Compositional analysis of the glycosaminoglycan family in velvet antlers of Sika deer (Cervus nippon) at different growing stages
- 31 Downloads
Glycosaminoglycans (GAG) from the velvet antlers of Sika deer (Cervus nippon) at the different growing stages (Fukurozuno, Anshi, and Santajo) of bred and wild deer were isolated and their concentrations and sulfation patterns were analyzed. GAG were digested with chondroitinase ABC, ACI, heparinase-I and -III, and keratanase-II into the corresponding repeating disaccharides of chondroitin sulfate (CS), dermatan sulfate (DS), hyaluronan, heparan sulfate (HS), and keratan sulfate. Cartilaginous tissues contained CS-DS at high concentrations with an almost equal ratio of 4- and 6-sulfates, while 4-sulfate-type CS-DS predominantly occupied ossified tissues, but at low concentrations. High O- and N-sulfation degrees of HS correspond to high ossification. Dynamic quantitative changes in CS-DS and compositional changes in CS-DS and HS were closely associated with the mineralization of deer antlers.
KeywordsVelvet antler Chondroitin sulfate Dermatan sulfate Heparan sulfate Keratan sulfate Hyaluronan
We are grateful to Mr. Tsuyoshi Kawato for the kind gift of wild velvet antlers. We also thank Amano Enzyme Inc. (Nagoya, Japan) for kindly gifting PROTIN NY100. The authors thank Dr. Kenji Uchimura (UMR8576-CNRS, University of Lille), Ms. Kwon-Jung Yi (Konkuk University), Mr. Takamu Fujii, Ms. Yukino Ito (Meijo University), Mr. Yuga Inoue, Ms. Asumi Uemura, Mr. Daiki Sugita, Ms. Yuna Uemura, Ms. Yuka Omura, Ms. Akari Tani, and Ms. Marin Mitani (Tottori University) for their helpful assistance.
N.T.-O. performed the preparation of glycans and analyzed CS/DS and HA. S.M. and S.Y. performed HS analyses. Z.Z. and K.K. performed KS analyses. S.-K.K., C.-H.L., and B.-T.J. collected deer antlers. Y.Z.H. performed histological examinations. J.T. designed the study and wrote the manuscript.
Compliance with ethical standards
Conflicts of interest
The authors declare that they have no conflicts of interests.
This article does not contain any studies with human participants or animals performed by any of the authors.
- 7.Arima, K., Fujita, H., Toita, R., Imazu-Okada, A., Tsutsumishita-Nakai, N., Takeda, N., Nakao, Y., Wang, H., Kawano, M., Matsushita, K., Tanaka, H., Morimoto, S., Nakamura, A., Kitagaki, M., Hieda, Y., Hatto, R., Watanabe, A., Yumura, T., Okuhara, T., Hayashi, H., Shimizu, K., Nakayama, K., Masuda, S., Ishihara, Y., Yoshioka, S., Yoshioka, S., Shirade, S., Tamura, J.I.: Amounts and compositional analysis of glycosaminoglycans in the tissue of fish. Carbohydr. Res. 366, 25–32 (2013)CrossRefGoogle Scholar
- 12.Zhang, Z., Ohtake-Niimi, S., Kadomatsu, K., Uchimura, K.: Reduced molecular size and altered disaccharide composition of cerebral chondroitin sulfate upon Alzheimer’s pathogenesis in mice. Nagoya J. Med. Sci. 78, 293–301 (2016)Google Scholar
- 15.Robinson, H.C., Dorfman, A.: The sulfation of chondroitin sulfate in embryonic chick cartilage epiphyses. J. Biol. Chem. 244, 348–352 (1969)Google Scholar
- 17.Habuchi, H., Kimata, K., Suzuki, S.: Changes in proteoglycan composition during development of rat skin. The occurrence in fetal skin of a chondroitin sulfate proteoglycan with high turnover rate. J. Biol. Chem. 261, 1031–1040 (1986)Google Scholar
- 18.Roughly, P.J., White, R.J.: Age-related changes in the structure of the proteoglycan subunits from human articular cartilage. J. Biol. Chem. 255, 217–224 (1980)Google Scholar