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Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer

  • Lina Seiz , Matthias Kotzsch , Nicolai I. Grebenchtchikov , Anneke J. Geurts-Moespot , Susanne Fuessel , Peter Goettig , Apostolos Gkazepis , Manfred P. Wirth , Manfred Schmitt , Arndt Lossnitzer , Fred C.G.J. Sweep and Viktor Magdolen
Published/Copyright: February 24, 2010
Biological Chemistry
From the journal Volume 391 Issue 4

Abstract

KLK4 is a member of the human kallikrein-related peptidase family of (chymo)trypsin-like serine proteases. The aim of the present study was to generate polyclonal antibodies (pAb) directed against KLK4 for the analysis of KLK4 by immunohistochemistry in human tissues. Recombinantly expressed human mature KLK4 was used for immunization of chickens. pAb 617A is an affinity-purified monospecific pAb fraction reacting with a linear epitope within a flexible surface-exposed loop of KLK4. pAb 617C is the KLK-directed pAb fraction completely depleted from pAb 617A. In healthy adult tissues, KLK4 was immunodetected by both antibody fractions in kidney, liver, and prostate, but not in other organs such as colon and lung. To evaluate protein expression of KLK4 in prostate cancer, samples of tumor tissue plus corresponding tumor-free areas of 44 prostate cancer patients, represented on a tissue microarray, were investigated. Distinct KLK4 immunostaining was observed with both antibodies in cancerous glandular epithelial cells, but not in surrounding stromal cells. KLK4 expression was lower in stage pT3+4 than in pT1+2 tumors, which was highly significant when employing pAb 617A. Thus, our results indicate that KLK4, which is expressed in the healthy prostate, is upregulated in early-stage but not late-stage prostate cancer.


Corresponding author

Received: 2009-10-15
Accepted: 2009-11-25
Published Online: 2010-02-24
Published in Print: 2010-04-01

©2010 by Walter de Gruyter Berlin New York

Articles in the same Issue

  1. Guest Editorial
  2. The 3rd International Symposium on Kallikreins and Kallikrein-Related Peptidases
  3. HIGHLIGHT: 3RD INTERNATIONAL SYMPOSIUM ON KALLIKREINS AND KALLIKREIN-RELATED PEPTIDASES
  4. Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
  5. Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
  6. Kallikrein-related peptidases: bridges between immune functions and extracellular matrix degradation
  7. Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer
  8. Tissue kallikrein in cardiovascular, cerebrovascular and renal diseases and skin wound healing
  9. Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia
  10. Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
  11. Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid
  12. Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer
  13. Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
  14. Dysregulation of kallikrein-related peptidases in renal cell carcinoma: potential targets of miRNAs
  15. Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
  16. Increased blood pressure and water intake in transgenic mice expressing rat tonin in the brain
  17. A structural network associated with the kallikrein-kinin and renin-angiotensin systems
  18. 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
  19. 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
  20. KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
  21. Identification of IGFBP-3 fragments generated by KLK2 and prevention of fragmentation by KLK2-inhibiting peptides
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