Search Results - (Author, Cooperation:V. E. Anderson)

2013-09-24

Nature Publishing Group (NPG)

0028-0836

1476-4687

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

5' Untranslated Regions/genetics ; Base Sequence ; Escherichia coli/*enzymology/genetics ; Escherichia coli Proteins/chemistry/genetics/*metabolism ; Kinetics ; Nucleic Acid Conformation ; RNA Precursors/chemistry/genetics/metabolism ; RNA, Bacterial/chemistry/genetics/metabolism ; RNA, Transfer/chemistry/genetics/*metabolism ; RNA, Transfer, Met/chemistry/genetics/metabolism ; Ribonuclease P/chemistry/genetics/*metabolism ; Substrate Specificity

1471-4159

Blackwell Publishing Journal Backfiles 1879-2005

Medicine

Abstract: Cytoplasmic inclusion bodies that are accumulations of neurofilaments are the pathological hallmark of many neurodegenerative diseases and have been produced in transgenic mice by overexpression of mouse (NF-L and NF-M; light and medium chains, respectively) and human (NF-M and NF-H; medium and heavy chains, respectively) neurofilament subunits. This report describes a neuronal culture model in which human NF-L was overexpressed to produce cytoplasmic accumulations of neurofilaments within cell bodies concomitant with the collapse of the endogenous neurofilament network. Electron microscopy showed that, within accumulations, neurofilaments retained a filamentous structure. The culture model thus provides a novel system in which the effect on neurofilament accumulations of manipulating protein phosphorylation can be studied. Treatment of cells containing neurofilament accumulations with bisindolylmaleimide, a specific protein kinase C inhibitor, resulted in regeneration of the filamentous network; this effect was not due to a change in the level of transfected NF-L expression. These findings lend support to the suggestion that an impairment in the regulation of protein phosphorylation may lead to the accumulation of neurofilaments seen in neurodegenerative disease.

Electronic Resource

1476-4687

Nature Archives 1869 - 2009

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

[Auszug] SIR - Oxidative stress results in the formation of free carbonyls derived from lipids, proteins, carbohydrates and nucleic acids1. For example, metal-catalysed 'site- specific' oxidation of several amino-acid side-chains produces aldehydes or ketones2, and peroxidation of lipids gener- ates ...

Electronic Resource

1573-7381

Springer Online Journal Archives 1860-2000

Medicine

Summary To determine the rate and routes of removal of lysosomal, lipofuscin-like dense bodies from neurons, the protease inhibitor, leupeptin, was infused into the lateral ventricle of rats for up to nine days. After seven days a number of animals were then allowed to recover. The formation and later disappearance of dense bodies was followed by morphology and immunocytochemistry. After 48 h of infusion lysosomal dense bodies in large numbers appeared in cortical, hippocampal and cerebellar neurons, which also showed increased ubiquitin immunoreactivity, as well as in other cell types. By 3–4 days ubiquitin-immunoreactive dense bodies were equally distributed between neurons and astroglia. After seven to nine days of infusion ubiquitin immunoreactive dense bodies filled neuronal perikarya, dendrites and expanded initial segments of many axons and were abundant in glial processes. All dense bodies studied by electron microscopy were ubiquitin immunoreactive. After four days of recovery dense bodies were markedly fewer in neuronal perikarya, and virtually all were now within glial processes. From 7 to 28 days of recovery, when most neurons appeared normal, lipofuscin bodies remained in axon initial segments and in reduced numbers in glial processes, particularly around blood vessels and beneath the pia of hippocampus and of cerebellar cortex. Thus, neurons probably have a steady passage of short lived proteins through the lysosomal excretory pathway. The observed temporal sequence of events on recovery suggests that secondary lysosomes probably pass rapidly from neuronal perikarya and dendrites to astrocytes and thus to the vascular bed or pia-arachnoid. The mechanism of cell-to-cell transfer is not clear from this study.

Electronic Resource

1573-3297

mental retardation ; maternal effect ; uterine environment ; genetics ; pedigrees

Springer Online Journal Archives 1860-2000

Biology

Psychology

Abstract The frequency of mental retardation in the offspring of maternal aunts of retarded probands is compared with the frequency in offspring of other aunts or uncles of the same probands. There is no support for inherited uterine inadequacy as an explanatory factor for mental retardation.

Electronic Resource

1075-4261

Chemistry ; Analytical Chemistry and Spectroscopy

Wiley InterScience Backfile Collection 1832-2000

Biology

Physics

The Raman bands associated with different rotamers of hexadienoyl ethyl thiolester, CH3—CH=CH—CH=CH—C(=O)—S—CH2—CH3, have been partially assigned using recent conformational and vibrational spectroscopic analyses of ethyl thiocrotonate CH3—CH=CH—C(=O)—S—CH2—CH3.1 In particular, rotational isomers involving the =CH—C(=O) and —S—CH2— axes have been characterized. The assignment of the vibrational modes of different conformers of hexadienoyl ethyl thiolester was further facilitated by variable-temperature (+20°C to -90°C) Raman studies on the neat thiolester. High-quality Raman spectra of hexadienoyl-coenzyme A bound to the enzyme enoyl-CoA hydratase were obtained using 647.1-nm excitation and Raman difference spectroscopy. The findings provided by analysis of the ethyl thiolester model compound enable us to conclude that conformational selection occurs for the CoA analog upon binding, resulting in the presence of a single-rotamer population in the hexadienoyl moiety on the enzyme. The hexadienoyl-CoA was labeled with 18O in the C=O group and, separately, with 13C at the C2 position. A comparison of Raman data for the free and bound ligands, isotopically labeled and unlabeled, indicates that strong π-electron polarization occurs in only a part of the hexadienoyl chain, viz, in the C=C—C=O fragment, upon binding. The polarization gives rise to important contributions from canonical (resonance) forms of the type —C+—C=C—O-. In contrast, the C4=C5 linkage (where the carbon atom numbering is C6—C5=C4—C3=C2—C1=O) seems little perturbed in the bound ligand. The causes and mechanistic advantage of the observed localized polarization are discussed. © 1995 John Wiley & Sons, Inc.

9 Ill.

Electronic Resource