Novel Protein Biomarkers of Monoamine Metabolism Defects Correlate with Disease Severity
ABSTRACT Background Genetic defects of monoamine neurotransmitters are rare neurological diseases amenable to treatment with variable response. They are major causes of early parkinsonism and other spectrum of movement disorders including dopa‐responsive dystonia. Objectives The objective of this st...
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| Veröffentlicht in: | Movement disorders 2021-03, Vol.36 (3), p.690-703 |
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| creator | Tristán‐Noguero, Alba Borràs, Eva Molero‐Luis, Marta Wassenberg, Tessa Peters, Tessa Verbeek, Marcel M. Willemsen, Michel Opladen, Thomas Jeltsch, Kathrin Pons, Roser Thony, Beat Horvath, Gabriella Yapici, Zuhal Friedman, Jennifer Hyland, Keith Agosta, Guillermo E. López‐Laso, Eduardo Artuch, Rafael Sabidó, Eduard García‐Cazorla, Àngels |
| description | ABSTRACT
Background
Genetic defects of monoamine neurotransmitters are rare neurological diseases amenable to treatment with variable response. They are major causes of early parkinsonism and other spectrum of movement disorders including dopa‐responsive dystonia.
Objectives
The objective of this study was to conduct proteomic studies in cerebrospinal fluid (CSF) samples of patients with monoamine defects to detect biomarkers involved in pathophysiology, clinical phenotypes, and treatment response.
Methods
A total of 90 patients from diverse centers of the International Working Group on Neurotransmitter Related Disorders were included in the study (37 untreated before CSF collection, 48 treated and 5 unknown at the collection time). Clinical and molecular metadata were related to the protein abundances in the CSF.
Results
Concentrations of 4 proteins were significantly altered, detected by mass spectrometry, and confirmed by immunoassays. First, decreased levels of apolipoprotein D were found in severe cases of aromatic L‐amino acid decarboxylase deficiency. Second, low levels of apolipoprotein H were observed in patients with the severe phenotype of tyrosine hydroxylase deficiency, whereas increased concentrations of oligodendrocyte myelin glycoprotein were found in the same subset of patients with tyrosine hydroxylase deficiency. Third, decreased levels of collagen6A3 were observed in treated patients with tetrahydrobiopterin deficiency.
Conclusion
This study with the largest cohort of patients with monoamine defects studied so far reports the proteomic characterization of CSF and identifies 4 novel biomarkers that bring new insights into the consequences of early dopaminergic deprivation in the developing brain. They open new possibilities to understand their role in the pathophysiology of these disorders, and they may serve as potential predictors of disease severity and therapies. © 2020 International Parkinson and Movement Disorder Society |
| doi_str_mv | 10.1002/mds.28362 |
| format | Article |
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Background
Genetic defects of monoamine neurotransmitters are rare neurological diseases amenable to treatment with variable response. They are major causes of early parkinsonism and other spectrum of movement disorders including dopa‐responsive dystonia.
Objectives
The objective of this study was to conduct proteomic studies in cerebrospinal fluid (CSF) samples of patients with monoamine defects to detect biomarkers involved in pathophysiology, clinical phenotypes, and treatment response.
Methods
A total of 90 patients from diverse centers of the International Working Group on Neurotransmitter Related Disorders were included in the study (37 untreated before CSF collection, 48 treated and 5 unknown at the collection time). Clinical and molecular metadata were related to the protein abundances in the CSF.
Results
Concentrations of 4 proteins were significantly altered, detected by mass spectrometry, and confirmed by immunoassays. First, decreased levels of apolipoprotein D were found in severe cases of aromatic L‐amino acid decarboxylase deficiency. Second, low levels of apolipoprotein H were observed in patients with the severe phenotype of tyrosine hydroxylase deficiency, whereas increased concentrations of oligodendrocyte myelin glycoprotein were found in the same subset of patients with tyrosine hydroxylase deficiency. Third, decreased levels of collagen6A3 were observed in treated patients with tetrahydrobiopterin deficiency.
