疏花毛萼香茶菜的二萜成分

从疏花毛萼香茶菜叶的乙醚提取物中一共分得七个二萜化合物,其中四个经各项光谱数据证明它们分别为毛萼乙素(1),毛萼晶甲(2),毛萼晶乙(3)和冬凌草素(4)。     

毛萼鞘蕊花甲素的结构

从毛萼鞘蕊花(Coleus esquirolii(L(?)vl. )Dunn.)的茎、叶中分离鉴定了一个新的二萜化合物,毛萼鞘蕊花甲素(对映-17-乙酰氧基-贝壳杉烷-16β-醇),和三个已知化合物,对映-贝壳杉烷-16p,17-二醇,齐墩果酸和β-谷甾醇。     

毛萼香茶菜中的三个新的对映—贝壳杉烷型二萜

从采自云南省江川县的毛萼香茶菜的甲醇提取物中分离得到３个新的６,７－螺断－对映－贝壳杉烷型二萜;表毛萼甲素,毛萼晶Ｎ和毛萼晶Ｏ,同时还分离到２个已知化合物,毛萼甲素及毛萼晶Ｌ,并修正了毛萼甲素的结构。     

毛萼香茶菜二萜化合物的高效液相色谱定量分析

本文报道用HPLC分离测定毛萼香茶菜(Rabdosia eriocalyx)中的二萜化合物。总二萜提取物在zorbax ODS柱上,用甲醇-水(70:30)作流动相,毛萼晶乙、毛萼晶丙等五个化合物在18分钟内能很好分离。以odonicin为内标,用峰面积比测定各组份的含量。结果符合一般含量测定的要求,此法可作为香茶菜二萜化合物一类生物活性物质的分析及发现新二萜化合物的前导性有效筛选手段。     

毛萼香茶菜中的新二萜化合物——毛萼晶P

从毛萼香茶菜的叶的甲醇提取物中分离得到两个二萜化合物,ｃｏｅｔｓｏｉｄｉｎＡ和毛萼晶Ｐ,它是目前从香茶菜属分离到的仅有的两个Ｂ环具有α,β－不饱和酮结构的对映－贝壳杉烷型二萜事物,其中毛萼晶Ｐ为新化合物     

黔产毛萼香茶菜二萜成分

综合利用硅胶、凝胶、MCI等柱层析方法从毛萼香茶菜中进行分离、纯化到10个二萜化合物,结合MS、1H NMR、13C NMR和相关文献资料分别鉴定为6-乙酰基-毛萼晶B(1)、毛萼晶O(2)、12-hydroxydehydro-abietic acid(3)、Neorabdosin(4)、毛萼晶D(5)、毛萼晶E(6)、毛萼晶B(7)、毛萼晶N(8)、Coetsoidin A(9)、毛萼晶L(10)。其中化合物1为新天然产物,3为首次从该植物中分离。     

疏花毛萼香茶菜中一新的对映-贝壳杉烷型二萜

从疏花毛萼香茶菜（Ｉｓｏｄｏｎ ｅｒｉｏｃａｌｙｘ ｖａｒ．ｌａｘｉｆｌｏｒａ）叶中分离得到一新的对映－贝壳杉烷型二萜,命名为疏花丁素（１）,通过波谱方法鉴定了它的结构。此外,还分离得到６个已知对映－贝壳杉烷型二萜化合物：疏花甲素（２）,毛萼晶Ａ－Ｃ（３－５）和Ｑ（６）,毛萼乙素（７）,以及ｃｉｒｓｉｍａｒｉｔｉｎ（８）和２α－羟基乌索酸（９）。     

