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Of Human Diseases (of + human_diseases)

Distribution by Scientific Domains
Life Sciences57%
Medical Sciences28%

Kinds of Of Human Diseases

  • variety of human diseases
    		•

    Selected Abstracts

    Multiplex primer extension analysis for rapid detection of major European mitochondrial haplogroups

    ELECTROPHORESIS, Issue 19 2006
    Martina Wiesbauer
    Abstract The evolution of the human mitochondrial genome is reflected in the existence of ethnically distinct lineages or haplogroups. Alterations of mitochondrial DNA (mtDNA) have been instrumental in studies of human phylogeny, in population genetics, and in molecular medicine to link pathological mutations to a variety of human diseases of complex etiology. For each of these applications, rapid and cost effective assays for mtDNA haplogrouping are invaluable. Here we describe a hierarchical system for mtDNA haplogrouping that combines multiplex PCR amplifications, multiplex single-base primer extensions, and CE for analyzing ten haplogroup-diagnostic mitochondrial single nucleotide polymorphisms. Using this rapid and cost-effective mtDNA genotyping method, we were able to show that within a large, randomly selected cohort of healthy Austrians (n,=,1172), mtDNAs could be assigned to all nine major European haplogroups. Forty-four percent belonged to haplogroup H, the most frequent haplogroup in European Caucasian populations. The other major haplogroups identified were U (15.4%), J (11.8%), T (8.2%) and K (5.1%). The frequencies of haplogroups in Austria is within the range observed for other European countries. Our method may be suitable for mitochondrial genotyping of samples from large-scale epidemiology studies and for identifying markers of genetic susceptibility. [source]

    Acetyl-coenzyme A carboxylases: Versatile targets for drug discovery

    JOURNAL OF CELLULAR BIOCHEMISTRY, Issue 6 2006
    Liang Tong
    Abstract Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism in humans and most other living organisms. They are attractive targets for drug discovery against a variety of human diseases, including diabetes, obesity, cancer, and microbial infections. In addition, ACCs from grasses are the targets of herbicides that have been in commercial use for more than 20 years. Significant progresses in both basic research and in drug discovery have been made over the past few years in the studies on these enzymes. At the basic research level, the crystal structures of the biotin carboxylase (BC) and the carboxyltransferase (CT) components of ACC have been determined, and the molecular basis for ACC inhibition by small molecules are beginning to be understood. At the drug discovery level, a large number of nanomolar inhibitors of mammalian ACCs have been reported and the extent of their therapeutic potential is being aggressively explored. This review summarizes these new progresses and also offers some prospects in terms of the future directions for the studies on these important enzymes. J. Cell. Biochem. 99: 1476,1488, 2006. © 2006 Wiley-Liss, Inc. [source]

    Emerging functions of the calpain superfamily of cysteine proteases in neuroendocrine secretory pathways

    JOURNAL OF NEUROCHEMISTRY, Issue 3 2007
    Joanne S. Evans
    Abstract The first calpain protease was discovered over 40 years ago now, yet despite the vast amount of literature that has subsequently emerged detailing their involvement in the pathophysiology of a variety of human diseases, it is only in the last decade that calpain-mediated actions along the secretory pathway have begun to emerge. However, the number of secretory pathway substrates identified and their diversity of function continues to grow. This review summarizes our current knowledge of calpain-mediated mechanisms of action that are pertinent to synaptic vesicle assembly and budding, cytoskeletal organization, endosomal recycling, and exocytotic membrane fusion. [source]

    Increased Acid Sphingomyelinase Activity in Peripheral Blood Cells of Acutely Intoxicated Patients With Alcohol Dependence

    ALCOHOLISM, Issue 1 2010
    Martin Reichel
    Background:, Acid sphingomyelinase (ASM; EC 3.1.4.12) hydrolyses membrane sphingomyelin into the bioactive lipid ceramide and is thus involved in different cellular processes such as differentiation, immunity, or cell death. Activation of ASM has been reported in particular in conjunction with the cellular stress response to several external stimuli, and increased ASM activity was observed in a variety of human diseases. Ethanol-induced activation of ASM has been observed in different cell culture systems, thus raising the question about the effect of alcohol intoxication in human subjects on ASM activity in vivo. Methods:, We determined ASM activity in peripheral blood mononucleated cells of 27 patients suffering from alcohol dependence. Patients were classified according to their blood alcohol concentration at admission, and ASM activity was determined repeatedly from all patients during alcohol withdrawal. Results:, Acutely intoxicated patients displayed significantly higher ASM activity than patients in early abstinence (Mann,Whitney U test: Z = , 2.6, p = 0.009). ASM activity declined in acutely intoxicated patients to normal values with the transition from the intoxicated state to early abstinence (Wilcoxon test: Z = ,2.7, p = 0.007). At the end of withdrawal, ASM activity was significantly increased again compared to the early phase of abstinence in both patient groups (Wilcoxon test: Z = ,2.691, p = 0.007 and Z = ,2.275, p = 0.023, respectively). Conclusions:, Alcohol-induced activation of ASM occurs in human subjects and might be responsible for deleterious effects of ethanol intoxication. Chronic alcohol abuse may induce deregulation of sphingomyelin metabolism in general, and this impairment may cause side effects during withdrawal from alcohol. [source]

