CD147-Mediated Mechanisms in Cancer Progression

CD147, also known as EMMPRIN or basigin, is a highly glycosylated immunoglobulin superfamily member frequently overexpressed in malignant cells. It orchestrates tumour invasion and metastasis by inducing matrix metalloproteinases (MMPs) that degrade extracellular matrix barriers. Through homophilic and heterophilic interactions with integrins, monocarboxylate transporters and CD44, CD147 modulates cell adhesion, motility and metabolic adaptation via lactate export. Its N-glycosylation status governs cell-surface trafficking and multimerisation, enabling assembly of signalling complexes that activate ERK, STAT3 and focal adhesion kinase pathways. Under hypoxic conditions, CD147 enhances angiogenesis by upregulating vascular endothelial growth factor and facilitating MMP-mediated matrix remodelling. Additionally, CD147 contributes to chemoresistance through interactions with drug transporters and promotion of prosurvival signalling. By integrating microenvironmental cues to drive tumour growth, invasiveness and treatment response, CD147 has emerged as both a prognostic indicator and a strategic target for novel anticancer interventions.

Research from Nature Portfolio

A comprehensive meta-analysis of over fifty studies has confirmed that elevated CD147 expression is consistently linked with poorer overall survival, reduced progression-free survival and increased risk of metastasis across multiple cancer types. Furthermore, high CD147 levels predict resistance to chemotherapy and radiotherapy, underscoring its role as a central mediator of tumour aggressiveness and treatment failure. This synthesis of diverse datasets strengthens the rationale for developing CD147-targeted therapies and incorporating CD147 assessment into clinical prognostication.

CD147-Mediated Mechanisms in Cancer Progression publication trend

The graph below shows the total number of articles in cd147-mediated mechanisms in cancer progression across all publications each year (not limited to Nature Index journals).

Technical terms

CD147 (EMMPRIN): A transmembrane glycoprotein that induces proteases and assembles signalling complexes to promote tumour progression.

Matrix metalloproteinases (MMPs): Zinc-dependent enzymes that degrade extracellular matrix components, facilitating cancer cell invasion.

Antibody-dependent cellular cytotoxicity (ADCC): Immune mechanism whereby antibody-coated target cells are recognised and killed by effector cells.

Hypoxia-responsive delivery: Drug-activation strategy triggered by low-oxygen conditions characteristic of solid tumours.

Rap1 signalling pathway: A small GTPase cascade regulating cell adhesion, migration and survival in response to extracellular cues.

References

1. Hypoxia‐activated ADCC‐enhanced humanized anti‐CD147 antibody for liver cancer imaging and targeted therapy with improved selectivity. MedComm (2024).
2. Role of CD147 in the development and diagnosis of hepatocellular carcinoma. Frontiers in Immunology (2023).
3. Silencing of CD147 inhibits cell proliferation, migration, invasion, lipid metabolism dysregulation and promotes apoptosis in lung adenocarcinoma via blocking the Rap1 signaling pathway. Respiratory Research (2023).
4. How, with whom and when: an overview of CD147-mediated regulatory networks influencing matrix metalloproteinase activity. Bioscience Reports (2016).
5. CD147/EMMPRIN overexpression and prognosis in cancer: A systematic review and meta-analysis. Scientific Reports (2016).
6. CD147 Is a Promising Target of Tumor Progression and a Prognostic Biomarker. Cancers (2019).
7. CD147, CD44, and the Epidermal Growth Factor Receptor (EGFR) Signaling Pathway Cooperate to Regulate Breast Epithelial Cell Invasiveness*. Journal of Biological Chemistry (2013).
8. Importance of N-Glycosylation on CD147 for Its Biological Functions. International Journal of Molecular Sciences (2014).
9. Extracellular Membrane-proximal Domain of HAb18G/CD147 Binds to Metal Ion-dependent Adhesion Site (MIDAS) Motif of Integrin β1 to Modulate Malignant Properties of Hepatoma Cells*. Journal of Biological Chemistry (2011).