毛萼香茶菜的新二萜化合物,毛萼晶甲-戊的结构

香茶菜属(Rabdosia)植物中的二萜化合物具有多种生理活性,如抗肿瘤,抗菌,抑制线粒体的吸呼作用和昆虫的生长等。在我们研究该属植物生理活性成分的课题中,我们从云南省丽江县蟠龙公社金沙江河谷地区产毛萼香茶菜〔Rabdosia eriocalyx(Dunn)Hara〕叶的乙醇提取物中分得七个结晶化合物,其中五个为新化合物,命名为毛萼晶甲一戊(maoecrystal A-E),另外两个为已知化合物毛萼甲素(eriocalyxinA)和乙素(eriocalyxin B)。     

绣线菊碱H,I及O的化学结构

绣线菊碱Ｈ,Ｉ,Ｏ为Ａｔｉｓｉｎｅ型的新二匝生物碱,从毛萼绣线菊根中分离得到。本文根据波谱解析及化学转换,分别测定了它们的化学结构。     

中国爵床科—新记录种——毛萼爵床

报道中国爵床-(Acanthaceae)爵床属—新记录种——毛萼爵床(Justicia poilanei Benoist).该种分布于云南南部石灰岩地区,在标本馆长期被鉴定为野靛棵(Justicia patentiflora Hemsl.),但与后者的区别在于它的花冠长约2 cm,花萼裂片三角状卵形和花药基部不具芒状附...     

Phosphorylation of the B1 (CD20) molecule by normal and malignant human B lymphocytes

The B1 molecule (CD20) is a phosphoprotein found only on B lymphocytes. Multiple isoforms of the B1 molecule are expressed with Mr of 33,000, B1(33) and Mr of 34,500-36,000, B1(35). In this study it was found that nonproliferating B cells did not incorporate 32PO4 into B1 although phosphorylated class I histocompatibility molecules were easily detected. In contrast B1 isolated from proliferating or malignant B cells or B cell lines was heavily phosphorylated. Cross-linking B1 on the cell surface by antibody resulted in enhanced phosphorylation of B1 as did exposure to phorbol esters, and the membrane permeable diacylglycerol analog 1,2,-dioctanoylglyceron. B1(33) and B1(35) produced identical peptide maps following limited proteinase digestion. However, B1(35) contained both phosphoserine and phosphothreonine, while B1(33) only contained phosphoserine. In addition alkaline phosphatase was able to remove the phosphate residue(s) that resulted in generation of the B1(35) form of B1 but was unable to remove the phosphorylation of B1(33). These results suggest that phosphorylation of B1 molecules is associated with proliferation and that the different Mr forms of B1 result from the phosphorylation of B1 at different sites. Also, the finding that antibody binding to B1 generated a transmembrane signal may explain why antibody binding to B1 alters B cell function.     

Induction of B1 receptors in streptozotocin diabetic rats: possible involvement in the control of hyperglycemia-induced glomerular Erk 1 and 2 phosphorylation

We investigated the effects of a 3-week treatment with various combinations of angiotensin-converting enzyme inhibitor (ACEI) and B1 and B2 bradykinin receptor (B1R and B2R) antagonists (B1A and B2A) and AT1 receptor antagonist on ERK 1 and 2 phosphorylation in isolated glomeruli from streptozotocin-treated diabetic rats (STZ rats). Body weight, glycemia, and blood pressure were monitored. The rats were divided into nine groups: (1) control; and groups 2-9 were STZ treated with (3) insulin, (4) ACEI, (5) ACEI + B1A, (6) ACEI + B2A, (7) B2A, (8) B1A, (9) AT1 antagonist. ERK 1 and 2 phosphorylation and expression of B1R and B2R were assessed by Western blot analysis. ERK 1 and 2 phosphorylation was higher in STZ rats; this activation was normalized by insulin and reduced by ACEI but not by AT1 antagonist. The reduction of ERK 1 and 2 phosphorylation by the ACEI was reversed by B1A and B2A. The induction of B1R was confirmed by increased expression of mRNA and B1 receptor protein. Since ERK 1 and 2 phosphorylation is an early event in the induction of matrix secretion and hyperproliferation associated with diabetic nephropathy, activation of B1R and B2R appears to be a useful pharmacological target in the management of this pathology.     

