Abstract
S100 proteins are widely expressed small molecular EF-hand calcium-binding proteins of vertebrates, which are involved in numerous cellular processes, such as Ca2+ homeostasis, proliferation, apoptosis, differentiation, and inflammation. Although the complex network of S100 signalling is by far not fully deciphered, several S100 family members could be linked to a variety of diseases, such as inflammatory disorders, neurological diseases, and also cancer. The research of the past decades revealed that S100 proteins play a crucial role in the development and progression of many cancer types, such as breast cancer, lung cancer, and melanoma. Hence, S100 family members have also been shown to be promising diagnostic markers and possible novel targets for therapy. However, the current knowledge of S100 proteins is limited and more attention to this unique group of proteins is needed. Therefore, this review article summarises S100 proteins and their relation in different cancer types, while also providing an overview of novel therapeutic strategies for targeting S100 proteins for cancer treatment.
Highlights
A potential active mechanism of secretion has not been fully understood since S100 proteins lack the structural sequence for the classical endoplasmic reticulum (ER)/Golgi secretory pathway, but cellular events leading to membrane ruptures such as passive cellular necrosis or regulated types of necrosis or tubulin-dependent translocation are considered in this context [30,31]
Recent studies mRNA expression of S100 proteins in correlation with the survival of ovarian cancer patients demonstrated that high levels of the S100 family members S100A2, S100A10, Recent studies investigating mRNA expression of S100 proteins in correlation with the survival
This study showed that treatment with tasquinimod resulted in significantly longer radiologic progression-free survival compared with the placebo group
Summary
Moore isolated a protein from the bovine brain to identify specific proteins of the nervous system. Since it was soluble in 100% saturated ammonium sulfate at neutral pH, the protein was named “S-100” [1]. Isobe et al later showed that this S100 protein formed a dimer, consisting of two homologous yet different molecules, defined as S100A and S100B [2,3]. It has since been shown that these proteins are involved in a variety of different pathways, thereby playing a critical role in essential cellular processes, such as proliferation, apoptosis, differentiation, and inflammation [5]
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