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Proteomics analysis of prefractionated human lumbar cerebrospinal fluid
Author(s) -
Yuan Xianglin,
Desiderio Dominic M.
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200400934
Subject(s) - proteomics , cerebrospinal fluid , proteome , blood proteins , chemistry , choroid plexus , two dimensional gel electrophoresis , albumin , biology , central nervous system , biochemistry , endocrinology , neuroscience , gene
Cerebrospinal fluid (CSF) is produced by the chorioid plexus in the ventricles. It surrounds the brain and bone marrow, and reflects several different disorders of the central nervous system (CNS). Proteomics has been used to analyze CSF in order to discover disease‐associated proteins and to elucidate the basic molecular mechanisms that either cause, or result from, CNS disorders. However, some disease‐associated proteins are of low‐abundance and are difficult to detect. A low total‐protein concentration, a high amount of albumin and immunoglobins, and a wide dynamic range (several orders of magnitude) of protein concentration cause several difficulties in the identification of low‐abundance CSF proteins. In this study, advantage was taken of the range of different hydrophobic properties of CSF proteins, and a reversed‐phase solid‐phase extraction (SPE) cartridge was used to prefractionate human lumbar CSF proteins into three separate fractions prior to two‐dimensional gel electrophoresis resolution of the proteome. A portion of the high‐abundance CSF proteins were removed from two (eluted with 35% and 50% acetonitrile) of the three fractions. Some trace CSF proteins were preferentially enriched in the two fractions, and many proteins were detected in the two‐dimensional (2‐D) gels of the two fractions. Among the novel proteins identified, sixty‐two protein spots that represent forty‐two proteins were characterized. Most of the proteins have not been annotated in any previous 2‐D map of human CSF, and several have been implicated in CNS diseases. The prefractionation of CSF proteins with SPE, followed by proteomics analysis, provides a new method to explore low‐abundance, disease‐specific CSF proteins.