Role of bradykinin B2 and B1 receptors in the local, remote, and systemic inflammatory responses that follow intestinal ischemia and reperfusion injury

The administration of bradykinin may attenuate ischemia and reperfusion (I/R) injury by acting on B(2)Rs. Blockade of B(2)R has also been shown to ameliorate lesions associated with I/R injury. In an attempt to explain these contradictory results, the objective of the present work was to investigate the role of and interaction between B(1) and B(2) receptors in a model of intestinal I/R injury in mice. The bradykinin B(2)R antagonist (HOE 140) inhibited reperfusion-induced inflammatory tissue injury and delayed lethality. After I/R, there was an increase in the expression of B(1)R mRNA that was prevented by HOE 140. In mice that were deficient in B(1)Rs (B(1)R(-/-) mice), inflammatory tissue injury was abrogated, and lethality was delayed and partially prevented. Pretreatment with HOE 140 reversed the protective anti-inflammatory and antilethality effects provided by the B(1)R(-/-) phenotype. Thus, B(2)Rs are a major driving force for B(1)R activation and consequent induction of inflammatory injury and lethality. In contrast, activation of B(2)Rs may prevent exacerbated tissue injury and lethality, an effect unmasked in B(1)R(-/-) mice and likely dependent on the vasodilatory actions of B(2)Rs. Blockade of B(1)Rs could be a more effective strategy than B(2) or B(1)/B(2) receptor blockade for the treatment of the inflammatory injuries that follow I/R.     

Synthesis of Messenger Ribonucleic Acid After Bacteriophage T1 Infection

Synthesis of host-specific and phage-specific messenger ribonucleic acid (mRNA) was studied in bacteria infected by unmodified (T1 . B) or modified [T1 . B(P1)] bacteriophage T1. In a "standard" infection of Escherichia coli B by T1 . B (no host-controlled modification involved), the rate and amount of T1 mRNA synthesis was intermediate between those values reported for infections by a virulent phage such as T4 or a temperate phage such as lambda. The initial rate of mRNA synthesis was slightly increased after T1 . B(P1) infection of E. coli B in comparison with T1 . B infection of the same host. Little or no phage mRNA synthesis could be detected in T1 . B infection of E. coli B(P1). Phage mRNA synthesis in T1 . B(P1)-infected E. coli B(P1) cells was approximately the same in amount as that seen in T1 . B(P1) infection of E. coli B. Synthesis of host-specific mRNA continued throughout the latent period in all infections studied. However, the enzyme beta-galactosidase could not be induced, except after T1 . B infection of E. coli B(P1). In an attempt to understand the apparent differences in mRNA synthesis after infection of E. coli B by phages T1 . B or T1 . B(P1), the effect of altered T1 deoxyribonucleic acid (DNA) methylation on mRNA synthesis was studied. Methyl-deficient T1 DNA, made in cells infected with ultraviolet-irradiated phage T3, inhibited (14)C-uridine incorporation more strongly than normal T1. One passage of methyl-deficient T1 through E. coli B restored uracil incorporation rates to those seen with ordinary T1. This suggests that methylation of T1 DNA can influence the rate of phage mRNA synthesis. However, attempts to relate the difference in mRNA synthesis seen between T1 . B and T1 . B(P1) in E. coli B to the activity of the P1 modification gene were not conclusive.     

Analysis of the non-covalent interaction between metal ions and the cysteine-rich domain of protein kinase C eta by electrospray ionization mass spectrometry

