This article introduces a new biomedical / open surgical instrument to assist surgeon in applying surgical clips to patient’s body tissue and blood vessel during surgical processes. The new clip delivery system is de...This article introduces a new biomedical / open surgical instrument to assist surgeon in applying surgical clips to patient’s body tissue and blood vessel during surgical processes. The new clip delivery system is designed to better the clip’s distal advance through internal clip channel, jaw guiding track, and all other transition areas to keep surgical clip from accidental shooting out during clip’s distal move into jaws. Currently the clip distal move in normal surgical instrument is usually driven by compression springs and some complains of clip accidental drop-off were recorded in surgical procedures. Because higher request of dimensional tolerance and better component surface quality are needed in case the compression springs are used as driven force, a little dimensional devia-tion or less qualified part surface produced from manufacturing processes will potentially cause surgical clip device malfunction or misfiring of the clips. It is clearly known that the jaws can seriously sever or damage patient’s blood ves-sel or body tissue if there is no clip inside the jaws due to accidental clip drop-off, when surgeons close instrument handles. The improved internal system design in this new open surgical instrument can prevent clip from accidental drop-off because of well guided and controlled clip distal move through internal clip channel and track. Besides the operational force to fully form clip is lower than existing surgical clip devices due to better mechanical advantage in this new instrument design. In addition to the above, manufacturing and product cost can be decreased since lower requirement of dimensional tolerance and surface quality of instrumental parts is allowed in this new surgical instrument design. This new instrumental prototype is build upon the analysis of computer aided modeling and simulation to prove its good mechanical advantage, feasible function, reliable performance. The preliminary results of instrument fir-ing force from both computer aided modeling and prototype testin展开更多
PLA2 enzyme hydrolyzes arachidonic acid, and other polyunsaturated fatty acids, from the sn-2 position to release free arachidonic acid and a lysophospholipid. Previous studies reported that the PLA2 in invertebrate o...PLA2 enzyme hydrolyzes arachidonic acid, and other polyunsaturated fatty acids, from the sn-2 position to release free arachidonic acid and a lysophospholipid. Previous studies reported that the PLA2 in invertebrate organisms participates in lipid signaling molecules like arachidonic acid release in immune-associated tissues like hemo- cytes and fat bodies. In the present study, we cloned the BmPLA2 gene from fat body tissue of silkworm Bombyx mori, which has a total sequence of 1.031 kb with a 31.90 kDa pro- tein. In silico results of BmPLA2 indicated that the protein has a putative WD40 conserved domain and its phylogeny tree clustered with Danaus plexippus species. We investigated the transcriptional expression in development stages and tissues. The highest expression of BmPLA2 was screened in fat body among the studied tissues of third day fifth instar larva, with a high expression on third day fifth instar larva followed by a depression of expression in the wandering stage of the fifth instar larva. The expression of BmPLA2 in female pupa was higher than that of male pupa. Our RNAi-mediated gene silencing results showed highest reduction of BmPLA2 expression in post-24 h followed by post-48 and post-72 h. The BmPLA2-RNAi larvae and pupa could be characterized by pharate adult lethality and underdevelopment. The phenotypic characters of fat body cells in RNAi-induced larva im- plied that BmPLA2 affects the metabolic functions of fat body tissue in silkworm Bombyx mori.展开更多
The family of 30kDa lipoproteins （LP1-5） is abundant in silkworm pupa fat body （FB） and hemolymph. One of its members, the 29 kDa protein decreased in concentration from peripheral （PP） FB tissue but was sustain...The family of 30kDa lipoproteins （LP1-5） is abundant in silkworm pupa fat body （FB） and hemolymph. One of its members, the 29 kDa protein decreased in concentration from peripheral （PP） FB tissue but was sustained in perivisceral （PV） FB tissue at the time of apoptosis. This study investigated the correlation of the 30kDa proteins with FB apoptosis. Two protein fractions were purified, a 29 and a 30/31 kDa protein fraction, and they were used to test for activity against actinomycin D-induced apoptosis in the FB tissues. Concentrations as little as 50/zg/mL of the 29 kDa protein fraction efficiently inhibited apoptosis. Less antiapoptotie activity was detected for the higher MW fraction; DNA fragmentation was observed in FB tissue treated with 50 #g/mL of the 30/31 kDa fraction. The viability of the cells in the 29 kDa protein-supplemented culture was 40% higher than in the 31 kDa protein-supplemented culture. However, the 30 kDa lipoproteins were not able to prevent scheduled FB degeneration during silkworm metamorphosis. Thus, it is hypothesized that the antiapoptotic 29 kDa protein needs to be proteolytically degraded by a regulatory mechanism to allow programmed cell death of FB tissue.展开更多
