目的观察白斑颗粒Ⅰ号方对白癜风患者Foxp3 m RNA表达的影响,阐明白斑Ⅰ号方治疗白癜风的作用机制。方法白癜风患者60例,随机分为试验组和对照组各30例,健康对照组30例,采用RT-PCR方法检测各组PBMC中Foxp3 m RNA表达变化情况。结果白癜...目的观察白斑颗粒Ⅰ号方对白癜风患者Foxp3 m RNA表达的影响,阐明白斑Ⅰ号方治疗白癜风的作用机制。方法白癜风患者60例,随机分为试验组和对照组各30例,健康对照组30例,采用RT-PCR方法检测各组PBMC中Foxp3 m RNA表达变化情况。结果白癜风患者组Foxp3 m RNA水平低于健康对照组,差异有统计学意义(P<0.05);实验组治疗3个月后Foxp3 m RNA水平高于治疗前,差异有统计学意义(P<0.05);对照组治疗3个月后Foxp3 m RNA水平高于治疗前,差异有统计学意义(P<0.05);治疗3个月后,实验组治疗前后外周血Foxp3 m RNA升高值高于对照组治疗前后外周血Foxp3 m RNA升高值,差异有统计学意义(P<0.05)。结论白斑颗粒Ⅰ号可能通过上调调节T细胞功能,使PBMC Foxp3 m RNA恢复或接近正常水平达到治疗白癜风的目的。展开更多
White spot syndrome virus (WSSV), a unique member within the virus family Nimaviridae, is the most notorious aquatic virus infecting shrimp and other crustaceans and has caused enormous economic losses in the shrimp f...White spot syndrome virus (WSSV), a unique member within the virus family Nimaviridae, is the most notorious aquatic virus infecting shrimp and other crustaceans and has caused enormous economic losses in the shrimp farming industry worldwide. Therefore, a comprehensive understanding of WSSV morphogenesis, structural proteins, and replication is essential for developing prevention measures of this serious parasite. The viral genome is approximately 300kb and contains more than 180 open reading frames (ORF). However, most of proteins encoded by these ORF have not been characterized. Due to the importance of WSSV structural proteins in the composition of the virion structure, infection process and interaction with host cells, knowledge of structural proteins is essential to understanding WSSV entry and infection as well as for exploring effective prevention measures. This review article summarizes mainly current investigations on WSSV structural proteins including the relative quantities, localization, function and protein-protein interactions. Traditional proteomic studies of 1D or 2D gel electrophoresis separations and mass spectrometry (MS) followed by database searches have identified a total of 39 structural proteins. Shotgun proteomics and iTRAQ were initiated to identify more structural proteins. To date, it is estimated that WSSV is assembled by at least 59 structural proteins, among them 35 are defined as the envelope fraction (including tegument proteins) and 9 as nucleocapsid proteins. Furthermore, the interaction within several major structural proteins has also been investigated. This identitification and characterization of WSSV protein components should help in the understanding of the viral assembly process and elucidate the roles of several major structural proteins.展开更多
The nucleocapsid protein VP15 of white spot syndrome virus (WSSV) is a basic DNA-binding protein. Three canonical bipartite nuclear localization signals (NLSs), called NLS1 (aa 11-27), NLS2 (aa 33-49) and NLS3 (44-60)...The nucleocapsid protein VP15 of white spot syndrome virus (WSSV) is a basic DNA-binding protein. Three canonical bipartite nuclear localization signals (NLSs), called NLS1 (aa 11-27), NLS2 (aa 33-49) and NLS3 (44-60), have been detected in this protein, using the ScanProsite computer program. To determine the nuclear localization sequence of VP15, the full-length open reading frame, or the sequence of one of the three NLSs, was fused to the green fluorescent protein (GFP) gene, and transiently expressed in insect Sf9 cells. Transfection with full-length VP15 resulted in GFP fluorescence being distributed exclusively in the nucleus. NLS1 alone could also direct GFP to the nucleus, but less efficiently. Neither of the other two NLSs (NLS2 and 3) was functional when expressed alone, but exhibited similar activity to NLS1 when they were expressed as a fusion peptide. Furthermore, a mutated VP15, in which the two basic amino acids (11RR12) of NLS1 were changed to two alanines (11AA12), caused GFP to be localized only in the cytoplasm of Sf9 cells. These results demonstrated that VP15, as a nuclear localization protein, needs cooperation between its three NLSs, and that the two residues (11RR12) of NLS1 play a key role in transporting the protein to the nucleus.展开更多
Fish glue is the collagen from scale skin and bone of fish. It is known for value added product from fish processing and the adhesive agent for wood paper book binding etc. This work was aimed with the method to produ...Fish glue is the collagen from scale skin and bone of fish. It is known for value added product from fish processing and the adhesive agent for wood paper book binding etc. This work was aimed with the method to produce fish glue from fish skin through representing optimum fish type and its glue character by study on standard method for fish glue processing (using Oreochromis niloticus skin as the model), optimum fish type and characterization of the glue from optimum fish skin. Soaking fish skin in 0.1 N NaOH for 6 h and changed it every 3 h for pretreatment before acid extraction with 0.5 M acetic acid was the optimum condition for the standard processing. Among 20 types (O. niloticus, Oreochromis sp., Nemipterus sp., Psettodes erumei, Epiephelus malabaricus, Sphyraena obstsata, Channa striata, Xenentodon cancila, Barbonymus gonionotus, Liza vaigiensis, Anabas testudineus, Chanos chanos, Micronema bleekeri, Thunnus tonggol, Rastrelliger brachysom, Epinephelus lanceolatus, Lutjanus lineolatus, Pomadasys hasta, Selar crumenophthalmus and Sardaorentalis sp.), Chanos chanos was an appropriate type for glue production. Fat, protein, carbohydrate, moisture, pH and viscosity of Chanos chanos glue were 0.32%, 4.23%, 83.8%, 11.56%, 3.35, 4,978.33-8,180 cp, respectively. The glue was collagen type I which was composed ofal (148 kDa) and a2 (129 kDa) chain and could bind paper, wood and foam sheet.展开更多
