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Glycosylation profi...
Glycosylation profiling of selected proteins in cerebrospinal fluid from Alzheimer's disease and healthy subjects
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- Quaranta, Alessandro (författare)
- Stockholms universitet,Institutionen för miljövetenskap och analytisk kemi,Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden
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- Karlsson, Isabella (författare)
- Stockholms universitet,Institutionen för miljövetenskap och analytisk kemi,Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden
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- Ndreu, Lorena (författare)
- Stockholms universitet,Institutionen för miljövetenskap och analytisk kemi,Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden
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- Marini, Federico (författare)
- Univ Sapienza, Dept Chem, Ple Aldo Moro 5, I-00185 Rome, Italy
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- Ingelsson, Martin (författare)
- Uppsala universitet,Geriatrik,Molekylär Geriatrik/ Rudbecklaboratoriet
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- Thorsén, Gunnar (författare)
- Stockholms universitet,Institutionen för miljövetenskap och analytisk kemi,Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden;IVL Swedish Environm Res Inst, S-11428 Stockholm, Sweden
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(creator_code:org_t)
- 2019
- 2019
- Engelska.
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Ingår i: Analytical Methods. - : Royal Society of Chemistry (RSC). - 1759-9660 .- 1759-9679. ; 11:26, s. 3331-3340
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Alteration of glycosylation has been observed in several diseases, such as cancer and neurodegenerative disorders. The study of changes in glycosylation could lead to a better understanding of mechanisms underlying these diseases and to the identification of new biomarkers. In this work the N-linked glycosylation of five target proteins in cerebrospinal fluid (CSF) from Alzheimer's disease (AD) patients and healthy controls have been analyzed for the first time. The investigated proteins, transferrin (TFN), alpha-1-antitrypsin (AAT), C1-inhibitor, immunoglobulin G (IgG), and alpha-1-acid glycoprotein (AGP), were selected based on the availability of VHH antibody fragments and their potential involvement in neurodegenerative and inflammation diseases. AD patients showed alterations in the glycosylation of low abundance proteins, such as C1-inhibitor and alpha-1-acid glycoprotein. These alterations would not have been detected if the glycosylation profile of the total CSF had been analyzed, due to the masking effect of the dominant profiles of high abundance glycoproteins, such as IgG. Information obtained from single proteins was not sufficient to correctly classify the two sample groups; however, by using an advanced multivariate technique a total non-error rate of 72 +/- 3% was obtained. In fact, the corresponding model was able to correctly classify 71 +/- 4% of the healthy subjects and 74 +/- 7% of the AD patients. Even if the results were not conclusive for AD, this approach could be extremely useful for diseases in which glycosylation changes are reported to be more extensive, such as several types of cancer and autoimmune diseases.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Neurovetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Neurosciences (hsv//eng)
Nyckelord
- Analytical Chemistry
- analytisk kemi
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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