Conclusion
This study with the largest cohort of patients with monoamine defects studied so far reports the proteomic characterization of CSF and identifies 4 novel biomarkers that bring new insights into the consequences of early dopaminergic deprivation in the developing brain. They open new possibilities to understand their role in the pathophysiology of these disorders, and they may serve as potential predictors of disease severity and therapies. © 2020 International Parkinson and Movement Disorder Society</description><identifier>ISSN: 0885-3185</identifier><identifier>EISSN: 1531-8257</identifier><identifier>DOI: 10.1002/mds.28362</identifier><identifier>PMID: 33152132</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Amino Acid Metabolism, Inborn Errors ; Amino acids ; Apolipoproteins ; Basal ganglia ; Biomarkers ; Brain diseases ; Central nervous system diseases ; Cerebrospinal fluid ; Collagen ; Dopamine receptors ; Dystonia ; Dystonic Disorders ; early parkinsonism ; Humans ; Hydroxylase ; Mass spectroscopy ; Monoamines ; Movement disorders ; Myelin ; Neurological diseases ; Neurotransmitters ; Oligodendrocyte-myelin glycoprotein ; Pathophysiology ; Patients ; Phenotypes ; Protein turnover ; Proteomics ; Severity of Illness Index ; Tetrahydrobiopterin ; Tyrosine 3-monooxygenase</subject><ispartof>Movement disorders, 2021-03, Vol.36 (3), p.690-703</ispartof><rights>2020 International Parkinson and Movement Disorder Society</rights><rights>2020 International Parkinson and Movement Disorder Society.</rights><rights>2021 International Parkinson and Movement Disorder Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3532-5f0a391aacaef314e91b933c6d9d3cac90110a6ca5f237145bfd7a5358f520df3</citedby><cites>FETCH-LOGICAL-c3532-5f0a391aacaef314e91b933c6d9d3cac90110a6ca5f237145bfd7a5358f520df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fmds.28362$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fmds.28362$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33152132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tristán‐Noguero, Alba</creatorcontrib><creatorcontrib>Borràs, Eva</creatorcontrib><creatorcontrib>Molero‐Luis, Marta</creatorcontrib><creatorcontrib>Wassenberg, Tessa</creatorcontrib><creatorcontrib>Peters, Tessa</creatorcontrib><creatorcontrib>Verbeek, Marcel M.</creatorcontrib><creatorcontrib>Willemsen, Michel</creatorcontrib><creatorcontrib>Opladen, Thomas</creatorcontrib><creatorcontrib>Jeltsch, Kathrin</creatorcontrib><creatorcontrib>Pons, Roser</creatorcontrib><creatorcontrib>Thony, Beat</creatorcontrib><creatorcontrib>Horvath, Gabriella</creatorcontrib><creatorcontrib>Yapici, Zuhal</creatorcontrib><creatorcontrib>Friedman, Jennifer</creatorcontrib><creatorcontrib>Hyland, Keith</creatorcontrib><creatorcontrib>Agosta, Guillermo E.</creatorcontrib><creatorcontrib>López‐Laso, Eduardo</creatorcontrib><creatorcontrib>Artuch, Rafael</creatorcontrib><creatorcontrib>Sabidó, Eduard</creatorcontrib><creatorcontrib>García‐Cazorla, Àngels</creatorcontrib><title>Novel Protein Biomarkers of Monoamine Metabolism Defects Correlate with Disease Severity</title><title>Movement disorders</title><addtitle>Mov Disord</addtitle><description>ABSTRACT
Background
Genetic defects of monoamine neurotransmitters are rare neurological diseases amenable to treatment with variable response. They are major causes of early parkinsonism and other spectrum of movement disorders including dopa‐responsive dystonia.
