中国叉茎管蚜蝇属及一新种记述(双翅目:食蚜蝇科)(英语)

叉茎管蚜蝇属Tigridemyia与墨管蚜蝇属 Mesembrius和美管蚜蝇属 Mallota形态相似,过去曾被作为后二属的亚属.但此属的雄性外生殖器阳茎的射精管端部4分叉与墨管蚜蝇属和美管蚜蝇属区别明显,因此,其属地位应予肯定.作者在整理中国的食蚜蝇标本时,发现该属1新种,刺腿叉茎管蚜蝇Tigridemyia acanthogemurilis sp.nov,加之过去已记录的1种,我国已知叉茎管蚜蝇属2种.本文描述了新种,并给出了中国已知2种的检索表和形态特征图及其分布.模式标本保存于华南农业大学植保系昆虫标本室.     

18β-甘草次酸抑制微动脉平滑肌细胞外向电流

本文旨在观察18β-甘草次酸(18β-glycyrrhetinic acid,18βGA)对微动脉平滑肌细胞膜电流的影响。分离出豚鼠小脑前下动脉(anterior inferior cerebellar artery,AICA)和肠系膜动脉(mesenteric artery,MA)后,用酶消化法制备单个血管平滑肌细胞(vascular smooth muscle cells,VSMCs),应用全细胞膜片钳技术记录平滑肌细胞外向电流的变化。结果显示:(1)1mmol/L4氨基吡啶(4-aminopyridine,4-AP)和1mmol/L tetraethylammonium(TEA)都可以部分抑制微动脉平滑肌细胞的外向电流。(2)18βGA电压和浓度依赖性地抑制微动脉平滑肌细胞外向电流。18βGA主要抑制0～+40mV电压区间的激活电流,其中对+40mV激活电流的抑制作用最强。10、30和100μmol/L18βGA对AICA平滑肌细胞外向电流(+40mV)的抑制率分别为(25.3±7.1)%、(43.1±10.4)%和(68.4±3.9)%,对MA平滑肌细胞外向电流(+40mV)的抑制率分别为(13.2±...     

Activation of PPAR-β/δ Attenuates Brain Injury by Suppressing Inflammation and Apoptosis in a Collagenase-Induced Intracerebral Hemorrhage Mouse Model

Neurochemical Research - Brain injury has been proposed as the major cause of the poor outcomes associated with intracerebral hemorrhage (ICH). Emerging evidence indicates that the nuclear...     

新疆苦豆子根瘤菌的数值分类研究

苦豆子(Sophora alopecuroides)对于干旱荒漠地区的畜牧业发展有着非常重要的意义,其生长特性与根瘤菌有密切关系。我们对分离自新疆苦豆子根瘤的67株根瘤菌及36个模式菌株进行了118项表型性状的测定,包括唯一碳源利用、唯一氮源利用、对抗生素和染料的抗性、耐盐性、初始pH值生长范围、生长温度范围及石蕊牛奶反应、氧化酶、过氧化氢酶和脲酶。对测定结果用聚类分析方法进行了分析,获得数值分类树状图。结果表明：新疆苦豆子根瘤菌在碳氮源利用、抗生素敏感性以及对染料的抗性程度等方面存在着差异。新疆苦豆子根瘤菌能耐受低温,并具有较强的耐盐、碱能力,所有供试菌株均能在初始pH值为9－12的YMA培养基上生长,92.5％的菌株能耐受3.0％的NaCl,91.0％的菌株能耐受4.0％的NaCl,有18株菌甚至能耐受5.0％和6.0％的NaCl。聚类结果表明, 在84.8%的相似性水平上,67个供试菌株构成了4个新的表观群,第Ⅰ、Ⅱ、Ⅲ、Ⅳ类群分别有21、7、4、3个菌株,中心菌株分别为NWBC152、NWTKX101、NWYJS12、NWLP112。此外,数值分类结果还表明,苦豆子根瘤菌与模式菌株的相似性较低,它们所形成的4个独立群可能有新种出现。     

巴西蘑菇原种培养基的筛选

以麦草、稻草、棉籽壳、玉米秸、木屑、麦粒、玉米粒和麦麸为原料 ,从 2 0种培养基中筛选出 2种适合巴西蘑菇菌丝生长的原种培养基。用这 2种培养基生产的菌种 ,菌丝粗壮、洁白、浓密 ,萌发快。     

