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Human Cerebrospinal Fluid (human + cerebrospinal_fluid)
Selected AbstractsManganese speciation in human cerebrospinal fluid using CZE coupled to inductively coupled plasma MSELECTROPHORESIS, Issue 9 2007Bernhard Michalke Dr. Abstract The neurotoxic effects of manganese (Mn) at elevated concentrations are well known. This raises the question, which of the Mn species can cross neural barriers and appear in cerebrospinal fluid (CSF). CSF is the last matrix in a living human organism available for analysis before a compound reaches the brain cells and therefore it is assumed to reflect best the internal exposure of brain tissue to Mn species. A previously developed CE method was modified for separation of albumin, histidine, tyrosine, cystine, fumarate, malate, inorganic Mn, oxalacetate, ,-keto-glutarate, nicotinamide-dinucleotide (NAD), citrate, adenosine, glutathione, and glutamine. These compounds are supposed in the literature to act as potential Mn carriers. In a first attempt, these compounds were analyzed by CZE-UV to check whether they are present in CSF. The CZE-UV method was simpler than the coupled CZE-inductively coupled plasma (ICP)-dynamic reaction cell (DRC)-MS method and it was therefore chosen to obtain a first overview information. In a second step, the coupled method (CZE-ICP-DRC-MS) was used to analyze, in detail, which of the compounds found in CSF by CZE-UV were actually bound to Mn. Finally, 13 Mn species were monitored in CSF samples, most of them being identified: Mn-histidine, Mn-fumarate, Mn-malate, inorganic Mn, Mn-oxalacetate, Mn-,-keto glutarate, Mn-carrying NAD, Mn-citrate and Mn-adenosine. By far the most abundant Mn species was Mn-citrate showing a concentration of 0.7,±,0.13,µg,Mn/L. Interestingly, several other Mn species can be related to the citric acid cycle. [source] Separation and determination of carnosine-related peptides using capillary electrophoresis with laser-induced fluorescence detectionELECTROPHORESIS, Issue 3 2005Ying Huang Abstract A capillary electrophoresis (CE) method with laser-induced fluorescence (LIF) detection was developed for the separation and detection of carnosine-related peptides (carnosine, anserine, and homocarnosine). A sensitive and fluorogenic regent, 3-(4-carboxybenzoyl) quinoline-2-carboxaldehyde (CBQCA) was selected as a precapillary labeling reagent for imidazole dipeptides to form isoindole derivatives. The optimized molar ratio between CBQCA and peptide was found to be 75:1, and 50 mmol/L borate buffer (pH 9.2) was used for the derivatization in order to achieve good efficiency. Three imidazole dipeptides were baseline-separated within 20 min by using 112 mmol/L sodium borate (pH 10.4,10.8) as running buffer. Concentration detection limits (signal-to-noise ratios) for carnosine, anserine, and homocarnosine were 4.73, 4.37, and 3.94 nmol/L, respectively. This method has been applied to the analysis of human cerebrospinal fluid (CSF) and meat dry powder of pig and sheep. Recoveries were in the range of 82.9,104.8% for homocarnosine in CSF. For carnosine and anserine, the recoveries are 98.3% and 80.2% in meat dry powder of pig and 111.2% and 112.8% in meat dry powder of sheep, respectively. [source] The 28-amino acid form of an APLP1-derived A,-like peptide is a surrogate marker for A,42 production in the central nervous systemEMBO MOLECULAR MEDICINE, Issue 4 2009Kanta Yanagida Abstract Surrogate markers for the Alzheimer disease (AD)-associated 42-amino acid form of amyloid-, (A,42) have been sought because they may aid in the diagnosis of AD and for clarification of disease pathogenesis. Here, we demonstrate that human cerebrospinal fluid (CSF) contains three APLP1-derived A,-like peptides (APL1,) that are generated by ,- and ,-cleavages at a concentration of ,4.5,nM. These novel peptides, APL1,25, APL1,27 and APL1,28, were not deposited in AD brains. Interestingly, most ,-secretase modulators (GSMs) and familial AD-associated presenilin1 mutants that up-regulate the relative production of A,42 cause a parallel increase in the production of APL1,28 in cultured cells. Moreover, in CSF from patients with pathological