Objectives
The objective of this study was to conduct proteomic studies in cerebrospinal fluid (CSF) samples of patients with monoamine defects to detect biomarkers involved in pathophysiology, clinical phenotypes, and treatment response.
Methods
A total of 90 patients from diverse centers of the International Working Group on Neurotransmitter Related Disorders were included in the study (37 untreated before CSF collection, 48 treated and 5 unknown at the collection time). Clinical and molecular metadata were related to the protein abundances in the CSF.
Results
Concentrations of 4 proteins were significantly altered, detected by mass spectrometry, and confirmed by immunoassays. First, decreased levels of apolipoprotein D were found in severe cases of aromatic L‐amino acid decarboxylase deficiency. Second, low levels of apolipoprotein H were observed in patients with the severe phenotype of tyrosine hydroxylase deficiency, whereas increased concentrations of oligodendrocyte myelin glycoprotein were found in the same subset of patients with tyrosine hydroxylase deficiency. Third, decreased levels of collagen6A3 were observed in treated patients with tetrahydrobiopterin deficiency.
Conclusion
This study with the largest cohort of patients with monoamine defects studied so far reports the proteomic characterization of CSF and identifies 4 novel biomarkers that bring new insights into the consequences of early dopaminergic deprivation in the developing brain. They open new possibilities to understand their role in the pathophysiology of these disorders, and they may serve as potential predictors of disease severity and therapies. © 2020 International Parkinson and Movement Disorder Society</description><subject>Amino Acid Metabolism, Inborn Errors</subject><subject>Amino acids</subject><subject>Apolipoproteins</subject><subject>Basal ganglia</subject><subject>Biomarkers</subject><subject>Brain diseases</subject><subject>Central nervous system diseases</subject><subject>Cerebrospinal fluid</subject><subject>Collagen</subject><subject>Dopamine receptors</subject><subject>Dystonia</subject><subject>Dystonic Disorders</subject><subject>early parkinsonism</subject><subject>Humans</subject><subject>Hydroxylase</subject><subject>Mass spectroscopy</subject><subject>Monoamines</subject><subject>Movement disorders</subject><subject>Myelin</subject><subject>Neurological diseases</subject><subject>Neurotransmitters</subject><subject>Oligodendrocyte-myelin glycoprotein</subject><subject>Pathophysiology</subject><subject>Patients</subject><subject>Phenotypes</subject><subject>Protein turnover</subject><subject>Proteomics</subject><subject>Severity of Illness Index</subject><subject>Tetrahydrobiopterin</subject><subject>Tyrosine 3-monooxygenase</subject><issn>0885-3185</issn><issn>1531-8257</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10M1KAzEUhuEgitbqwhuQgBtdjE1yJu3MUlv_wKpQBXchzZxgdGaiybTSu3dqqwvB1dk8fBxeQg44O-WMiV5VxFORQV9skA6XwJNMyMEm6bAskwnwTO6Q3RhfGeNc8v422QHgUnAQHfJ85-dY0ofgG3Q1PXe-0uENQ6Te0rGvva5cjXSMjZ760sWKjtCiaSId-hCw1A3ST9e80JGLqCPSCc4xuGaxR7asLiPur2-XPF1ePA6vk9v7q5vh2W1iQIJIpGUacq610WiBp5jzaQ5g-kVegNEmb39mum-0tAIGPJVTWwy0BJlZKVhhoUuOV7vvwX_MMDaqctFgWeoa_SwqkcqMQZoBtPToD331s1C33ykhWS5SnudLdbJSJvgYA1r1HlwbZaE4U8vcqs2tvnO39nC9OJtWWPzKn74t6K3Apytx8f-SGo8mq8kv5heI_g</recordid><startdate>202103</startdate><enddate>202103</enddate><creator>Tristán‐Noguero, Alba</creator><creator>Borràs, Eva</creator><creator>Molero‐Luis, Marta</creator><creator>Wassenberg, Tessa</creator><creator>Peters, Tessa</creator><creator>Verbeek, Marcel M.