Periostin and Integrin Signaling in Stem Cell Regulation

Kim

et al. 2019

Cells

Human palatine tonsils are potential tissue source of multipotent mesenchymal stem cells (MSCs). The proliferation rate of palatine tonsil-derived MSCs (TMSCs) is far higher than that of bone marrow-derived MSCs (BMSCs) or adipose tissue-derived MSCs (ADSCs). In our previous study, we had found through DNA microarray analysis that tensin-3 (TNS3), a type of focal adhesion protein, was more highly expressed in TMSCs than in both BMSCs and ADSCs. Here, the role of TNS3 in TMSCs and its relationship with integrin were investigated. TNS3 expression was significantly elevated in TMSCs than in other cell types. Cell growth curves revealed a significant decrease in the proliferation and migration of TMSCs treated with siRNA for TNS3 (siTNS3). siTNS3 treatment upregulated p16 and p21 levels and downregulated SOX2 expression and focal adhesion kinase, protein kinase B, and c-Jun N-terminal kinase phosphorylation. siTNS3 transfection significantly reduced adipogenic differentiation of TMSCs and slightly decreased osteogenic and chondrogenic differentiation. Furthermore, TNS3 inhibition reduced active integrin beta-1 (ITGβ1) expression, while total ITGβ1 expression was not affected. Inhibition of ITGβ1 expression in TMSCs by siRNA showed similar results observed in TNS3 inhibition. Thus, TNS3 may play an important role in TMSC proliferation and differentiation by regulating active ITGβ1 expression.

Section: Discussionmentioning

confidence: 99%

Tensin-3 Regulates Integrin-Mediated Proliferation and Differentiation of Tonsil-Derived Mesenchymal Stem Cells

Kim

et al. 2019

Cells

“…Chondrocytes express several integrins including αvβ3 and αvβ5 (34). Thus, interaction between periostin and integrins on chondrosarcoma cells may play a major role in the survival and proliferation like as has also been found in other cells (35,36). Proliferation is reduced in periostin knockdown SW1353 cells, and recombinant periostin restored the phenotype.…”

Section: Discussionmentioning

confidence: 75%

Mesenchymal Stem Cells Combined With IFNγ Induce Apoptosis of Breast Cancer Cells Partially Through TRAIL

et al. 2020

Background/Aim: Periostin exists as an extracellular matrix protein in several carcinomas and is related to metastasis and poor prognosis. It is mainly secreted from cancer associated fibroblasts, and not from carcinoma cells. As a tumor microenvironment component, periostin usually mediates tumor cell stemness, metastasis, angiogenesis and lymphangiogenesis. This study aimed to examine the role of periostin in chondrosarcoma. Materials and Methods: To evaluate the effect of periostin on the proliferation of chondrosarcoma cells, MTT assay was performed on SW1353 cells and periostin knockdown SW1353 cells. Migration activity was examined using Boyden chamber. Results: Periostin, secreted from chondrosarcoma cells, was found to support proliferation, and maintain stemness and migration of chondrosarcoma cells. Periostin also induced proliferation and migration of lymphatic endothelial cells. Conclusion: Periostin plays an important role in chondrosarcoma development and disease progression.

“…Therefore, it is important to monitor, recognize, and manage these complications in parallel with the intracranial complications, thereby allowing the optimization of the management of aSAH patients, leading to improvement in the overall outcomes. However, as described earlier in the present report, since periostin may be upregulated by a number of stimuli and interacts with several molecules [20][21][22][23][24][25], it may be difficult to identify the tissues or pathologies from which the observed increases in the plasma periostin levels might be originating. This implies potential limitations such as determining the specificity when applying periostin as a biomarker for predicting or monitoring the clinical events in the aSAH patients.…”

Section: Potential Limitationsmentioning

confidence: 69%

“…The EMI domain potentially binds to other ECM proteins such as collagen (types I and V), fibronectin, and a matricellular protein βig-h3 (also known as keratoepithelin, RGD-CAP, or transforming growth factor [TGF]-β-induced protein), and it is essential for the multimerization of periostin from a dimer to a hexamer [20][21][22]. The four Fasciclin-1 domains bind to a pro-collagen C-proteinase (i.e., bone morphogenetic protein (BMP)-1), matricellular proteins tenascin-C, cellular communication network factor 3 (also referred to nephroblastoma overexpressed), and integrins [21][22][23][24][25]. The carboxyl-terminal domain binds to heparin and proteoglycan [22].…”

Section: Periostinmentioning

confidence: 99%

The Role of Periostin in Brain Injury Caused by Subarachnoid Hemorrhage

Kanamaru¹,

Kawakita²,

Asada³

et al. 2019

obm neurobiol

Aneurysmal subarachnoid hemorrhage (aSAH) causes serious brain injury, and its mechanisms have not been completely unraveled so far. The causative factors for the brain injury initiated by an aneurysm rupture, which is referred to as the early brain injury (EBI), include elevated intracranial pressure, cerebral hypoperfusion, and blood contents that are directly exposed to the brain surface. At Day 4-14 post aSAH, delayed cerebral ischemia (DCI) often develops, which may worsen the neurological outcomes critically. DCI may be a consequence of EBI. Understanding the complex mechanisms underlying the post-aSAH brain injury (EBI and DCI) is, therefore, important in order to improve the neurological outcomes. In addition, several biomarkers possibly associated with EBI, DCI, and neurological outcome have been investigated, although none of these has been conclusive. A matricellular protein periostin has emerged as an important potential contributor to EBI and DCI, and may serve as the biomarker and a therapeutic molecular target for EBI and DCI. In the present report, the possible role of periostin in aSAH has been reviewed.