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A Robust Sericin Hydrogel Formed by a Native Sericin from Silkworm Bodies
Yeshun Zhang,Wu Tangfeng,Congyi Shen,Gang Xu,Heguang Chen,Hui Yan,Meng Xiong,Guozheng Zhang 한국섬유공학회 2022 Fibers and polymers Vol.23 No.7
Sericin hydrogels with a serial of excellent properties are attractive in tissue engineering but still limited due totheir poor mechanical strength. In this study we report a robust sericin hydrogel with high elastic modulus (310 kPa) that wasformed by a native sericin solution with high concentration (16 %, w/v) collected from silkworm bodies. The hydrogel wasperformed via H2O2 and presented gelling kinetics within 30 s. This hydrogel possesses eximious elasticity, goodcytocompatibility, and more stable in solution as well as porous structure. In addition, the hydrogel system is suitable forloading bioactive molecules owing to its wonderful sustained manner for delivering bioactive reagent. Together, our studyindicates that the sericin hydrogel may serve as a new multifunctional platform for extending the application of sericin intissue engineering and regenerative medicine.
Feng Ming Zou,이광식,김보연,김홍자,Zhong Zheng Gui,Guozheng Zhang,Xijie Guo,진병래 한국응용곤충학회 2015 Journal of Asia-Pacific Entomology Vol.18 No.4
Insect cuticular melanization is regulated by the prophenoloxidase (proPO)-activating system, which is also involved in the innate immune reaction. Here, we demonstrate how the differentiation of the proPO-activating system is regulated toward a cuticular melanization or innate immunity function in silkworm (Bombyx mori) pupae. Our results indicate that the differential and spatial regulation of key components, such as the proPOactivating enzyme and proPOs, primes the proPO-activating system for either cuticular melanization or innate immunity. This dual strategy for cuticular melanization in development and innate immunity upon infection demonstrates a two-pronged defense mechanism that is mediated by the priming of the proPO system.
Molecular Cloning of a Profilin cDNA from Bombyx mori
Wei, Yadong,Gui, Zhongzheng,Choi, Young Soo,Guo, Xijie,Zhang, Guozheng,Sohn, Hung Dae,Jin, Byung Rae Korean Society of Sericultural Science 2004 International Journal of Industrial Entomology Vol.9 No.1
The actin-binding protein profilin cDNA was firstly isolated from the lepidopteran insect, silkworm Bombyx mori. The B. mori profilin cDNA contains an open reading frame of 378 bp encoding 126 amino acid residues and possesses three cysteine residues. The deduced amino acid sequence of the B. mori profilin cDNA showed 80% identity to Apis mellifera profilin and 72% to Drosophila melanogaster profilin. Northern blot analysis showed that B. mori profilin is highly expressed in epidermis and less strongly in silk gland. In addition, Northern blot analysis revealed the presence of B. mori profilin transcripts in all tissues examined, suggesting that B. mori profilin gene is expressed in most, if not all, body tissues.