</creator><creator>Willemsen, Michel</creator><creator>Opladen, Thomas</creator><creator>Jeltsch, Kathrin</creator><creator>Pons, Roser</creator><creator>Thony, Beat</creator><creator>Horvath, Gabriella</creator><creator>Yapici, Zuhal</creator><creator>Friedman, Jennifer</creator><creator>Hyland, Keith</creator><creator>Agosta, Guillermo E.</creator><creator>López‐Laso, Eduardo</creator><creator>Artuch, Rafael</creator><creator>Sabidó, Eduard</creator><creator>García‐Cazorla, Àngels</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>202103</creationdate><title>Novel Protein Biomarkers of Monoamine Metabolism Defects Correlate with Disease Severity</title><author>Tristán‐Noguero, Alba ; Borràs, Eva ; Molero‐Luis, Marta ; Wassenberg, Tessa ; Peters, Tessa ; Verbeek, Marcel M. ; Willemsen, Michel ; Opladen, Thomas ; Jeltsch, Kathrin ; Pons, Roser ; Thony, Beat ; Horvath, Gabriella ; Yapici, Zuhal ; Friedman, Jennifer ; Hyland, Keith ; Agosta, Guillermo E. ; López‐Laso, Eduardo ; Artuch, Rafael ; Sabidó, Eduard ; García‐Cazorla, Àngels</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3532-5f0a391aacaef314e91b933c6d9d3cac90110a6ca5f237145bfd7a5358f520df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino Acid Metabolism, Inborn Errors</topic><topic>Amino acids</topic><topic>Apolipoproteins</topic><topic>Basal ganglia</topic><topic>Biomarkers</topic><topic>Brain diseases</topic><topic>Central nervous system diseases</topic><topic>Cerebrospinal fluid</topic><topic>Collagen</topic><topic>Dopamine receptors</topic><topic>Dystonia</topic><topic>Dystonic Disorders</topic><topic>early parkinsonism</topic><topic>Humans</topic><topic>Hydroxylase</topic><topic>Mass spectroscopy</topic><topic>Monoamines</topic><topic>Movement disorders</topic><topic>Myelin</topic><topic>Neurological diseases</topic><topic>Neurotransmitters</topic><topic>Oligodendrocyte-myelin glycoprotein</topic><topic>Pathophysiology</topic><topic>Patients</topic><topic>Phenotypes</topic><topic>Protein turnover</topic><topic>Proteomics</topic><topic>Severity of Illness Index</topic><topic>Tetrahydrobiopterin</topic><topic>Tyrosine 3-monooxygenase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tristán‐Noguero, Alba</creatorcontrib><creatorcontrib>Borràs, Eva</creatorcontrib><creatorcontrib>Molero‐Luis, Marta</creatorcontrib><creatorcontrib>Wassenberg, Tessa</creatorcontrib><creatorcontrib>Peters, Tessa</creatorcontrib><creatorcontrib>Verbeek, Marcel M.</creatorcontrib><creatorcontrib>Willemsen, Michel</creatorcontrib><creatorcontrib>Opladen, Thomas</creatorcontrib><creatorcontrib>Jeltsch, Kathrin</creatorcontrib><creatorcontrib>Pons, Roser</creatorcontrib><creatorcontrib>Thony, Beat</creatorcontrib><creatorcontrib>Horvath, Gabriella</creatorcontrib><creatorcontrib>Yapici, Zuhal</creatorcontrib><creatorcontrib>Friedman, Jennifer</creatorcontrib><creatorcontrib>Hyland, Keith</creatorcontrib><creatorcontrib>Agosta, Guillermo E.</creatorcontrib><creatorcontrib>López‐Laso, Eduardo</creatorcontrib><creatorcontrib>Artuch, Rafael</creatorcontrib><creatorcontrib>Sabidó, Eduard</creatorcontrib><creatorcontrib>García‐Cazorla, Àngels</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Movement disorders</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tristán‐Noguero, Alba</au><au>Borràs, Eva</au><au>Molero‐Luis, Marta</au><au>Wassenberg, Tessa</au><au>Peters, Tessa</au><au>Verbeek, Marcel M.</au><au>Willemsen, Michel</au><au>Opladen, Thomas</au><au>Jeltsch, Kathrin</au><au>Pons, Roser</au><au>Thony, Beat</au><au>Horvath, Gabriella</au><au>Yapici, Zuhal</au><au>Friedman, Jennifer</au><au>Hyland, Keith</au><au>Agosta, Guillermo E.