    Peptide-based radiopharmaceuticals: Future tools for diagnostic imaging of cancers and other diseases

    MEDICINAL RESEARCH REVIEWS, Issue 3 2004
    S.M. Okarvi
    Abstract An Erratum has been published for this article in Medicinal Research Reviews 2004;24:685,686. Small synthetic receptor-binding peptides are the agents of choice for diagnostic imaging and radiotherapy of cancers due to their favorable pharmacokinetics. Molecular modification techniques permit the synthesis of a variety of bioactive peptides with chelating groups, without compromising biological properties. Various techniques have been developed that allow efficient and site-specific labeling of peptides with clinically useful radionuclides such as 99mTc, 123I, 111In, and 18F. Among them, 99mTc is the radionuclide of choice because of its excellent chemical and imaging characteristics. Recently, many 99mTc-labeled peptides have proven to be useful imaging agents. Beside 99mTc-labeled peptides, several peptides radiolabeled with 111In and 123I have been prepared and characterized. In addition, 18F-labeled peptides hold clinical potential due to their ability to quantitatively detect and characterize a variety of human diseases using positron-emission tomography. The availability of this wide range of peptides labeled with different radionuclides offers multiple diagnostic and therapeutic applications. Various receptors are over-expressed in particular tumor types and peptides binding to these receptors can be used to visualize tumor lesions scintigraphically. Thus, radiolabeled peptides have potential use as carriers for the delivery of radionuclides to tumors, infarcts, and infected tissues for diagnostic imaging and radiotherapy. Many radiolabeled peptides are currently under investigation to determine their potential as imaging agents. These peptides are designed mainly for thrombus, tumor, and infection/inflammation imaging. This article presents recent developments in small synthetic peptides for imaging of thrombosis, tumors, and infection/inflammation. © 2004 Wiley Periodicals, Inc. Med Res Rev, 24, No. 3, 357,397, 2004 [source]

    Synthesis and assembly of a full-length human monoclonal antibody in algal chloroplasts

    BIOTECHNOLOGY & BIOENGINEERING, Issue 4 2009
    Miller Tran
    Abstract Monoclonal antibodies can be effective therapeutics against a variety of human diseases, but currently marketed antibody-based drugs are very expensive compared to other therapeutic options. Here, we show that the eukaryotic green algae Chlamydomonas reinhardtii is capable of synthesizing and assembling a full-length IgG1 human monoclonal antibody (mAb) in transgenic chloroplasts. This antibody, 83K7C, is derived from a human IgG1 directed against anthrax protective antigen 83 (PA83), and has been shown to block the effects of anthrax toxin in animal models. Here we show that 83K7C heavy and light chain proteins expressed in the chloroplast accumulate as soluble proteins that assemble into complexes containing two heavy and two light chain proteins. The algal-expressed 83K7C binds PA83 in vitro with similar affinity to the mammalian-expressed 83K7C antibody. In addition, a second human IgG1 and a mouse IgG1 were also expressed and shown to properly assemble in algal chloroplast. These results show that chloroplasts have the ability to fold and assemble full-length human mAbs, and suggest the potential of algae as a platform for the cost effective production of complex human therapeutic proteins. Biotechnol. Bioeng. 2009; 104: 663,673 © 2009 Wiley Periodicals, Inc. [source]

    FUNCTIONAL DIVERSITY OF MAMMALIAN TYPE 2C PROTEIN PHOSPHATASE ISOFORMS: NEW TALES FROM AN OLD FAMILY

    CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY, Issue 2 2008
    Gang Lu
    SUMMARY 1The Type 2C protein phosphatases (PP2C) represent a highly conserved gene family in the mammalian genome. Recent studies have revealed that PP2C isoforms possess unique patterns of tissue and subcellular distribution associated with diverse functionalities. 2The functional importance of PP2C isoforms has been shown in a plethora of signalling networks controlling cell differentiation, proliferation, growth, survival and metabolism. However, little is known about the regulatory mechanisms of PP2C at the molecular level. It is uncertain how PP2C isoforms are recruited, activated and inactivated during signalling transduction processes. 3In the present paper, an overview of the critical functions of individual PP2C isoforms in regulating cellular signalling events will be provided, along with our perspectives on the challenging issues to be addressed. It is clear that a better understanding of the complex biological effects elicited by specific signalling pathways involving PP2C isoforms has great potential for developing novel therapies for a variety of human diseases, including cancer, diabetes and neural disorders, as well as cardiovascular diseases. [source]