Mass spectral measurements of the apoHDL in horse (Equus caballus) cerebrospinal fluid.
Abstract: As a continuation of our proteogenomic studies of equine apolipoproteins, we have obtained molecular masses for several of the apolipoproteins associated with the HDL in horse cerebrospinal fluid (CSF). Using electrospray-ionization mass spectrometry (ESI-MS), we report on values for apolipoproteins, A-I and A-II, as well as acylated apoA-I. In comparison with our previously published data on equine plasma apolipoproteins, there appears to be a higher percentage of acylated apoA-I in the CSF than in plasma. As was the case in plasma, apoA-II circulates as a homodimer. These studies also revealed a protein with a mass of 34,468Da that we are speculating is the value for horse apoE.
Copyright © 2012 Elsevier Inc. All rights reserved.
Publication Date: 2012-02-12 PubMed ID: 22377539DOI: 10.1016/j.cbd.2012.02.002Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
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The research article presents information on a molecular mass study of apolipoproteins associated with the Horse High-Density Lipoprotein (HDL) available in the cerebrospinal fluid, as part of proteogenomic research on equine apolipoproteins.
Study Overview
- The researchers carried their studies forward in the field of proteogenomics related to equine apolipoproteins focused on apolipoproteins related to HDL (High-Density Lipoprotein) in horse cerebrospinal fluid.
- They made use of electrospray-ionization mass spectrometry (ESI-MS), a sensitive technique to measure the molecular weight of different compounds, to obtain the molecular masses for these proteins.
Mass Spectral Measurements
- The research elucidated the values for apolipoproteins A-I and A-II and acylated apoA-I.
- The process they used for the measurements involved a technique called electrospray ionization mass spectrometry (ESI-MS), which is an analytical technique that can determine the molecular mass and structural information of molecules.
- The main advantage of ESI-MS is its ability to handle samples that are in complex mixtures and are thermally labile or relatively large in size. This makes it an ideal tool for the study of proteins.
Comparative Analysis
- The researchers compared their results with previous data on equine plasma apolipoproteins.
- They observed a higher frequency of acylated apoA-I in the cerebrospinal fluid (CSF) as compared to the plasma.
- Acylated apoA-I were significant because acylation typically helps proteins achieve their active forms and function properly. Therefore, higher levels of acylated apoA-I in the CSF might point to specific changes in the equine body or specific functionality therein.
Additional Findings
- ApoA-II, like in plasma, circulates as a homodimer (two identical molecules joined together) in cerebrospinal fluid too. This is noteworthy because dimerization often helps proteins perform their functions more effectively.
- The researchers found a protein with a mass of 34,468Da, which they speculated to be horse apoE, a protein involved in fat metabolism.
Cite This Article
APA
Puppione DL, Della Donna L, Bassilian S, Souda P, MacDonald MH, Whitelegge JP.
(2012).
Mass spectral measurements of the apoHDL in horse (Equus caballus) cerebrospinal fluid.
Comp Biochem Physiol Part D Genomics Proteomics, 7(2), 172-174.
https://doi.org/10.1016/j.cbd.2012.02.002 Publication
Researcher Affiliations
- The Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA. puppione@chem.ucla.edu
MeSH Terms
- Animals
- Apolipoprotein A-I / cerebrospinal fluid
- Apolipoprotein A-I / chemistry
- Apolipoprotein A-II / cerebrospinal fluid
- Apolipoprotein A-II / chemistry
- Horses / cerebrospinal fluid
- Male
- Molecular Weight
- Spectrometry, Mass, Electrospray Ionization
Grant Funding
- R21 RR023132 / NCRR NIH HHS
Citations
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