mutations in presenilin1 gene, the relative APL1,28 levels are higher than in non-AD controls, while the relative A,42 levels are unchanged or lower. Most strikingly, the relative APL1,28 levels are higher in CSF from sporadic AD patients (regardless of whether they are at mild cognitive impairment or AD stage), than those of non-AD controls. Based on these results, we propose the relative level of APL1,28 in the CSF as a candidate surrogate marker for the relative level of A,42 production in the brain. [source] Ventricular cerebrospinal fluid melatonin concentrations investigated with an endoscopic techniqueJOURNAL OF PINEAL RESEARCH, Issue 2 2007Pierluigi Longatti Abstract:, The role of melatonin in humans still remains unclear. Uncertainties persist about its effects on neurophysiology regarding its levels in human cerebrospinal fluid (CSF), as the bulk of knowledge on this subject mainly derives from studies conducted on animals. In this study, CSF was micro-sampled with a simple, new method from each cerebral ventricle of patients undergoing neuroendoscopy for hydrocephalus. Our purpose was to measure CSF melatonin levels and determine possible differences in its concentration among various significant areas in the cerebral ventricles (e.g. pineal recess, pituitary recess, lateral ventricle, fourth ventricle) and lumbar cistern. From 2002 to 2004, 10 hydrocephalic patients were operated on using a neuroendoscopic technique. The CSF specimens were investigated for melatonin concentrations (free plus protein-bound) after deproteinization; the measurement technique was high-performance liquid chromatography. The preliminary data obtained with this endoscopic micro-sampling technique (applied to humans for the first time) suggest that melatonin is more concentrated within the ventricles and its highest concentration is found in the third ventricle (IIIv), although the difference detected between the CSF of the IIIv and that of the pineal recess was not significant. [source] Quantification of D -Asp and D -Glu in rat brain and human cerebrospinal fluid by microchip electrophoresisJOURNAL OF SEPARATION SCIENCE, JSS, Issue 17 2009Yong Huang Abstract A microchip electrophoresis (MCE) method with LIF detection was presented for quantification of D -aspartic acid (D -Asp) and D -glutamate (D -Glu) in biological samples. D -Asp and D -Glu were determined after precolumn derivatization with FITC. The chiral separation was performed on a glass/PDMS hybrid microfluidic chip using ,-CD as chiral selector in the running buffer. High sensitive detection was obtained by the LIF detection. The LODs (S/N = 3) for D -Asp and D -Glu were 6.0×10,8 and 4.0×10,8 M, respectively. Using this method, the levels of D -Asp and D -Glu in rat brain and human cerebrospinal fluid (CSF) were determined. [source] Determination of amino acid neurotransmitters in human cerebrospinal fluid and saliva by capillary electrophoresis with laser-induced fluorescence detectionJOURNAL OF SEPARATION SCIENCE, JSS, Issue 16-17 2008Ying-Hua Deng Abstract A CE,LIF detection method has been developed to identify and quantitate six amino acid neurotransmitters including glutamic acid, aspartic acid, ,-aminobutyric acid, glycine, taurine, and glutamine. N -Hydroxysuccinimidyl fluorescein- O -acetate, a fluorescein-based dye, was employed for the derivatization of these neurotransmitters prior to CE,LIF analysis. Different parameters which influenced separation and derivatization were optimized in detail. Under optimum conditions, linearity was achieved within concentration ranges of up to three orders of magnitudes for those analytes with correlation coefficients from 0.9989 to 0.9998. The LODs ranged from 0.06 nM to 0.1 nM, and are thus superior or equivalent to those previously reported in the literature using CE,LIF detection. The proposed method has been successfully applied to the determination of amino acid neurotransmitters in biological samples such as human cerebrospinal fluid and saliva with satisfactory recoveries. [source] Proteomics of brain extracellular fluid (ECF) and cerebrospinal fluid (CSF),MASS SPECTROMETRY REVIEWS, Issue 1 2010Martin H. Maurer Abstract Mass spectrometry has