S100B suppresses the differentiation of C3H/10T1/2 murine embryonic mesenchymal cells into osteoblasts

Abstract

S100 calcium-binding protein B (S100B) is expressed and released by adipocytes, and is positively correlated with body mass index, however, the direct effects of S100B on adipocytes remain unclear. Bone marrow‑derived mesenchymal stem cells have the capacity to differentiate into osteoblasts and adipocytes, which is important for bone metabolism. The current study aimed to determine the effect of S100B on adipogenesis and osteogenesis. The mouse embryo cell line C3H/10T1/2 was used to build cell models with varying levels of S100B protein expression. Western blot analysis was performed to assess the expression of various marker proteins. Oil red O staining and alizarin red S staining were used to detect adipogenesis and osteogenesis, respectively. S100B overexpression was associated with a significant increase in oil red O staining and a significant reduction in alizarin red S staining. Runt‑related transcription factor‑2 and bone morphogenetic protein 2 expression levels were significantly increased in the S100B underexpression group, however not in the S100B overexpression group. By contrast, the expression levels of the adipogenesis markers peroxisome proliferator‑activated receptor γ and CCAAT‑enhancer‑binding protein α was significantly increased in the S100B overexpression group, however not in the S100B underexpression group. Osteogenesis stimulation increased extracellular signal‑regulated kinase (ERK) phosphorylation, and adipogenesis stimulation increased c‑Jun N‑terminal kinase (JNK) phosphorylation. The results suggest that S100B inhibits osteogenesis, however stimulates adipogenesis. The ERK pathway is involved in the regulation of osteogenesis, whereas the JNK pathway is involved in the regulation of adipogenesis.

Growing role of S100B protein as a putative therapeutic target for neurological- and nonneurological-disorders

“…As an intracellular regulator, S100B is involved in a series of activities, such as cell proliferation, survival, differentiation, regulation of calcium homeostasis, enzyme regulation, interaction with the cytoskeleton (Agam and Almog, 2015;Arcuri et al, 2005;Baudier et al, 1992;Baudier and Cole, 1988;Brozzi et al, 2009;Donato, 1988;Gentil et al, 2001;Gógl et al, 2016;Heierhorst et al, 1996;Li et al, 2016;Mbele et al, 2002;Millward et al, 1998;Pozdnyakov et al, 1997;Raponi et al, 2007;Riuzzi et al, 2011;Saito et al, 2007;Shimamoto et al, 2014;Skripnikova and Gusev, 1989;Tsoporis et al, 2009;Wen et al, 2012;Xiong et al, 2000;Zimmer and Van Eldik, 1986), but these functions do not appear to delineate a clear univocal intracellular role for the protein. On the other hand, mounting evidence is now designing more defined roles for extracellular S100B in both physiological and pathological conditions.…”

The S100B story: from biomarker to active factor in neural injury

“…; Li et al . ), participates in the regulation of cellular calcium homeostasis and enzyme activities (Zimmer and Van Eldik ; Heierhorst et al . ; Pozdnyakov et al .…”

“…Intracellularly, S100B, as a calcium-sensor protein, appears to regulate a variety of activities, transferring signals from second messengers and interacting with different molecules in different cell types. In particular, S100B intervenes in cell proliferation, survival and differentiation (Baudier et al 1992;Millward et al 1998;Arcuri et al 2005;Raponi et al 2007;Saito et al 2007;Riuzzi et al 2011;Shimamoto et al 2014;Li et al 2016), participates in the regulation of cellular calcium homeostasis and enzyme activities (Zimmer and Van Eldik 1986;Heierhorst et al 1996;Pozdnyakov et al 1997;Xiong et al 2000;Gentil et al 2001;Brozzi et al 2009;Tsoporis et al 2009;Wen et al 2012;Agam and Almong 2015;Gogl et al 2016) and even interacts with the cytoskeleton (Baudier and Cole 1988;Donato 1988;Skripnikova and Gusev 1989;Mbele et al 2002), but data currently available do not appear to converge toward a clearly defined function. In contrast, there is mounting evidence indicating an increasingly clearer role for extracellular S100B.…”

Systematic Review and Meta-Analysis of Damage Associated Molecular Patterns HMGB1 and S100B in Schizophrenia

“…S100B is a calcium binding protein localised in the cytosol of glial cells and astrocytes of the central nervous system [ 19 ], and both immune and non-immune cells of the peripheral nervous system [ 20 ]. S100B is important for a plethora of homeostatic activities including cell cycle progression and differentiation [ 21 , 22 ], calcium homeostasis [ 23 ], activation of calcium dependent enzymes [ 24 ], and microtubule assembly and disassembly of the cytoskeleton [ 25 ]. S100B is released by damaged or dying cells and interacts with the receptor for advanced glycation end products (RAGE) [ 26 ], conferring neuroprotective or neurotoxic effects on neurons in a concentration dependent manner [ 27 ].…”