A unique N-glycan on human transferrin in CSF: a possible biomarker for iNPH

Futakawa, Satoshi; Nara, Kiyomitsu; Miyajima, Masakazu; Kuno, Atsushi; Ito, Hiromi; Kaji, Hiroyuki; Shirotani, Keiro; Honda, Takashi; Tohyama, Yuriko; Hoshi, Koki; Hanzawa, Yusuke; Kitazume, Shinobu; Imamaki, Rie; Furukawa, Koichi; Tasaki, Kazuhiro; Arai, Hiroyuki; Yuasa, Tatsuhiko; Abe, Masafumi; Arai, Hajime; Narimatsu, Hisashi; Hashimoto, Yasuhiro

doi:10.1016/j.neurobiolaging.2011.02.023

Cited by 62 publications

(65 citation statements)

References 17 publications

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“…2). However, there is a report indicating that transferrin in CSF from iNPH patients have a unique N-glycan modification (21), suggesting that PTPRQ in CSF from iNPH patients also possibly have unique modification. Unfortunately, PTPRQ in CSF is not abundant compared to transferrin, it makes difficult to analyze PTPRQ modifications at present.…”

Section: Discussionmentioning

confidence: 99%

PTPRQ as a potential biomarker for idiopathic normal pressure hydrocephalus

Nagata

Bundo

Sugiura

et al. 2017

Molecular Medicine Reports

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Idiopathic normal pressure hydrocephalus (iNPH) is caused by the accumulation of cerebrospinal fluid (CSF) and is characterized by gait disturbance, urinary incontinence, and dementia. iNPH dementia is treatable by shunt operation; however, since the cognitive symptoms of iNPH are often similar to those of other dementias, including Alzheimer's disease (AD), accurate diagnosis of iNPH is difficult. To overcome this problem, the identification of novel diagnostic markers to distinguish iNPH and AD is warranted. Using comparative proteomic analysis of CSF from patients with iNPH and AD, protein tyrosine phosphatase receptor type Q (PTPRQ) was identified as a candidate biomarker protein for discriminating iNPH from AD. ELISA analysis indicated that the PTPRQ concentration in the CSF was significantly higher in patients with iNPH compared with those with AD. In addition, the PTPRQ concentration in the CSF of non-responders to shunt operation (SNRs) tended to be relatively lower compared with that in the responders. PTPRQ may be a useful biomarker for discriminating between patients with iNPH and AD, and may be a potential companion biomarker to identify SNRs among patients with iNPH. Additional large-scale analysis may aid in understanding the novel aspects of iNPH.

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Section: Discussionmentioning

confidence: 99%

PTPRQ as a potential biomarker for idiopathic normal pressure hydrocephalus

Nagata

Bundo

Sugiura

et al. 2017

Molecular Medicine Reports

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“…As WGA binds to sialic acid and GlcNAc, these data indicate altered glycosylation. Futakawa et al [76] identified two Tf variants in CSF with different SDS/PAGE migration properties. One was determined to be bi-antennary asialo, agalacto complex-type N-glycan that carries bisecting b-1,4-GlcNAc and core a-1,6-Fuc (Tf1), and one was determined to carry a-2,6-sialyl glycans such as serum Tf (Tf2).…”

Section: Tf and Glycosylationmentioning

confidence: 99%

The role of protein glycosylation in Alzheimer disease

2013

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Glycosylation is one of the most common, and the most complex, forms of post-translational modification of proteins. This review serves to highlight the role of protein glycosylation in Alzheimer disease (AD), a topic that has not been thoroughly investigated, although glycosylation defects have been observed in AD patients. The major pathological hallmarks in AD are neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles are composed of phosphorylated tau, and the plaques are composed of amyloid b-peptide (Ab), which is generated from amyloid precursor protein (APP). Defects in glycosylation of APP, tau and other proteins have been reported in AD. Another interesting observation is that the two proteases required for the generation of amyloid b-peptide (Ab), i.e. c-secretase and b-secretase, also have roles in protein glycosylation. For instance, c-secretase and b-secretase affect the extent of complex N-glycosylation and sialylation of APP, respectively. These processes may be important in AD pathogenesis, as proper intracellular sorting, processing and export of APP are affected by how it is glycosylated. Furthermore, lack of one of the key components of c-secretase, presenilin, leads to defective glycosylation of many additional proteins that are related to AD pathogenesis and/or neuronal function, including nicastrin, reelin, butyrylcholinesterase, cholinesterase, neural cell adhesion molecule, v-ATPase, and tyrosine-related kinase B. Improved understanding of the effects of AD on protein glycosylation, and vice versa, may therefore be important for improving the diagnosis and treatment of AD patients.

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“…For these reasons, biofluids such as blood serum or CSF have been used as attractive sources for biomarker discovery, using either glycomics or glycoproteomics approaches . For instance, previous studies have shown the existence of 'brain‐type' N‐glycans on some CSF proteins, and also underlined variations in their relative abundances in relation to neurodegenerative disorders …”

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confidence: 99%