become the gold standard for the identification of proteins in proteomics. In this review, I will discuss the available literature on proteomic experiments that analyze human cerebrospinal fluid (CSF) and brain extracellular fluid (ECF), mostly obtained by cerebral microdialysis. Both materials are of high diagnostic value in clinical neurology, for example, in cerebrovascular disorders like stroke, neurodegenerative diseases like Alzheimer's Disease, Parkinson's Disease, amyotrophic lateral sclerosis (ALS), traumatic brain injury and cerebral infectious and inflammatory disease, such as multiple sclerosis. Moreover, there are standard procedures for sampling. In a number of studies in recent years, biomarkers have been proposed in CSF and ECF for improved diagnosis or to control therapy, based on proteomics and mass spectrometry. I will also discuss the needs for a transition of research-based experimental screening with mass spectrometry to fast and reliable diagnostic instrumentation for clinical use. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 29:17,28, 2010 [source] Correlation-associated peptide networks of human cerebrospinal fluidPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 11 2005Jens Lamerz Dr. Abstract Profiling of peptides and small proteins from either human body fluids or tissues by chromatography and subsequent mass spectrometry reveals several thousand individual peptide signals per sample. Any peptide is an intermediate in the course of biosynthesis, post-translational modification (PTM), proteolytic processing and degradation. Changes in the concentration of one peptide often affects the concentration of the other, hence a challenge consists in the development of suitable tools to turn this large amount of data into biologically relevant information. Comprehensive statistical analysis of the peptide profiling data allows associating peptides, which are closely related in terms of peptide biochemistry. Here, the bioinformatic concept of peptide networks, correlation-associated peptide networks (CANs), is introduced. Peptides with statistical similarity of their concentrations are grouped in form of networks, and these networks are interpreted in terms of peptide biochemistry. The spectrum of functional relationships found in cerebrospinal fluid CAN covers PTM and proteolytic degradation of peptides, clearance processing in the complement cascade, common secretion of peptides by neuroendocrine cells as well as ubiquitin-mediated degradation. Our results indicate that CAN is a powerful bioinformatic tool for the systematic analysis and interpretation of large peptidomics and proteomics data and helps to discover novel bioactive and diagnostic peptides. [source] Proteomics of human cerebrospinal fluid , the good, the bad, and the uglyPROTEOMICS - CLINICAL APPLICATIONS, Issue 8 2007Jing Zhang ProfessorArticle first published online: 13 JUL 200 Abstract The development of MALDI ESI in the late 1980s has revolutionized the biological sciences and facilitated the emergence of a new discipline called proteomics. Application of proteomics to human cerebrospinal fluid (CSF) has greatly hastened the advancement of characterizing the CSF proteome as well as revealing novel protein biomarkers that are diagnostic of various neurological diseases. While impressive progressions have been made in this field, it has become increasingly clear that proteomics results generated by various laboratories are highly variable. The underlying issues are vast, including limitations and complications with heterogeneity of patients/testing subjects, experimental design, sample processing, as well as current proteomics technology. Accordingly, this review not only summarizes the current status of characterization of the human CSF proteome and biomarker discovery for major neurodegenerative disorders, i.e., Alzheimer's disease and Parkinson's disease, but also addresses a few essential caveats involved in several steps of CSF proteomics that may contribute to the variable/contradicting results reported by different laboratories. The potential future directions of CSF proteomics are also discussed with this analysis. [source] | |||||||||||||