Cargando…

Glycosylation status of serum immunoglobulin G in patients with prostate diseases

Occurrences of high values in patients with benign prostate disease and low values in patients with highly suspicious cancer have diminished the trustworthiness of prostate‐specific antigen as an early diagnostic marker of prostate cancer. In the search for other complimentary markers, we focused on...

Descripción completa

Detalles Bibliográficos
Autores principales: Kazuno, Saiko, Furukawa, Jun‐ichi, Shinohara, Yasuro, Murayama, Kimie, Fujime, Makoto, Ueno, Takashi, Fujimura, Tsutomu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4924372/
https://www.ncbi.nlm.nih.gov/pubmed/26880719
http://dx.doi.org/10.1002/cam4.662
_version_ 1782439861458829312
author Kazuno, Saiko
Furukawa, Jun‐ichi,
Shinohara, Yasuro
Murayama, Kimie
Fujime, Makoto
Ueno, Takashi
Fujimura, Tsutomu
author_facet Kazuno, Saiko
Furukawa, Jun‐ichi,
Shinohara, Yasuro
Murayama, Kimie
Fujime, Makoto
Ueno, Takashi
Fujimura, Tsutomu
author_sort Kazuno, Saiko
collection PubMed
description Occurrences of high values in patients with benign prostate disease and low values in patients with highly suspicious cancer have diminished the trustworthiness of prostate‐specific antigen as an early diagnostic marker of prostate cancer. In the search for other complimentary markers, we focused on serum IgG from patients with prostate diseases as well as normal subjects. IgG purified from the sera of normal control subjects and patients with prostate diseases, was digested with peptide N‐glycanase. Released glycans were quantified using MALDI‐time of flight mass spectrometry. We report that N‐linked (N‐acetylhexosamine)(2)(deoxyhexose)(mannose)(3)(N‐acetylglucosamine)(2) was significantly increased in the IgG heavy chains of patients with prostate cancer compared with that of either benign prostatic disease patients or healthy subjects, whereas (hexose)(N‐acetylhexosamine)(2)(deoxyhexose)(mannose)(3) (N‐acetylglucosamine)(2) was more abundant in the heavy chains of healthy subjects and benign prostatic disease patients. Thus, an absence of the terminal hexose of N‐linked glycans has been closely connected to the progression of prostate cancer. Furthermore, surface plasmon resonance analyses have revealed that IgG from patients with prostate cancer has a decreased binding for Sambucus nigra lectin, compared with that from the benign prostatic disease patients or from normal subjects, suggesting lower levels of (N‐acetylneuraminic acid)(α2‐6)galactose/N‐acetylgalactosamine groups in the N‐linked glycans of patient IgG. Meanwhile, wheat germ agglutinin binding to IgG of the cancer group was significantly larger than that for the benign prostatic disease group but smaller than that for normal subjects. Our study indicates that the glycosylation changes in IgG can become useful diagnostic parameters for prostate cancer.
format Online
Article
Text
id pubmed-4924372
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-49243722016-06-29 Glycosylation status of serum immunoglobulin G in patients with prostate diseases Kazuno, Saiko Furukawa, Jun‐ichi, Shinohara, Yasuro Murayama, Kimie Fujime, Makoto Ueno, Takashi Fujimura, Tsutomu Cancer Med Clinical Cancer Research Occurrences of high values in patients with benign prostate disease and low values in patients with highly suspicious cancer have diminished the trustworthiness of prostate‐specific antigen as an early diagnostic marker of prostate cancer. In the search for other complimentary markers, we focused on serum IgG from patients with prostate diseases as well as normal subjects. IgG purified from the sera of normal control subjects and patients with prostate diseases, was digested with peptide N‐glycanase. Released glycans were quantified using MALDI‐time of flight mass spectrometry. We report that N‐linked (N‐acetylhexosamine)(2)(deoxyhexose)(mannose)(3)(N‐acetylglucosamine)(2) was significantly increased in the IgG heavy chains of patients with prostate cancer compared with that of either benign prostatic disease patients or healthy subjects, whereas (hexose)(N‐acetylhexosamine)(2)(deoxyhexose)(mannose)(3) (N‐acetylglucosamine)(2) was more abundant in the heavy chains of healthy subjects and benign prostatic disease patients. Thus, an absence of the terminal hexose of N‐linked glycans has been closely connected to the progression of prostate cancer. Furthermore, surface plasmon resonance analyses have revealed that IgG from patients with prostate cancer has a decreased binding for Sambucus nigra lectin, compared with that from the benign prostatic disease patients or from normal subjects, suggesting lower levels of (N‐acetylneuraminic acid)(α2‐6)galactose/N‐acetylgalactosamine groups in the N‐linked glycans of patient IgG. Meanwhile, wheat germ agglutinin binding to IgG of the cancer group was significantly larger than that for the benign prostatic disease group but smaller than that for normal subjects. Our study indicates that the glycosylation changes in IgG can become useful diagnostic parameters for prostate cancer. John Wiley and Sons Inc. 2016-02-16 /pmc/articles/PMC4924372/ /pubmed/26880719 http://dx.doi.org/10.1002/cam4.662 Text en © 2016 The Authors. Cancer Medicine published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Clinical Cancer Research
Kazuno, Saiko
Furukawa, Jun‐ichi,
Shinohara, Yasuro
Murayama, Kimie
Fujime, Makoto
Ueno, Takashi
Fujimura, Tsutomu
Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title_full Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title_fullStr Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title_full_unstemmed Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title_short Glycosylation status of serum immunoglobulin G in patients with prostate diseases
title_sort glycosylation status of serum immunoglobulin g in patients with prostate diseases
topic Clinical Cancer Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4924372/
https://www.ncbi.nlm.nih.gov/pubmed/26880719
http://dx.doi.org/10.1002/cam4.662
work_keys_str_mv AT kazunosaiko glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT furukawajunichi glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT shinoharayasuro glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT murayamakimie glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT fujimemakoto glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT uenotakashi glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases
AT fujimuratsutomu glycosylationstatusofserumimmunoglobulinginpatientswithprostatediseases