Immunohistochemical localization of rK9, an enzyme of the kallikrein gene                family, in the rat ventral prostate.

Berg, Torill; Schøyen, H

doi:10.1177/43.1.7822766

Cited by 3 publications

(1 citation statement)

References 11 publications

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“…Comparison of the amino acid sequences of p18 and the known sequences in the protein database demonstrated that the first 18-amino-acid sequence of p18 and the sequence of rat glandular kallikrein 9 (rKLK9) were identical (100% identity). Rat glandular kallikrein 9 (rKLK9) is one of the proteins encoded by a group of genes showing a high degree (74-86%) of sequence similarity, which is known as the kallikrein gene family, since one of the genes encodes tissue kallikrein (rK1) [21].…”

Section: Discussionmentioning

confidence: 99%

Expression of a kallikrein-like protein in prostatic intraepithelial neoplasia in ventral prostate of the noble rat

et al. 2000

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BACKGROUND In an effort to identify biomarker(s) for prostatic cancer (PCa), we analyzed the changes of secretory proteins in the ventral prostate (VP) of Noble rats at early stages of carcinogenesis. METHODS Ventral prostates were removed from both control (n = 36) and experimental (n = 88) rats implanted with a known ratio of testosterone (T) and 17β‐estradiol (E2). Tissue sections were stained by hematoxylin and eosin (H&E) for pathological screening, and secretions were collected for SDS‐PAGE analysis followed by N‐terminal microsequencing, antiserum production, Western blot, and immunohistochemical study. RESULTS Pathologically, low‐grade prostatic intraepithelial neoplasia (LGPIN) and high‐grade PIN (HGPIN) were observed in ducts or alveoli after 3 and 5 months of T + E2 treatment, respectively. The results of SDS‐PAGE showed an elevated expression of 18‐kDa protein (p18) in secretions of VP with HGPIN or cancerous lesions. Analysis of p18 by N‐terminal sequencing showed a high score of homology to rat glandular kallikrein. To characterize the expression pattern of the protein in tissue samples, an antiserum was raised against the N‐terminus of the p18. The monospecificity of the antiserum against p18 was confirmed by Western blot analysis. Immunohistochemical study showed that in ducts or alveoli of normal and LGPIN samples, a mild positive staining for p18 was observed in secretions. However, the reactivity was intense not only in luminal secretions but also in some luminal secretory cells in HGPIN and cancer cells as well. CONCLUSIONS The high expression of p18 in connection with neoplastic transformation of cells strongly suggests that the potential application of this protein as a marker for early detection of PCa should be further investigated. Prostate 42:8–17, 2000. © 2000 Wiley‐Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Expression of a kallikrein-like protein in prostatic intraepithelial neoplasia in ventral prostate of the noble rat

et al. 2000

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Purification and characterization of active recombinant rat kallikrein rK9

Zani

Brillard-Bourdet

Lazure

et al. 2001

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Kallikreins on Steroids: Structure, Function, and Hormonal Regulation of Prostate-Specific Antigen and the Extended Kallikrein Locus

2010

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The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the current serum biomarker for prostate cancer. The kallikrein locus is also notable because it is extraordinarily responsive to steroids and other hormones. Indeed, at least 14 functional hormone response elements have been identified in the kallikrein locus. A more comprehensive understanding of the transcriptional regulation of kallikreins may help the field make more informed hypotheses about the physiological functions of kallikreins and their effectiveness as biomarkers. In this review, we describe the organization of the kallikrein locus and the structure of kallikrein genes and proteins. We also focus on the transcriptional regulation of kallikreins by androgens, progestins, glucocorticoids, mineralocorticoids, estrogens, and other hormones in animal models and human prostate, breast, and reproductive tract tissues. The interaction of the androgen receptor with androgen response elements in the promoter and enhancer of KLK2 and KLK3 is also summarized in detail. There is evidence that all kallikreins are regulated by multiple nuclear receptors. Yet, apart from KLK2 and KLK3, it is not clear whether all kallikreins are direct transcriptional targets. Therefore, we argue that gaining more detailed information about the mechanisms that regulate kallikrein expression should be a priority of future studies and that the kallikrein locus will continue to be an important model in the era of genome-wide analyses.

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Immunohistochemical localization of rK9, an enzyme of the kallikrein gene family, in the rat ventral prostate.

Cited by 3 publications

References 11 publications

Expression of a kallikrein-like protein in prostatic intraepithelial neoplasia in ventral prostate of the noble rat

Expression of a kallikrein-like protein in prostatic intraepithelial neoplasia in ventral prostate of the noble rat

Purification and characterization of active recombinant rat kallikrein rK9

Kallikreins on Steroids: Structure, Function, and Hormonal Regulation of Prostate-Specific Antigen and the Extended Kallikrein Locus

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