The S100B Protein: A Multifaceted Pathogenic Factor More Than a Biomarker
- Int J Mol Sci. 2023 May 31;24(11):9605. doi: 10.3390/ijms24119605.
- 1. Department of Neuroscience, Catholic University of the Sacred Heart, 00168 Rome, Italy.
- 2. IRCCS San Raffaele Scientific Institute, Università Vita-Salute San Raffaele, 20132 Milan, Italy.
- 3. Department of Medicine, LUM University, 70010 Casamassima, Italy.
- 4. Genes, Via Venti Settembre 118, 00187 Roma, Italy.
- 5. Istituto di Scienze e Tecnologie Chimiche "Giulio Natta" SCITEC-CNR, 00168 Rome, Italy.
- 6. Department of Pharmaceutical and Pharmacological Sciences, University of Padova, 35131 Padova, Italy.
- 7. Laboratory of Epidemiology and Biotechnologies, Department of Movement, Human and Health Sciences, University of Rome "Foro Italico", 00135 Rome, Italy.
- 8. Department of Translational Medicine and Surgery, Section of General Pathology, Catholic University of the Sacred Heart, 00168 Rome, Italy.
- 9. Department of Medicine and Surgery, Section of Human, Clinical and Forensic Anatomy, University of Perugia, 06132 Perugia, Italy.
S100B is a calcium-binding protein mainly concentrated in astrocytes in the nervous system. Its levels in biological fluids are recognized as a reliable biomarker of active neural distress, and more recently, mounting evidence points to S100B as a Damage-Associated Molecular Pattern molecule, which, at high concentration, triggers tissue reactions to damage. S100B levels and/or distribution in the nervous tissue of patients and/or experimental models of different neural disorders, for which the protein is used as a biomarker, are directly related to the progress of the disease. In addition, in experimental models of diseases such as Alzheimer's and Parkinson's diseases, amyotrophic lateral sclerosis, multiple sclerosis, traumatic and vascular acute neural injury, epilepsy, and inflammatory bowel disease, alteration of S100B levels correlates with the occurrence of clinical and/or toxic parameters. In general, overexpression/administration of S100B worsens the clinical presentation, whereas deletion/inactivation of the protein contributes to the amelioration of the symptoms. Thus, the S100B protein may be proposed as a common pathogenic factor in different disorders, sharing different symptoms and etiologies but appearing to share some common pathogenic processes reasonably attributable to neuroinflammation.