» Articles » PMID: 32184815

S100A12 in Digestive Diseases and Health: A Scoping Review

Overview
Publisher Wiley
Specialty Gastroenterology
Date 2020 Mar 19
PMID 32184815
Citations 23
Authors
Affiliations
Soon will be listed here.
Abstract

Calgranulin proteins are an important class of molecules involved in innate immunity. These members of the S100 class of the EF-hand family of calcium-binding proteins have numerous cellular and antimicrobial functions. One protein in particular, S100A12 (also called EN-RAGE or calgranulin C), is highly abundant in neutrophils during acute inflammation and has been implicated in immune regulation. Structure-function analyses reveal that S100A12 has the capacity to bind calcium, zinc, and copper, processes that contribute to nutritional immunity against invading microbial pathogens. S100A12 is a ligand for the receptor for advanced glycation end products (RAGE), toll-like receptor 4 (TLR4), and CD36, which promote cellular and immunological pathways to alter inflammation. We conducted a scoping review of the existing literature to define what is known about the association of S100A12 with digestive disease and health. Results suggest that S100A12 is implicated in gastroenteritis, necrotizing enterocolitis, gastritis, gastric cancer, Crohn's disease, irritable bowel syndrome, inflammatory bowel disease, and digestive tract cancers. Together, these results reveal S100A12 is an important molecule broadly associated with the pathogenesis of digestive diseases.

Citing Articles

Screening for transcriptomic associations with Swine Inflammation and Necrosis Syndrome.

Gerhards K, Becker S, Kuehling J, Lechner M, Willems H, Ringseis R BMC Vet Res. 2025; 21(1):26.

PMID: 39825377 PMC: 11740493. DOI: 10.1186/s12917-024-04469-y.


Role of the Receptor for Advanced Glycation End Products (RAGE) and Its Ligands in Inflammatory Responses.

Cross K, Vetter S, Alam Y, Hasan M, Nath A, Leclerc E Biomolecules. 2025; 14(12.

PMID: 39766257 PMC: 11673996. DOI: 10.3390/biom14121550.


Orosomucoid 1 interacts with S100A12 and activates ERK signalling to expedite the advancement of bladder cancer.

Liu Z, Pu X Cell Adh Migr. 2024; 19(1):1-11.

PMID: 39644201 PMC: 11633163. DOI: 10.1080/19336918.2024.2434209.


Changes in Immunoglobulins G and A in the Saliva and Serum of Horses with Equine Gastric Ulcer Syndrome (EGUS) and Their Relationship with Other Immune and Redox Status Biomarkers.

Botia M, Martin-Cuervo M, Martinez-Subiela S, Ceron J, Ayala I, Hansen S Biology (Basel). 2024; 13(11).

PMID: 39596846 PMC: 11591608. DOI: 10.3390/biology13110891.


Advanced glycation end products in gastric cancer: A promising future.

Wang M, Fang H, Xie C World J Clin Oncol. 2024; 15(9):1117-1121.

PMID: 39351465 PMC: 11438846. DOI: 10.5306/wjco.v15.i9.1117.


References
1.
Loes A, Bridgham J, Harms M . Coevolution of the Toll-Like Receptor 4 Complex with Calgranulins and Lipopolysaccharide. Front Immunol. 2018; 9:304. PMC: 5826337. DOI: 10.3389/fimmu.2018.00304. View

2.
Heizmann C, Fritz G, Schafer B . S100 proteins: structure, functions and pathology. Front Biosci. 2002; 7:d1356-68. DOI: 10.2741/A846. View

3.
Moroz O, Blagova E, Wilkinson A, Wilson K, Bronstein I . The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation. J Mol Biol. 2009; 391(3):536-51. DOI: 10.1016/j.jmb.2009.06.004. View

4.
Kovacic M, Mitrovic-Ajtic O, Beleslin-cokic B, Djikic D, Suboticki T, Diklic M . TLR4 and RAGE conversely mediate pro-inflammatory S100A8/9-mediated inhibition of proliferation-linked signaling in myeloproliferative neoplasms. Cell Oncol (Dordr). 2018; 41(5):541-553. DOI: 10.1007/s13402-018-0392-6. View

5.
Moroz O, Antson A, Murshudov G, Maitland N, Dodson G, Wilson K . The three-dimensional structure of human S100A12. Acta Crystallogr D Biol Crystallogr. 2001; 57(Pt 1):20-9. DOI: 10.1107/s090744490001458x. View