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Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
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Manal Gabril
Published/Copyright:
February 3, 2010
Abstract
Kallikrein-related peptidases (KLKs) have been shown to be differentially expressed in various malignancies and shown to be useful tumor markers. Previous immunohistochemistry (IHC) analysis demonstrated that KLKs 5, 6, 10, and 11 have a potential prognostic significance in renal cell carcinoma (RCC). To further explore the significance of KLKs, we examined KLKs 1, 6, 7, and 15 in different subtypes of renal tumors. KLK1 has stronger expression in high grade compared to low grade clear cell RCC. However, KLK6 and KLK7 show strong expression in low grade in contrast to high grade clear cell RCC. Furthermore, the expression of KLK7 can distinguish between oncocytoma and chromophobe RCC. Oncocytoma showed diffuse, strong granular cytoplasmic staining, but chromophobe RCC showed focal weak homogeneous cytoplasmic stain. The pattern of staining of different KLKs can also be helpful in differentiating some of the subtypes of renal tumors. Our results show the potential ability of KLKs to serve as diagnostic markers and expand previous data about the prognostic significance of KLKs in kidney cancer. In addition, our study is the first to show the ability of KLK staining to distinguish various types of kidney cancers when morphology is similar.
Keywords: immunohistochemistry; kallikrein; kallikrein-related peptidases; kidney; kidney cancer; renal cell carcinoma (RCC); tumor markers
Received: 2009-10-16
Accepted: 2009-12-3
Published Online: 2010-02-03
Published in Print: 2010-04-01
©2010 by Walter de Gruyter Berlin New York
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- The 3rd International Symposium on Kallikreins and Kallikrein-Related Peptidases
- HIGHLIGHT: 3RD INTERNATIONAL SYMPOSIUM ON KALLIKREINS AND KALLIKREIN-RELATED PEPTIDASES
- Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
- Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
- Kallikrein-related peptidases: bridges between immune functions and extracellular matrix degradation
- Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer
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- Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia
- Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
- Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid
- Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer
- Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
- Dysregulation of kallikrein-related peptidases in renal cell carcinoma: potential targets of miRNAs
- Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
- Increased blood pressure and water intake in transgenic mice expressing rat tonin in the brain
- A structural network associated with the kallikrein-kinin and renin-angiotensin systems
- Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
- Expression of PSA-RP2, an alternatively spliced variant from the PSA gene, is increased in prostate cancer tissues but the protein is not secreted from prostate cancer cells
- KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
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Keywords for this article
immunohistochemistry;
kallikrein;
kallikrein-related peptidases;
kidney;
kidney cancer;
renal cell carcinoma (RCC);
tumor markers
Articles in the same Issue
- Guest Editorial
- The 3rd International Symposium on Kallikreins and Kallikrein-Related Peptidases
- HIGHLIGHT: 3RD INTERNATIONAL SYMPOSIUM ON KALLIKREINS AND KALLIKREIN-RELATED PEPTIDASES
- Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
- Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
- Kallikrein-related peptidases: bridges between immune functions and extracellular matrix degradation
- Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer
- Tissue kallikrein in cardiovascular, cerebrovascular and renal diseases and skin wound healing
- Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia
- Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
- Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid
- Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer
- Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
- Dysregulation of kallikrein-related peptidases in renal cell carcinoma: potential targets of miRNAs
- Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
- Increased blood pressure and water intake in transgenic mice expressing rat tonin in the brain
- A structural network associated with the kallikrein-kinin and renin-angiotensin systems
- Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
- Expression of PSA-RP2, an alternatively spliced variant from the PSA gene, is increased in prostate cancer tissues but the protein is not secreted from prostate cancer cells
- KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
- Identification of IGFBP-3 fragments generated by KLK2 and prevention of fragmentation by KLK2-inhibiting peptides
