http://www.clinicalproteomicsjournal.com/content/8/1/5 |
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