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Abstract
The α3(V) chain is poorly characterized among type V collagen chains. Pro-α3(V) collagen is expressed in newly synthesized bone as well as in the superficial fascia of developing muscle. Present study examined the expression in a mouse model of wound healing. Real-time reverse transcriptase polymerase chain reaction and in situ hybridization revealed transient expression of pro-α3(V) chain at a lower level than other fibrillar collagen genes after injury. Immunohistochemistry showed a similar expression pattern in the injured skin. In addition, electron microscopy showed that pro-α3(V) chain was localized in the amorphous nonfibrillar region, but not in fine or dense fibrils. The pro-α3(V) chain co-localized with heparan sulfate, which appeared in the skin after injury and might bind via an acidic segment of the pro-α3(V) chain. The matrix containing the pro-α3(V) chain may therefore be needed for the initiation of wound healing.
Acknowledgments
We thank Ms. S. Adachi, Mr. S. Imi, Mr. T. Matsuyama, Ms. T. Takayama, Mr. T. Kajitani, Ms. Y. Ueda, and Ms. M. Yasaka for their valuable technical support, and the staff members of Divisions of Life science Research, Laboratory Animal Science and Radioisotope Research, Department of Research Support, Research Promotion Project, Oita University, where we performed some experiments. This work was supported by the Grants-in-Aid for Scientific Research (Nos. 17390418 and 20390402 to Hidekatsu Yoshioka, and 21591672 to Hideaki Sumiyoshi) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
Declaration of interest
The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.