Effect of zinc and other metal ions on the folding of the protein kinase C (PKC) surrogate peptide (PKCeta-C1B) was analyzed intact under neutral conditions by electrospray ionization mass spectrometry (ESI-MS). ESI-MS spectrum of 64ZnCl(2)-folded PKCeta-C1B clearly showed that PKCeta-C1B coordinates specifically two atoms of zinc, and that the two thiol protons are lost in each zinc ion coordinate center. 113CdCl(2)-folded PKCeta-C1B also showed stoichiometry of two cadmium atoms that was proved by addition of EDTA. The dissociation constants of zinc- and cadmium-folded PKCeta-C1B in the phorbol 12,13-dibutyrate binding (PDBu) were similar (0.66 and 0.81 nM) with different B(max) values (46.4 and 71.4%). The difference would reflect higher coordination potency of cadmium ion that was demonstrated by ESI-MS when PKCeta-C1B was folded by 1:1 mixture of zinc and cadmium ions. In contrast, 63CuCl(2)-treated PKCeta-C1B did not show any copper-coordinated peak, instead a molecular mass less than 6 mass units smaller than that of apo-PKCeta-C1B was observed. The multiple charge mass envelope of copper-treated PKCeta-C1B shifted to that of the lower mass charge state like zinc-treated PKCeta-C1B. These data suggest that the copper treatment formed three intramolecular S-S bonds to abolish the PDBu binding of PKCeta-C1B.     

Influence of B Locus Blood Groups on Adult Mortality and Egg Production in the White Leghorn Chicken

The influence of the B locus blood group on adult viability and egg production was studied in two White Leghorn populations (S1 and S2) synthesized from inbred line crosses. Each line segregated for four B alleles. Four homozygotes and six heterozygotes were produced in each line over a five-year period, and for an additional three years tests on certain blood-group combinations were continued. A total of 4371 birds were included in the study. Greatest differences in blood groups were found in the S1 line, with the B(2) and B(21) alleles seemingly having favorable effects and with B(1) having unfavorable effects. The B(1) homozygote was consistently the lowest in egg production (53.2%) and highest adult mortality (40.4%). The relative spread in standard deviation units between the B(1) and B(2) homozygotes was more than three times greater in adult mortality than in egg production; B(2) was incompletely dominant to B(1). Within the S1 line, the superiority of the heterozygotes was mainly a consequence of the poor fitness of the B(1) homozygote, suggesting that in a random-mated population B(1) would be maintained only by mutation and not by a polymorphic mechanism.-Over the eight years of the experiment, adult viability of the B(1) homozygote improved 4.4% per year (P<0.05). Assuming this regression results from natural selection, either of two hypotheses can account for the results: (1) The B locus is pleiotropic with natural selection for many B modifiers, and (2) the B locus is neutral but linked to a major fitness locus.     

The human B1 bradykinin receptor exhibits high ligand-independent, constitutive activity. Roles of residues in the fourth intracellular and third transmembrane domains

The B1 bradykinin (BK) receptor (B1R) is a seven-transmembrane domain, G protein-coupled receptor that is induced by injury and important in inflammation and nociception. Here, we show that the human B1R exhibits a high level of ligand-independent, constitutive activity. Constitutive activity was identified by the increase in basal cellular phosphoinositide hydrolysis as a function of the density of the receptors in transiently transfected HEK293 cells. Several B1R peptide antagonists were neutral antagonists or very weakly efficacious inverse agonists. Constitutive B1R activity was further increased by alanine mutation of Asn(121) in the third transmembrane domain of the receptor (B1A(121)). This mutant resembled the agonist-preferred receptor state since it also exhibited increased agonist affinity and decreased agonist responsiveness. A dramatic loss of constitutive activity occurred when the fourth intracellular C-terminal domain (IC-IV) of the human B2 BK receptor subtype (B2R), which exhibits minimal constitutive activity, was substituted in either B1R or B1A(121) to make B1(B2ICIV) and B1(B2ICIV)A(121), respectively. Activity was partially recovered by subsequent alanine mutation of a cluster of two serines and two threonines in IC-IV of either B1(B2ICIV) or B1(B2ICIV)A(121), a cluster that is important for B2R desensitization. The ligand-independent, constitutive activity of B1R therefore depends on epitopes in both transmembrane and intracellular domains. We propose that the activity is primarily due to the lack of critical epitopes in IC-IV that regulate such activity.     

