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Clinicopathologic Application of Lectin Histochemistry Bisecting GlcNAc in Glioblastoma

Clinicopathologic Application of Lectin Histochemistry Bisecting GlcNAc in Glioblastoma RESEARCH ARTICLE Clinicopathologic Application of Lectin Histochemistry Bisecting GlcNAc in Glioblastoma Eiko Aoyanagi, AD,* Ken Sasai, PhD,*w Miho Nodagashira, BD,* Lei Wang, MSc,* Hiroshi Nishihara, MD, PhD,* Hideyuki Ihara, PhD,z Yoshitaka Ikeda, MD, PhD,z and Shinya Tanaka, MD, PhD* growing body of evidence supports the crucial roles Abstract: Glycosylation is one of the most common posttransla- Afor glycans at various pathophysiologic steps of tional modifications and changes in oligosaccharide structures tumor progression. Glycans are involved in tumor proli- are associated with many human diseases including a number of feration, invasion, hematogenous metastasis and angio- cancers. Thus, discovering aberrant glycosylation patterns that genesis, and malignant transformation is often associated serve as markers for brain tumor progression and metastasis with changes in the glycosylation of cell surface proteins. represents an attractive strategy to improve clinicopathologic One of the most common structural changes in aspar- diagnosis and to provide aids to the development of novel agine-linked (N-linked) oligosaccharides during malignant therapies. To identify glioblastoma (GBM) cells express- transformation is caused by the action of N-acetylgluco- ing glycoproteins that contain high levels of the bisecting saminyltransferase (GnT)-V, which catalyzes the transfer N-acetylglucosamine (GlcNAc) structures, lectin histochemistry of N-acetylglucosamine (GlcNAc) to the a1,6-linked was http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Immunohistochemistry & Molecular Morphology Wolters Kluwer Health

Clinicopathologic Application of Lectin Histochemistry Bisecting GlcNAc in Glioblastoma

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Copyright
Copyright © 2010 by Lippincott Williams & Wilkins
ISSN
1541-2016
DOI
10.1097/PAI.0b013e3181e3bf0d
pmid
20661133
Publisher site
See Article on Publisher Site

Abstract

RESEARCH ARTICLE Clinicopathologic Application of Lectin Histochemistry Bisecting GlcNAc in Glioblastoma Eiko Aoyanagi, AD,* Ken Sasai, PhD,*w Miho Nodagashira, BD,* Lei Wang, MSc,* Hiroshi Nishihara, MD, PhD,* Hideyuki Ihara, PhD,z Yoshitaka Ikeda, MD, PhD,z and Shinya Tanaka, MD, PhD* growing body of evidence supports the crucial roles Abstract: Glycosylation is one of the most common posttransla- Afor glycans at various pathophysiologic steps of tional modifications and changes in oligosaccharide structures tumor progression. Glycans are involved in tumor proli- are associated with many human diseases including a number of feration, invasion, hematogenous metastasis and angio- cancers. Thus, discovering aberrant glycosylation patterns that genesis, and malignant transformation is often associated serve as markers for brain tumor progression and metastasis with changes in the glycosylation of cell surface proteins. represents an attractive strategy to improve clinicopathologic One of the most common structural changes in aspar- diagnosis and to provide aids to the development of novel agine-linked (N-linked) oligosaccharides during malignant therapies. To identify glioblastoma (GBM) cells express- transformation is caused by the action of N-acetylgluco- ing glycoproteins that contain high levels of the bisecting saminyltransferase (GnT)-V, which catalyzes the transfer N-acetylglucosamine (GlcNAc) structures, lectin histochemistry of N-acetylglucosamine (GlcNAc) to the a1,6-linked was

Journal

Applied Immunohistochemistry & Molecular Morphology – Wolters Kluwer Health

Published: Dec 1, 2010

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