</au><au>López‐Laso, Eduardo</au><au>Artuch, Rafael</au><au>Sabidó, Eduard</au><au>García‐Cazorla, Àngels</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel Protein Biomarkers of Monoamine Metabolism Defects Correlate with Disease Severity</atitle><jtitle>Movement disorders</jtitle><addtitle>Mov Disord</addtitle><date>2021-03</date><risdate>2021</risdate><volume>36</volume><issue>3</issue><spage>690</spage><epage>703</epage><pages>690-703</pages><issn>0885-3185</issn><eissn>1531-8257</eissn><abstract>ABSTRACT
Background
Genetic defects of monoamine neurotransmitters are rare neurological diseases amenable to treatment with variable response. They are major causes of early parkinsonism and other spectrum of movement disorders including dopa‐responsive dystonia.
Objectives
The objective of this study was to conduct proteomic studies in cerebrospinal fluid (CSF) samples of patients with monoamine defects to detect biomarkers involved in pathophysiology, clinical phenotypes, and treatment response.
Methods
A total of 90 patients from diverse centers of the International Working Group on Neurotransmitter Related Disorders were included in the study (37 untreated before CSF collection, 48 treated and 5 unknown at the collection time). Clinical and molecular metadata were related to the protein abundances in the CSF.
Results
Concentrations of 4 proteins were significantly altered, detected by mass spectrometry, and confirmed by immunoassays. First, decreased levels of apolipoprotein D were found in severe cases of aromatic L‐amino acid decarboxylase deficiency. Second, low levels of apolipoprotein H were observed in patients with the severe phenotype of tyrosine hydroxylase deficiency, whereas increased concentrations of oligodendrocyte myelin glycoprotein were found in the same subset of patients with tyrosine hydroxylase deficiency. Third, decreased levels of collagen6A3 were observed in treated patients with tetrahydrobiopterin deficiency.
Conclusion
This study with the largest cohort of patients with monoamine defects studied so far reports the proteomic characterization of CSF and identifies 4 novel biomarkers that bring new insights into the consequences of early dopaminergic deprivation in the developing brain. They open new possibilities to understand their role in the pathophysiology of these disorders, and they may serve as potential predictors of disease severity and therapies. © 2020 International Parkinson and Movement Disorder Society</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><pmid>33152132</pmid><doi>10.1002/mds.28362</doi><tpages>14</tpages></addata></record> |
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| ispartof | Movement disorders, 2021-03, Vol.36 (3), p.690-703 |
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| subjects | Amino Acid Metabolism, Inborn Errors Amino acids Apolipoproteins Basal ganglia Biomarkers Brain diseases Central nervous system diseases Cerebrospinal fluid Collagen Dopamine receptors Dystonia Dystonic Disorders early parkinsonism Humans Hydroxylase Mass spectroscopy Monoamines Movement disorders Myelin Neurological diseases Neurotransmitters Oligodendrocyte-myelin glycoprotein Pathophysiology Patients Phenotypes Protein turnover Proteomics Severity of Illness Index Tetrahydrobiopterin Tyrosine 3-monooxygenase |
| title | Novel Protein Biomarkers of Monoamine Metabolism Defects Correlate with Disease Severity |
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