Biological Activity of Aflatoxin B2a

The toxicity of alfatoxin B(2a) (hydroxydihydro-aflatoxin B(1)) was studied in several biological systems. Aflatoxin B(2a) is the monohydroxylated derivative obtained from addition of water to the double bond of the terminal furan of B(1). Examination of the sensitivity of a group of microorganisms to B(2a) demonstrated that the inhibitory spectrum was similar to aflatoxin B(1). However, the toxicity of B(2a) was markedly lower than B(1), as measured by the initiation of bile duct hyperplasia in ducklings. Binding of aflatoxin to deoxyribonucleic acid (DNA) was determined by measuring the hypochromicity produced by the nucleic acid at 363 nm and the capacity of increasing amounts of DNA to quench the fluorescence of the toxin was also used as a measure of the binding of toxin to nucleic acid. These tests showed that the DNA-binding capacity of B(2a) was lower than B(1).     

High agonist-independent clearance of rabbit kinin B1 receptors in cultured cells

We hypothesized that the inducible kinin B(1) receptor (B(1)R) is rapidly cleared from cells when its synthesis subsides. The agonist-independent degradation of the rabbit B(1)Rs and related B(2) receptors (B(2)Rs) was investigated. Endocytosis of the B(1)R-yellow fluorescent protein (YFP) conjugate was more intense than that of B(2)R-green fluorescent protein (GFP) based on fluorescence accumulation in HEK 293 cells treated with a lysosomal inhibitor. The cells expressing B(1)R-YFP contained more GFP/YFP-sized degradation product(s) than those expressing B(2)R-GFP (immunoblot, antibodies equally reacting with both fluorescent proteins). The binding site density of B(1)R-YFP decreased in the presence of protein synthesis or maturation inhibitors (anisomycin, brefeldin A), whereas that of B(2)R-GFP remained constant. Wild-type B(1)Rs were also cleared faster than B(2)Rs in rabbit smooth muscle cells treated with metabolic inhibitors. Contractility experiments based on brefeldin A-treated isolated rabbit blood vessels also functionally support that B(1)Rs are more rapidly eliminated than B(2)Rs (decreased maximal effect of agonist over 2 h). The highly regulated B(1)R is rapidly degraded, relative to the constitutive B(2)R.     

Identification of a key region of kinin B(1) receptor for high affinity binding of peptide antagonists

To investigate the molecular basis for the specificity of ligand recognition in human kinin B(1) (B(1)R) and B(2) (B(2)R) receptors, we constructed a series of chimeric receptors by progressively replacing, from the N to the C terminus, the human B(2)R domains by their B(1) counterparts. The chimeric construct possessing the C-terminal tail and the transmembrane domain VII (TM VII) of the B(2)R (construct 6) displayed 7- and 20- fold decreased affinities for the B(1) agonist [(3)H]desArg(10)-kallidin (desArg(10)-KD) and the B(1) antagonist [(3)H]desArg(10)-[Leu(9)]-KD respectively, as compared with the wild-type B(1)R. Moreover, the substitution of the B(1) TM VII by its B(2) homologue TM increased the affinity for the pseudopeptide antagonists, Hoe140 and NPC 567. High affinity for desArg(10)-KD binding was fully regained when the B(2) residue Thr(287) was replaced in construct 6 by the corresponding B(1) Leu(294) residue. When the B(2) residue Tyr(295) was exchanged with the corresponding B(1) Phe(302), high affinity binding for both agonist and antagonist was recovered. Moreover, the L294T and F302Y mutant B(1)R exhibited 69- and 6.5-fold increases, respectively, in their affinities for the B(2) receptor antagonist, Hoe140. Therefore we proposed that Leu(294) and Phe(302) residues, which may not be directly involved in the binding of B(1)R ligands and, hence, their Thr(287) and Tyr(295) B(2) counterparts, are localized in a receptor region, which plays a pivotal role in the binding selectivity of the peptide or pseudopeptide kinin ligands.