Evidence map›Paper›PMID 26022737›Full record

ArticleJournal of proteome research2015

Characterization of the Glycosylation Site of Human PSA Prompted by Missense Mutation using LC-MS/MS.

Ehwang Song, Yunli Hu, Ahmed Hussein, Chuan-Yih Yu, Haixu Tang, Yehia Mechref

Abstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  3. Mass Spectrometry-Based Glycoproteomics and Prostate Cancer.International journal of molecular sciences · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Ehwang Song
Yunli Hu
Ahmed Hussein∥Department of Biotechnology, Alexandria University, 163-Horreya Avenue, El-Shatby 21526, Alexandria, Egypt.
Chuan-Yih Yu
Haixu Tang
Yehia Mechref
Texas Tech University · USIndiana University Bloomington · US

Funding

Sensitive and Quantitative MS-bases Glycomic Mapping PlatformR01GM112490 · NIGMS · TEXAS TECH UNIVERSITY · PI MECHREF, YEHIA · 2014 to 2024
$3.2M
Developing high-throughput IMS-MS and IMS-IMS-MS techniques for glycomics analysiR01GM093322 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., MECHREF, YEHIA · 2010 to 2013
$1.1M
NIGMS NIH HHS 1R01GM093322-05NIGMS NIH HHS 1R01GM112490-01NIGMS NIH HHS R01 GM093322NIGMS NIH HHS R01 GM112490
6 · The paper itself

Abstract

Prostate specific antigen (PSA) is currently used as a diagnostic biomarker for prostate cancer. It is a glycoprotein possessing a single glycosylation site at N69. During our previous study of PSA N69 glycosylation, additional glycopeptides were observed in the PSA sample that were not previously reported and did not match glycopeptides of impure glycoproteins existing in the sample. This extra glycosylation site of PSA is associated with a mutation in KLK3 genes. Among single nucleotide polymorphisms (SNPs) of KLKs families, the rs61752561 in KLK3 genes is an unusual missense mutation resulting in the conversion of D102 to N in PSA amino acid sequence. Accordingly, a new N-linked glycosylation site is created with an N102MS motif. Here we report the first qualitative and quantitative glycoproteomic study of PSA N102 glycosylation site by LC-MS/MS. We successfully applied tandem MS to verify the amino acid sequence possessing N102 glycosylation site and associated glycoforms of PSA samples acquired from different suppliers. Among the three PSA samples, HexNAc2Hex5 was the predominant glycoform at N102, while HexNAc4Hex5Fuc1NeuAc1 or HexNAc4Hex5Fuc1NeuAc2 was the primary glycoforms at N69. D102 is the first amino acid of "kallikrein loop", which is close to a zinc-binding site and catalytic triad. The different glycosylation of N102 relative to N69 might be influenced by the close vicinity of N102 to these functional sites and steric hindrance.

Indexed as

Mutation, MissenseAmino Acid SequenceChromatography, LiquidGlycosylationHumansMolecular Sequence DataPolymorphism, Single NucleotideProstate-Specific AntigenSequence Homology, Amino AcidTandem Mass SpectrometryProstate-Specific AntigenD102NglycopeptideglycoproteomicsLC−MS/MSmissense mutationN-linked glycosylationprostate specific antigenPSArs61752561

Identifiers

PMID26022737
PMCPMC4866810
OpenAlexW814829813

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.