Journal
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY
Volume 63, Issue 6, Pages 438-448Publisher
SAGE PUBLICATIONS LTD
DOI: 10.1369/0022155415580622
Keywords
alpha-SMA; culture; fibrillin-1; human dental pulp; pSmad2; 3
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Funding
- Ministry of Education, Science, Sports and Culture, Japan [22592119, 25462952, 24592863]
- Grants-in-Aid for Scientific Research [15K11093, 24592863, 22592119, 25462952] Funding Source: KAKEN
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Myofibroblasts and extracellular matrix are important components in wound healing. Alpha-smooth muscle actin (-SMA) is a marker of myofibroblasts. Fibrillin-1 is a major constituent of microfibrils and an extracellular-regulator of TGF-1, an important cytokine in the transdifferentiation of resident fibroblasts into myofibroblasts. To study the correlation between changes in fibrillin-1 expression and myofibroblast differentiation, we examined alterations in fibrillin-1 and -SMA expression in organotypic cultures of dental pulp in vitro. Extracted healthy human teeth were cut to 1-mm-thick slices and cultured for 7 days. In intact dental pulp, fibrillin-1 was broadly distributed, and -SMA was observed in pericytes and vascular smooth muscle cells. After 7 days of culture, immunostaining for fibrillin-1 became faint concomitant with a downregulation in its mRNA levels. Furthermore, fibroblasts, odontoblasts and Schwann cells were immunoreactive for -SMA with a significant increase in -SMA mRNA expression. Double immunofluorescence staining was positive for pSmad2/3, central mediators of TGF- signaling, and -SMA. The administration of inhibitors for extracellular matrix proteases recovered fibrillin-1 immunostaining; moreover, fibroblasts lost their immunoreactivity for -SMA along with a downregulation in -SMA mRNA. These findings suggest that the expression of -SMA is TGF-1 dependent, and fibrillin-1 degradation and downregulation might be implicated in the differentiation of myofibroblasts in dental pulp wound healing.
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