Abstract
Laminins (αβγ heterotrimers) form the basement membrane. They are important for many cell processes, through adhesion and signaling. There are 17 known laminins with different properties, depending on their subunits. Among the many functions fulfilled by laminins, they actively contribute to all stages of cancer progression, from the onset of the disease to the life-threatening development of metastases. At the cellular level, laminins are crucial in helping cells adhere, migrate, and differentiate.
Following the six hallmarks of cancer (self-sufficiency in growth signals, sustained angiogenesis, evading apoptosis, insensitivity to antigrowth signals, limitless replicative potential, and the ability for tissue invasion and metastasis), this chapter will outline available data involving laminins and their receptors in cell proliferation, death, angiogenesis, and cancer invasion and metastasis.
In light of those evidences, there is no doubt that laminins are able to regulate all stages of cancer progression, either directly or in partnership with receptors and coreceptors. Two laminins (laminin-111 and -332) are particularly active in carcinogenesis, while others seem to be more specific to angiogenesis (laminin-211, -213, and -221) or motility (laminin-511). Furthermore, laminins can activate different receptors, which induce different signaling pathways. Some are redundant to laminin functions (PI-3K, FAK, ERK), and others are only activated in a particular context, such as the laminin-induced relocation to the nucleus of transcription factors.
Overall, this chapter updates our knowledge on the role played by laminins in cancer. By integrating the latest developments in the field, this review helps elucidate how these proteins can be at the center of new diagnostic tools, prognostic power, and therapeutic strategies in the fight against cancer.
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Abbreviations
- 3-D:
-
Three-dimensional
- 67LR:
-
67 kDa laminin receptor
- ADPKD:
-
Autosomal dominant polycystic kidney disease
- AE-2:
-
Alveolar epithelial type II cells
- BM:
-
Basement membrane
- BP:
-
Bullous pemphigoid antigen
- CDKI:
-
Cyclin-dependent kinase inhibitor
- ECM:
-
Extracellular matrix
- EGF:
-
Epidermal growth factor
- EGFR:
-
Epidermal growth factor receptor
- EHS:
-
Engelbreth-Holm-Swarm
- ERK:
-
Extracellular signal-regulated kinase
- FAK:
-
Focal adhesion kinase
- FGF:
-
Fibroblast growth factor
- Grb2:
-
Activation of growth factor receptor-bound protein 2
- HGF:
-
Hepatocyte growth factor
- IGCA:
-
Intestinal-type gastric carcinomas
- IGF:
-
Insulin-like growth factor
- IL:
-
Interleukin
- IRS:
-
Insulin receptors
- JNK:
-
Jun N-terminal kinase
- LCNC:
-
Large-cell neuroendocrine carcinoma
- LG:
-
Laminin G domain-like
- MAPK:
-
Mitogen-activated protein kinase
- MEK:
-
Mitogen-activated protein kinase kinase
- MMP:
-
Matrix metalloproteinase
- MT-MMP:
-
Membrane type matrix metalloproteinase
- mTOR:
-
Mammalian target of rapamycin
- NFκB:
-
Nuclear factor-kappa B
- NGF:
-
Nerve growth factor
- NSCLC:
-
Non-small cell lung carcinomas
- PI-3K:
-
Phosphoinositide 3-kinase
- PKB:
-
Protein kinase B
- PKC:
-
Protein kinase C
- RTK:
-
Receptor tyrosine kinase
- SCC:
-
Squamous cell carcinoma
- SH2:
-
Src homology 2 domain
- STAT:
-
Signal transducers and activators of transcription
- TGF:
-
Transforming growth factor
- tPA:
-
Tissue plasminogen activator
- TUNEL:
-
Terminal transferase dUTP nick end labeling
- VEGF:
-
Vascular endothelial growth factor.
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Jourquin, J., Tripathi, M., Guess, C., Quaranta, V. (2010). Laminins and Cancer Progression. In: Zent, R., Pozzi, A. (eds) Cell-Extracellular Matrix Interactions in Cancer. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0814-8_5
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