Sustained expression of MCP-1 induced low wall shear stress loading in conjunction with turbulent flow on endothelial cells of intracranial aneurysm

Shear stress was reported to regulate the expression of AC007362, but its underlying mechanisms remain to be explored. In this study, to isolate endothelial cells of blood vessels, unruptured and ruptured intracranial aneurysm (IA) tissues were collected from IA patients. Subsequently, quantitative real-time PCR (qRT-PCR), Western blot and luciferase assay were performed to investigate the relationships between AC007362, miRNAs-493 and monocyte chemoattractant protein-1 (MCP-1) in human umbilical vein endothelial cells (HUVECs) exposed to shear stress. Reduced representation bisulphite sequencing (RRBS) was performed to assess the level of DNA methylation in AC007362 promoter. Accordingly, AC007362 and MCP-1 were significantly up-regulated while miR-493 was significantly down-regulated in HUVECs exposed to shear stress. AC007362 could suppress the miR-493 expression and elevate the MCP-1 expression, and miR-493 was shown to respectively target AC007362 and MCP-1. Moreover, shear stress in HUVECs led to the down-regulated DNA methyltransferase 1 (DNMT1), as well as the decreased DNA methylation level of AC007362 promoter. Similar results were also observed in ruptured IA tissues when compared with unruptured IA tissues. In conclusion, this study presented a deep insight into the operation of the regulatory network of AC007362, miR-493 and MCP-1 upon shear stress. Under shear stress, the expression of AC007362 was enhanced by the inhibited promoter DNA methylation, while the expression of MCP-1 was enhanced by sponging the expression of miR-493.     

Molecular evolution and structural analysis of the Ca(2+) release-activated Ca(2+) channel subunit, Orai

Depletion of intracellular Ca(2+) stores evokes Ca(2+) entry across the plasma membrane by inducing Ca(2+) release-activated Ca(2+) (CRAC) currents in many cell types. Recently, Orai and STIM proteins were identified as the molecular identities of the CRAC channel subunit and the endoplasmic reticulum Ca(2+) sensor, respectively. Here, extensive database searching and phylogenetic analysis revealed several lineage-specific duplication events in the Orai protein family, which may account for the evolutionary origins of distinct functional properties among mammalian Orai proteins. Based on similarity to key structural domains and essential residues for channel functions in Orai proteins, database searching also identifies a putative primordial Orai sequence in hyperthermophilic archaeons. Furthermore, modern Orai appears to acquire new structural domains as early as Urochodata, before divergence into vertebrates. The evolutionary patterns of structural domains might be related to distinct functional properties of Drosophila and mammalian CRAC currents. Interestingly, Orai proteins display two conserved internal repeats located at transmembrane segments 1 and 3, both of which contain key amino acids essential for channel function. These findings demonstrate biochemical and physiological relevance of Orai proteins in light of different evolutionary origins and will provide novel insights into future structural and functional studies of Orai proteins.     

Molecular evolution and functional divergence of the Ca(2+) sensor protein in store-operated Ca(2+) entry: stromal interaction molecule

Receptor-mediated Ca(2+) signaling in many non-excitable cells initially induces Ca(2+) release from intracellular Ca(2+) stores, followed by Ca(2+) influx across the plasma membrane. Recent findings have suggested that stromal interaction molecules (STIMs) function as the Ca(2+) sensor to detect changes of Ca(2+) content in the intracellular Ca(2+) stores. Human STIMs and invertebrate STIM share several functionally important protein domains, but diverge significantly in the C-terminus. To better understand the evolutionary significance of STIM activity, phylogenetic analysis of the STIM protein family was conducted after extensive database searching. Results from phylogeny and sequence analysis revealed early adaptation of the C-terminal divergent domains in Urochordata, before the expansion of STIMs in Vertebrata. STIMs were subsequently subjected to one round of gene duplication as early as in the Euteleostomi lineage in vertebrates, with a second round of fish-specific gene duplication. After duplication, STIM-1 and STIM-2 molecules appeared to have undergone purifying selection indicating strong evolutionary constraints within each group. Furthermore, sequence analysis of the EF-hand Ca(2+) binding domain and the SAM domain, together with functional divergence studies, identified critical regions/residues likely underlying functional changes, and provided evidence for the hypothesis that STIM-1 and STIM-2 might have developed distinct functional properties after duplication.