Lectins in Cancer

A special issue of Cancers (ISSN 2072-6694). This special issue belongs to the section "Cancer Metastasis".

Deadline for manuscript submissions: 25 May 2025 | Viewed by 1335

Special Issue Editors


E-Mail Website
Guest Editor
Institute of Medical Biology, Polish Academy of Sciences, Lodowa 106, 93-232 Łódź, Poland
Interests: collectins; ficolins; complement activation

E-Mail Website
Guest Editor
Institute of Medical Biology, Polish Academy of Sciences, Lodowa 106, 93-232 Łódź, Poland
Interests: collectins; ficolins; complement activation

Special Issue Information

Dear Colleagues,

Lectins are produced by bacteria, protists, fungi, plants, invertebrates, and vertebrates. They are classified into a variety of families, depending on host, structure, and function. Their carbohydrate/glycoconjugate recognition is a ubiquitous mode of molecular interactions and signalling. Neoplastic transformation is associated with, among other things, alterations in the cell surface. Due to an abnormal glycosylation pattern, cancer cells may be recognised by endogenous defence lectins, which may contribute to their elimination. On the other hand, they possess a variety of mechanisms of escape from a host’s immunity. Furthermore, cancer cells may employ lectins to facilitate metastatic spread. The specific recognition of cancer antigens by exogenous lectins makes possible their usage in diagnostics and therapy.

This Special Issue will be focused on the multiway associations of lectins with cancer, including primarily the following:

- Lectins in anti-cancer defence.

- Lectins in cancer diagnostics and treatment.

- Involvement of lectins in the epithelial to mesenchymal transition and metastasis.

- Expression of lectins in cancer (cancer cells, the tumour microenvironment, and hosts in general).

- Interactions of lectins with cancer cells.

- Interactions of lectins with oncogenic pathogens.

- Contribution of lectins to chronic inflammation.

- Cancer sugar code.

Prof. Dr. Maciej Cedzyński
Prof. Dr. Anna S. Świerzko
Guest Editors

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Keywords

  • lectin
  • sugar code
  • epithelial to mesenchymal transition (EMT)
  • metastasis
  • complement
  • oncogenic pathogen

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Published Papers (1 paper)

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Review

14 pages, 2302 KiB  
Review
The Role of Pulmonary Collectins, Surfactant Protein A (SP-A) and Surfactant Protein D (SP-D) in Cancer
by Maciej Cedzyński and Anna S. Świerzko
Cancers 2024, 16(18), 3116; https://doi.org/10.3390/cancers16183116 - 10 Sep 2024
Viewed by 966
Abstract
Surfactant proteins A and D (SP-A and SP-D) belong to the collectin subfamily of C-type oligomeric lectins. They are pattern-recognition molecules (PRMs), able to recognise pathogen- or danger-associated molecular patterns (PAMPs, DAMPs) in the presence of Ca2+ cations. That property enables opsonisation [...] Read more.
Surfactant proteins A and D (SP-A and SP-D) belong to the collectin subfamily of C-type oligomeric lectins. They are pattern-recognition molecules (PRMs), able to recognise pathogen- or danger-associated molecular patterns (PAMPs, DAMPs) in the presence of Ca2+ cations. That property enables opsonisation or agglutination of non-self or altered/abnormal self cells and contributes to their clearance. Like other collectins, SP-A and SP-D are characterised by the presence of four distinct domains: a cysteine-rich domain (at the N-terminus), a collagen-like region, an α-helical neck domain and a globular carbohydrate-recognition domain (CRD) (at the C-terminus). Pulmonary surfactant is a lipoprotein complex, preventing alveolar collapse by reducing surface tension at the air–liquid interface. SP-A and SP-D, produced by type II alveolar epithelial cells and Clara cells, are not only pattern-recognition molecules but also contribute to the surfactant structure and homeostasis. Moreover, they are expressed in a variety of extrapulmonary sites where they are involved in local immunity. The term “cancer” includes a variety of diseases: tumours start from uncontrolled growth of abnormal cells in any tissue which may further spread to other sites of the body. Many cancers are incurable, difficult to diagnose and often fatal. This short review summarises anti- and pro-tumorigenic associations of SP-A and SP-D as well as perspectives of their usefulness in cancer diagnosis and therapy. Full article
(This article belongs to the Special Issue Lectins in Cancer)
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