文摘This article introduces a new biomedical / open surgical instrument to assist surgeon in applying surgical clips to patient’s body tissue and blood vessel during surgical processes. The new clip delivery system is designed to better the clip’s distal advance through internal clip channel, jaw guiding track, and all other transition areas to keep surgical clip from accidental shooting out during clip’s distal move into jaws. Currently the clip distal move in normal surgical instrument is usually driven by compression springs and some complains of clip accidental drop-off were recorded in surgical procedures. Because higher request of dimensional tolerance and better component surface quality are needed in case the compression springs are used as driven force, a little dimensional devia-tion or less qualified part surface produced from manufacturing processes will potentially cause surgical clip device malfunction or misfiring of the clips. It is clearly known that the jaws can seriously sever or damage patient’s blood ves-sel or body tissue if there is no clip inside the jaws due to accidental clip drop-off, when surgeons close instrument handles. The improved internal system design in this new open surgical instrument can prevent clip from accidental drop-off because of well guided and controlled clip distal move through internal clip channel and track. Besides the operational force to fully form clip is lower than existing surgical clip devices due to better mechanical advantage in this new instrument design. In addition to the above, manufacturing and product cost can be decreased since lower requirement of dimensional tolerance and surface quality of instrumental parts is allowed in this new surgical instrument design. This new instrumental prototype is build upon the analysis of computer aided modeling and simulation to prove its good mechanical advantage, feasible function, reliable performance. The preliminary results of instrument fir-ing force from both computer aided modeling and prototype testin
基金Acknowledgments The work was supported by the Nalional Basic Research Program of China under Grand No. 2012CB 114601 and the National Natural Science Foundation of China （No. NSFC：31372374/C 1703）, the Science and Technology Innovation Team of Zhejiang Province （No. 2010R50031 ） and Chinese Universities Scientific Fund to Yun-Gen Miao.
文摘PLA2 enzyme hydrolyzes arachidonic acid, and other polyunsaturated fatty acids, from the sn-2 position to release free arachidonic acid and a lysophospholipid. Previous studies reported that the PLA2 in invertebrate organisms participates in lipid signaling molecules like arachidonic acid release in immune-associated tissues like hemo- cytes and fat bodies. In the present study, we cloned the BmPLA2 gene from fat body tissue of silkworm Bombyx mori, which has a total sequence of 1.031 kb with a 31.90 kDa pro- tein. In silico results of BmPLA2 indicated that the protein has a putative WD40 conserved domain and its phylogeny tree clustered with Danaus plexippus species. We investigated the transcriptional expression in development stages and tissues. The highest expression of BmPLA2 was screened in fat body among the studied tissues of third day fifth instar larva, with a high expression on third day fifth instar larva followed by a depression of expression in the wandering stage of the fifth instar larva. The expression of BmPLA2 in female pupa was higher than that of male pupa. Our RNAi-mediated gene silencing results showed highest reduction of BmPLA2 expression in post-24 h followed by post-48 and post-72 h. The BmPLA2-RNAi larvae and pupa could be characterized by pharate adult lethality and underdevelopment. The phenotypic characters of fat body cells in RNAi-induced larva im- plied that BmPLA2 affects the metabolic functions of fat body tissue in silkworm Bombyx mori.
文摘The family of 30kDa lipoproteins （LP1-5） is abundant in silkworm pupa fat body （FB） and hemolymph. One of its members, the 29 kDa protein decreased in concentration from peripheral （PP） FB tissue but was sustained in perivisceral （PV） FB tissue at the time of apoptosis. This study investigated the correlation of the 30kDa proteins with FB apoptosis. Two protein fractions were purified, a 29 and a 30/31 kDa protein fraction, and they were used to test for activity against actinomycin D-induced apoptosis in the FB tissues. Concentrations as little as 50/zg/mL of the 29 kDa protein fraction efficiently inhibited apoptosis. Less antiapoptotie activity was detected for the higher MW fraction; DNA fragmentation was observed in FB tissue treated with 50 #g/mL of the 30/31 kDa fraction. The viability of the cells in the 29 kDa protein-supplemented culture was 40% higher than in the 31 kDa protein-supplemented culture. However, the 30 kDa lipoproteins were not able to prevent scheduled FB degeneration during silkworm metamorphosis. Thus, it is hypothesized that the antiapoptotic 29 kDa protein needs to be proteolytically degraded by a regulatory mechanism to allow programmed cell death of FB tissue.
