Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
566.8±50.0 °C at 760 mmHg
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Reovirus serotype 1, strain Lang (T1/L), a well characterized enteric virus, elicits humoral and cellular immune responses in mice. Although orally and intradermally induced infections generate comparable reovirus-specific serum antibody titers, little is known about the effects of the route of infection on the systemic immunoglobulin G (IgG) response. To assess whether the route of exposure affects virus-specific humoral immunity, we infected various strains of mice with reovirus T1/L by the oral or intradermal routes. At day 10 following infection, virus-specific serum antibody titers and IgG subclasses were determined by enzyme-linked immunosorbent assay. Serum IgG2a and IgG2b antibodies were detected in all mouse strains independent of the route of infection. Mice of the H-2d haplotype that received an intradermal infection also had high levels of reovirus-specific serum IgG1. This dichotomy of responses was not associated with differences in the types of cytokine produced by draining peripheral lymph nodes. However, peripheral lymph node lymphocytes from C3H mice produced significantly higher levels of gamma interferon than did BALB/c, C57BL/6, and B10.D2 mice. Additionally, peripheral lymph node lymphocytes from all strains of mice produced only low levels of interleukin-5, with no detectable level of interleukin-4 or interleukin-6. Analysis of specific antibody at inductive sites of the immune response showed that orally infected Peyer’s patches produced predominantly IgA and intradermally infected peripheral lymph nodes produced predominantly IgG2a. Western blot (immunoblot) analysis showed that virus-specific IgA, IgG1, and IgG2a reacted with reovirus structural proteins. These data suggest that the route of infection affects the isotype and IgG subclasses, but not the antigen specificity, of the local antibody response. In addition, virus-specific IgG1 generated following an intradermally induced infection is linked to the H-2d major histocompatibility complex haplotype.
Effects of the route of infection on immunoglobulin G subclasses and specificity of the reovirus-specific humoral immune response.
A S Major and C F Cuff
Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulation, in particular through the modification of histones and nuclear transcription regulators. We show that lysine acetylation is a prevalent modification in enzymes that catalyze intermediate metabolism. Virtually every enzyme in glycolysis, gluconeogenesis, the tricarboxylic acid (TCA) cycle, the urea cycle, fatty acid metabolism, and glycogen metabolism was found to be acetylated in human liver tissue. The concentration of metabolic fuels, such as glucose, amino acids, and fatty acids, influenced the acetylation status of metabolic enzymes. Acetylation activated enoyl-coenzyme A hydratase/3-hydroxyacyl-coenzyme A dehydrogenase in fatty acid oxidation and malate dehydrogenase in the TCA cycle, inhibited argininosuccinate lyase in the urea cycle, and destabilized phosphoenolpyruvate carboxykinase in gluconeogenesis. Our study reveals that acetylation plays a major role in metabolic regulation.
Regulation of Cellular Metabolism by Protein Lysine Acetylation
Shimin Zhao,1,2 Wei Xu,1,2,* Wenqing Jiang,1,2,* Wei Yu,1,2 Yan Lin,2 Tengfei Zhang,1,2 Jun Yao,3 Li Zhou,4 Yaxue Zeng,4 Hong Li,5 Yixue Li,6 Jiong Shi,6 Wenlin An,7 Susan M. Hancock,7 Fuchu He,3 Lunxiu Qin,5 Jason Chin,7 Pengyuan Yang,3 Xian Chen,3,4 Qunying Lei,1,2,8 Yue Xiong,1,2,4,† and Kun-Liang Guan1,2,8,9,†
2011 Dec 7.
Type IIa von Willebrand’s disease (vWd) has been characterized by the absence of the largest and a reduction in the intermediate-sized multimers of the plasma and platelet von Willebrand factor (vWf) and by the diminished response of the platelet-rich plasma of these patients to ristocetin. Other recently demonstrated abnormalities include the presence of an abnormal triplet structure of vWf. We have studied the plasma and platelets from three patients with this form of vWd and have found that both their plasma and platelets manifest the previously described abnormalities. Because of the heterogeneity of the multimeric structure of the vWf in these patients, we considered the possibility that postsynthetic events may have modified the vWf. When blood was collected in 5 mM EDTA or 5 mM EDTA/leupeptin/N-ethylmaleimide, the abnormal multimeric structure of the plasma and platelet vWf was partially normalized in that the intermediate and the largest vWf multimers were increased, the abnormal multimer structure was no longer as apparent, and the fastest migrating band (an abnormality seen only in the type IIa vWd plasma and platelets) disappeared. The enzymatic activity responsible for this degradation can be classified as a calcium-dependent protease. Studies of normal radiolabeled vWf incubated with platelet lysates from normal subjects and these patients revealed that the patients’ platelets did not contain increased amounts of calcium-dependent protease activity as assessed by degradation of normal vWf. These data suggest that patients with type IIa vWd synthesize an abnormal vWf protein that is susceptible to in vitro proteolytic degradation and that proteolytic degradation can play a significant role in the phenotypic expression of vWd by modifying the plasma and platelet vWf multimeric structure.
In vitro correction of the abnormal multimeric structure of von Willebrand factor in type IIa von Willebrand's disease.
H R Gralnick, S B Williams, L P McKeown, P Maisonneuve, C Jenneau, Y Sultan, and M E Rick