A proteomic study of serum from children with autism showing differential expression of apolipoproteins and complement proteins

Modern methods that use systematic, quantitative and unbiased approaches are making it possible to discover proteins altered by a disease. To identify proteins that might be differentially expressed in autism, serum proteins from blood were subjected to trypsin digestion followed by liquid chromatog...

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Veröffentlicht in:Molecular psychiatry 2007-03, Vol.12 (3), p.292-306
Hauptverfasser: Corbett, B A, Kantor, A B, Schulman, H, Walker, W L, Lit, L, Ashwood, P, Rocke, D M, Sharp, F R
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container_start_page 292
container_title Molecular psychiatry
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creator Corbett, B A
Kantor, A B
Schulman, H
Walker, W L
Lit, L
Ashwood, P
Rocke, D M
Sharp, F R
description Modern methods that use systematic, quantitative and unbiased approaches are making it possible to discover proteins altered by a disease. To identify proteins that might be differentially expressed in autism, serum proteins from blood were subjected to trypsin digestion followed by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) on time-of-flight (TOF) instruments to identify differentially expressed peptides. Children with autism 4–6 years of age ( n =69) were compared to typically developing children ( n =35) with similar age and gender distributions. A total of 6348 peptide components were quantified. Of these, five peptide components corresponding to four known proteins had an effect size >0.99 with a P
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To identify proteins that might be differentially expressed in autism, serum proteins from blood were subjected to trypsin digestion followed by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) on time-of-flight (TOF) instruments to identify differentially expressed peptides. Children with autism 4–6 years of age ( n =69) were compared to typically developing children ( n =35) with similar age and gender distributions. A total of 6348 peptide components were quantified. Of these, five peptide components corresponding to four known proteins had an effect size &gt;0.99 with a P &lt;0.05 and a Mascot identification score of 30 or greater for autism compared to controls. The four proteins were: Apolipoprotein (apo) B-100, Complement Factor H Related Protein (FHR1), Complement C1q and Fibronectin 1 (FN1). In addition, apo B-100 and apo A-IV were higher in children with high compared to low functioning autism. Apos are involved in the transport of lipids, cholesterol and vitamin E. The complement system is involved in the lysis and removal of infectious organisms in blood, and may be involved in cellular apoptosis in brain. 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To identify proteins that might be differentially expressed in autism, serum proteins from blood were subjected to trypsin digestion followed by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) on time-of-flight (TOF) instruments to identify differentially expressed peptides. Children with autism 4–6 years of age ( n =69) were compared to typically developing children ( n =35) with similar age and gender distributions. A total of 6348 peptide components were quantified. Of these, five peptide components corresponding to four known proteins had an effect size &gt;0.99 with a P &lt;0.05 and a Mascot identification score of 30 or greater for autism compared to controls. The four proteins were: Apolipoprotein (apo) B-100, Complement Factor H Related Protein (FHR1), Complement C1q and Fibronectin 1 (FN1). In addition, apo B-100 and apo A-IV were higher in children with high compared to low functioning autism. Apos are involved in the transport of lipids, cholesterol and vitamin E. The complement system is involved in the lysis and removal of infectious organisms in blood, and may be involved in cellular apoptosis in brain. Despite limitations of the study, including the low fold changes and variable detection rates for the peptide components, the data support possible differences of circulating proteins in autism, and should help stimulate the continued search for causes and treatments of autism by examining peripheral blood.</description><subject>Apolipoproteins</subject><subject>Apolipoproteins - blood</subject><subject>Apoptosis</subject><subject>Autism</subject><subject>Autistic children</subject><subject>Autistic Disorder - blood</subject><subject>Behavioral Sciences</subject><subject>Biological and medical sciences</subject><subject>Biological Psychology</subject><subject>Child</subject><subject>Child clinical studies</subject><subject>Child, Preschool</subject><subject>Children</subject><subject>Cholesterol</subject><subject>Complement component C1q</subject><subject>Complement factor H</subject><subject>Complement system</subject><subject>Complement System Proteins - metabolism</subject><subject>Developmental disorders</subject><subject>Female</subject><subject>Fibronectin</subject><subject>Gene Expression - physiology</subject><subject>Humans</subject><subject>Infantile autism</subject><subject>Lipids</subject><subject>Liquid chromatography</subject><subject>Lysis</subject><subject>Male</subject><subject>Mass Spectrometry - methods</subject><subject>Mass spectroscopy</subject><subject>Medical sciences</subject><subject>Medicine</subject><subject>Medicine &amp; Public Health</subject><subject>Neurosciences</subject><subject>original-article</subject><subject>Peptides</subject><subject>Peripheral blood</subject><subject>Pharmacotherapy</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Psychiatry</subject><subject>Psychology. 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To identify proteins that might be differentially expressed in autism, serum proteins from blood were subjected to trypsin digestion followed by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) on time-of-flight (TOF) instruments to identify differentially expressed peptides. Children with autism 4–6 years of age ( n =69) were compared to typically developing children ( n =35) with similar age and gender distributions. A total of 6348 peptide components were quantified. Of these, five peptide components corresponding to four known proteins had an effect size &gt;0.99 with a P &lt;0.05 and a Mascot identification score of 30 or greater for autism compared to controls. The four proteins were: Apolipoprotein (apo) B-100, Complement Factor H Related Protein (FHR1), Complement C1q and Fibronectin 1 (FN1). In addition, apo B-100 and apo A-IV were higher in children with high compared to low functioning autism. Apos are involved in the transport of lipids, cholesterol and vitamin E. The complement system is involved in the lysis and removal of infectious organisms in blood, and may be involved in cellular apoptosis in brain. Despite limitations of the study, including the low fold changes and variable detection rates for the peptide components, the data support possible differences of circulating proteins in autism, and should help stimulate the continued search for causes and treatments of autism by examining peripheral blood.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>17189958</pmid><doi>10.1038/sj.mp.4001943</doi><tpages>15</tpages></addata></record>
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subjects Apolipoproteins
Apolipoproteins - blood
Apoptosis
Autism
Autistic children
Autistic Disorder - blood
Behavioral Sciences
Biological and medical sciences
Biological Psychology
Child
Child clinical studies
Child, Preschool
Children
Cholesterol
Complement component C1q
Complement factor H
Complement system
Complement System Proteins - metabolism
Developmental disorders
Female
Fibronectin
Gene Expression - physiology
Humans
Infantile autism
Lipids
Liquid chromatography
Lysis
Male
Mass Spectrometry - methods
Mass spectroscopy
Medical sciences
Medicine
Medicine & Public Health
Neurosciences
original-article
Peptides
Peripheral blood
Pharmacotherapy
Proteins
Proteomics
Proteomics - methods
Psychiatry
Psychology. Psychoanalysis. Psychiatry
Psychopathology. Psychiatry
Serum proteins
Statistics, Nonparametric
Trypsin
Vitamin E
title A proteomic study of serum from children with autism showing differential expression of apolipoproteins and complement proteins
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