Tetranectin: Molecular Mechanisms, Biological Functions and Clinical Implications

Tetranectin (TN), also known as C-type lectin domain family 3 member B (CLEC3B), is a secreted glycoprotein originally identified through its high-affinity interaction with plasminogen. Although initially linked to fibrinolysis, TN is now increasingly recognized as an extracellular regulator associated with matrix remodeling, bone development, tissue repair, and disease-related proteolytic processes. Dysregulated TN expression has been reported in a broad range of pathological conditions, including cancer, cardiovascular disease, inflammatory disorders, and neurodegenerative states. In this review, we summarize current knowledge of TN with emphasis on its molecular architecture, ligand-binding properties, trimeric organization, and regulatory mechanisms. We further discuss its context-dependent biological functions, with particular attention to how tissue-specific and compartment-specific TN patterns may influence disease progression and clinical interpretation, especially in oncology. In addition, we evaluate the evidence supporting TN as a diagnostic and prognostic biomarker and consider its emerging therapeutic relevance. Finally, we outline the major challenges that currently limit clinical translation and highlight key directions for future investigation.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2026-07-28
DOI
https://doi.org/10.3390/ijms27156732
Primary Topic
Protease and Inhibitor Mechanisms
Type
article
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article

Tetranectin: Molecular Mechanisms, Biological Functions and Clinical Implications

Sana Iram, K. S. Kim, Amar Akash, Jihoe Kim et al.
International Journal of Molecular Sciences
Protease and Inhibitor Mechanisms
article

Tetranectin: Molecular Mechanisms, Biological Functions and Clinical Implications

Sana Iram, K. S. Kim, Amar Akash, Jihoe Kim, Sarfraz Ahmed
article en

Abstract

Tetranectin (TN), also known as C-type lectin domain family 3 member B (CLEC3B), is a secreted glycoprotein originally identified through its high-affinity interaction with plasminogen. Although initially linked to fibrinolysis, TN is now increasingly recognized as an extracellular regulator associated with matrix remodeling, bone development, tissue repair, and disease-related proteolytic processes. Dysregulated TN expression has been reported in a broad range of pathological conditions, including cancer, cardiovascular disease, inflammatory disorders, and neurodegenerative states. In this review, we summarize current knowledge of TN with emphasis on its molecular architecture, ligand-binding properties, trimeric organization, and regulatory mechanisms. We further discuss its context-dependent biological functions, with particular attention to how tissue-specific and compartment-specific TN patterns may influence disease progression and clinical interpretation, especially in oncology. In addition, we evaluate the evidence supporting TN as a diagnostic and prognostic biomarker and consider its emerging therapeutic relevance. Finally, we outline the major challenges that currently limit clinical translation and highlight key directions for future investigation.

International Journal of Molecular SciencesVol. 27(15)
Yeungnam University (KR)
Good health and well-being
Openalex Percentile: Top 11%
Protease and Inhibitor Mechanisms
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