文摘目的观察白斑颗粒Ⅰ号方对白癜风患者Foxp3 m RNA表达的影响,阐明白斑Ⅰ号方治疗白癜风的作用机制。方法白癜风患者60例,随机分为试验组和对照组各30例,健康对照组30例,采用RT-PCR方法检测各组PBMC中Foxp3 m RNA表达变化情况。结果白癜风患者组Foxp3 m RNA水平低于健康对照组,差异有统计学意义(P<0.05);实验组治疗3个月后Foxp3 m RNA水平高于治疗前,差异有统计学意义(P<0.05);对照组治疗3个月后Foxp3 m RNA水平高于治疗前,差异有统计学意义(P<0.05);治疗3个月后,实验组治疗前后外周血Foxp3 m RNA升高值高于对照组治疗前后外周血Foxp3 m RNA升高值,差异有统计学意义(P<0.05)。结论白斑颗粒Ⅰ号可能通过上调调节T细胞功能,使PBMC Foxp3 m RNA恢复或接近正常水平达到治疗白癜风的目的。
文摘White spot syndrome virus (WSSV), a unique member within the virus family Nimaviridae, is the most notorious aquatic virus infecting shrimp and other crustaceans and has caused enormous economic losses in the shrimp farming industry worldwide. Therefore, a comprehensive understanding of WSSV morphogenesis, structural proteins, and replication is essential for developing prevention measures of this serious parasite. The viral genome is approximately 300kb and contains more than 180 open reading frames (ORF). However, most of proteins encoded by these ORF have not been characterized. Due to the importance of WSSV structural proteins in the composition of the virion structure, infection process and interaction with host cells, knowledge of structural proteins is essential to understanding WSSV entry and infection as well as for exploring effective prevention measures. This review article summarizes mainly current investigations on WSSV structural proteins including the relative quantities, localization, function and protein-protein interactions. Traditional proteomic studies of 1D or 2D gel electrophoresis separations and mass spectrometry (MS) followed by database searches have identified a total of 39 structural proteins. Shotgun proteomics and iTRAQ were initiated to identify more structural proteins. To date, it is estimated that WSSV is assembled by at least 59 structural proteins, among them 35 are defined as the envelope fraction (including tegument proteins) and 9 as nucleocapsid proteins. Furthermore, the interaction within several major structural proteins has also been investigated. This identitification and characterization of WSSV protein components should help in the understanding of the viral assembly process and elucidate the roles of several major structural proteins.
基金State Key Program for Basic ResearchGrants (2006CB101801)the Chinese Academy ofSciences (KSCX2-SW-302).
文摘The nucleocapsid protein VP15 of white spot syndrome virus (WSSV) is a basic DNA-binding protein. Three canonical bipartite nuclear localization signals (NLSs), called NLS1 (aa 11-27), NLS2 (aa 33-49) and NLS3 (44-60), have been detected in this protein, using the ScanProsite computer program. To determine the nuclear localization sequence of VP15, the full-length open reading frame, or the sequence of one of the three NLSs, was fused to the green fluorescent protein (GFP) gene, and transiently expressed in insect Sf9 cells. Transfection with full-length VP15 resulted in GFP fluorescence being distributed exclusively in the nucleus. NLS1 alone could also direct GFP to the nucleus, but less efficiently. Neither of the other two NLSs (NLS2 and 3) was functional when expressed alone, but exhibited similar activity to NLS1 when they were expressed as a fusion peptide. Furthermore, a mutated VP15, in which the two basic amino acids (11RR12) of NLS1 were changed to two alanines (11AA12), caused GFP to be localized only in the cytoplasm of Sf9 cells. These results demonstrated that VP15, as a nuclear localization protein, needs cooperation between its three NLSs, and that the two residues (11RR12) of NLS1 play a key role in transporting the protein to the nucleus.
文摘Fish glue is the collagen from scale skin and bone of fish. It is known for value added product from fish processing and the adhesive agent for wood paper book binding etc. This work was aimed with the method to produce fish glue from fish skin through representing optimum fish type and its glue character by study on standard method for fish glue processing (using Oreochromis niloticus skin as the model), optimum fish type and characterization of the glue from optimum fish skin. Soaking fish skin in 0.1 N NaOH for 6 h and changed it every 3 h for pretreatment before acid extraction with 0.5 M acetic acid was the optimum condition for the standard processing. Among 20 types (O. niloticus, Oreochromis sp., Nemipterus sp., Psettodes erumei, Epiephelus malabaricus, Sphyraena obstsata, Channa striata, Xenentodon cancila, Barbonymus gonionotus, Liza vaigiensis, Anabas testudineus, Chanos chanos, Micronema bleekeri, Thunnus tonggol, Rastrelliger brachysom, Epinephelus lanceolatus, Lutjanus lineolatus, Pomadasys hasta, Selar crumenophthalmus and Sardaorentalis sp.), Chanos chanos was an appropriate type for glue production. Fat, protein, carbohydrate, moisture, pH and viscosity of Chanos chanos glue were 0.32%, 4.23%, 83.8%, 11.56%, 3.35, 4,978.33-8,180 cp, respectively. The glue was collagen type I which was composed ofal (148 kDa) and a2 (129 kDa) chain and could bind paper, wood and foam sheet.