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Venom Gland Structure of Chinese Centipede Scolopendra subspinipes mutilans
Hua Weijian1,2, Xu Guohua1, Zhou Siqiao3, Hua Zichun2*
1Department of Biology, Jiangsu Institute of Education, Nanjing 210013, China;2State Key Lab of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, China;3Nanjing Drum Tower Hospital, the Affiliated Hospital
Abstract: Structure of venom gland from Chinese centipede Scolopendra subspinipes mutilans was observed with immunohistochemistry by light microscopy, transmission electron microscopy and laser confocal microscope. Results showed the crescent-shaped venom gland ran through the whole maxilliped segment. It was a simple tubuloacinar gland and mainly consisted of two cell types, secretary cells and intermediate thin epithelial cells. The secretary cells surrounded by mussels radicalized around a chitinous venom duct with its thin neck controlled by a ring sphincter. Its excreting end intruded into the duct lumen through a pore on the duct wall with a back and forth folded valve, its enlarged blunt end directed to base membrane of the gland. A large amount of secretary substances and high electronic dens secretary lysosomes distributed in cytoplasm of the secreting cell. Within the secretary lysosomes, rod-like venom proteins diluted gradually through an amorphous structure in the extreme dense core, and were degraded into non-vesicle homogenized venom before it arrived the venom duct, concomitant with decrease in the secretary lysosomes’ electronic dense. Venom was discharged into the lumen by exocytosis at last and became more dispersed and homogenerous. Immunohistochemistry showed that main constituents of the secretary bodies gathered near the neck of the secretary cells were venom proteins. They distributed in a gradient enhancement pattern from the base membrane to the lumen center of the gland, consistent with the self-excited fluorescence distribution pattern. Based on these observations, authors propose that centipede venom is secreted by a non-classical pathway which is mediated via secretary lysosomes.