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<p>Mounting evidence suggests that the kallikrein-related peptidase family is dysregulated in thyroid cancer. However, previous analyses of kallikrein-related peptidase 7 (KLK7) expression patterns have yielded inconsistent results. In this study, KLK7 expression was examined in different histological types of thyroid cancer using immunohistochemistry. We found no detectable KLK7 immunoreactivity in the follicular epithelium of normal thyroid tissue or follicular adenomas. Weak KLK7 expression was observed in papillary (mean H-score 47) and follicular carcinomas (mean H-score 29), with moderate expression in anaplastic cancers (mean H-score 88; <i>P</i> for trend &lt; 0.001). Membranous and cytoplasmic staining was validated using two independent antibodies and small interfering RNA (siRNA) knockdown controls. These observations were consistent with our bioinformatics analysis, which demonstrated that KLK7 was upregulated in less differentiated thyroid cancer and inversely correlated with thyroid differentiation scores. Knockdown of KLK7 expression through transfection with siRNA significantly impaired the viability, clonogenicity, and migratory abilities of thyroid cancer cells. This was accompanied by upregulation of E-cadherin and integrin-β1, along with elevated levels of the KLK7 substrates midkine and tenascin-C. Taken together, our results indicate that KLK7 is overexpressed in thyroid cancer and is linked to disease progression and dedifferentiation, partly by disrupting cell adhesion networks. KLK7 may therefore serve as a biomarker for aggressive thyroid cancer and a potential therapeutic target.</p>

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Oncogenic overexpression of kallikrein-related peptidase 7 is associated with the progression of thyroid cancer

  • 期刊论文

  • 发表日期：

    2026年4月22日

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  • Shun-Yu Chi,
  • Chi-Yu Kuo,
  • Shih-Yuan Huang,
  • Shih-Ping Cheng

摘要

Mounting evidence suggests that the kallikrein-related peptidase family is dysregulated in thyroid cancer. However, previous analyses of kallikrein-related peptidase 7 (KLK7) expression patterns have yielded inconsistent results. In this study, KLK7 expression was examined in different histological types of thyroid cancer using immunohistochemistry. We found no detectable KLK7 immunoreactivity in the follicular epithelium of normal thyroid tissue or follicular adenomas. Weak KLK7 expression was observed in papillary (mean H-score 47) and follicular carcinomas (mean H-score 29), with moderate expression in anaplastic cancers (mean H-score 88; P for trend < 0.001). Membranous and cytoplasmic staining was validated using two independent antibodies and small interfering RNA (siRNA) knockdown controls. These observations were consistent with our bioinformatics analysis, which demonstrated that KLK7 was upregulated in less differentiated thyroid cancer and inversely correlated with thyroid differentiation scores. Knockdown of KLK7 expression through transfection with siRNA significantly impaired the viability, clonogenicity, and migratory abilities of thyroid cancer cells. This was accompanied by upregulation of E-cadherin and integrin-β1, along with elevated levels of the KLK7 substrates midkine and tenascin-C. Taken together, our results indicate that KLK7 is overexpressed in thyroid cancer and is linked to disease progression and dedifferentiation, partly by disrupting cell adhesion networks. KLK7 may therefore serve as a biomarker for aggressive thyroid cancer and a potential therapeutic target.