Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers

Hirohiko Ise, Sadanori Yamasaki, Kazuaki Sueyoshi, Yoshiko Miura

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin belong to type III intermediate filament family and are expressed in mesenchymal cells, skeletal muscle cells, astrocytes and peripheral neurons, respectively. Vimentin and desmin possess N-acetyl-d-glucosamine (GlcNAc)-binding properties on cell surfaces. The rod II domain of these proteins is a GlcNAc-binding site, which also exists in GFAP and peripherin. However, the GlcNAc-binding activities and behaviors of these proteins remain unclear. Here, we characterized the interaction and binding behaviors of these proteins, using various well-defined GlcNAc-bearing polymers synthesized by radical polymerization with a reversible addition-fragmentation chain transfer reagent. The small GlcNAc-bearing polymers strongly interacted with HeLa cells through vimentin expressed on the cell surface and interacted with vimentin-, desmin-, GFAP- and peripherin-transfected vimentin-deficient HeLa cells. These proteins present high affinity to GlcNAc-bearing polymers, as shown by surface plasmon resonance. These results show that type III intermediate filament proteins possess GlcNAc-binding activities on cell surfaces. These findings provide important insights into novel cellular functions and physiological significance of type III intermediate filaments.

Original languageEnglish
Pages (from-to)900-917
Number of pages18
JournalGenes to Cells
Volume22
Issue number10
DOIs
Publication statusPublished - Oct 2017

Fingerprint

Intermediate Filament Proteins
Vimentin
Peripherins
Polymers
Desmin
Glial Fibrillary Acidic Protein
Intermediate Filaments
HeLa Cells
Surface Plasmon Resonance
Glucosamine
Astrocytes
Polymerization
Muscle Cells
Carrier Proteins
Skeletal Muscle
Proteins
Binding Sites
Neurons

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

Cite this

Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers. / Ise, Hirohiko; Yamasaki, Sadanori; Sueyoshi, Kazuaki; Miura, Yoshiko.

In: Genes to Cells, Vol. 22, No. 10, 10.2017, p. 900-917.

Research output: Contribution to journalArticle

@article{3a19d0b4ba664f14b1a16a9dbc056920,
title = "Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers",
abstract = "Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin belong to type III intermediate filament family and are expressed in mesenchymal cells, skeletal muscle cells, astrocytes and peripheral neurons, respectively. Vimentin and desmin possess N-acetyl-d-glucosamine (GlcNAc)-binding properties on cell surfaces. The rod II domain of these proteins is a GlcNAc-binding site, which also exists in GFAP and peripherin. However, the GlcNAc-binding activities and behaviors of these proteins remain unclear. Here, we characterized the interaction and binding behaviors of these proteins, using various well-defined GlcNAc-bearing polymers synthesized by radical polymerization with a reversible addition-fragmentation chain transfer reagent. The small GlcNAc-bearing polymers strongly interacted with HeLa cells through vimentin expressed on the cell surface and interacted with vimentin-, desmin-, GFAP- and peripherin-transfected vimentin-deficient HeLa cells. These proteins present high affinity to GlcNAc-bearing polymers, as shown by surface plasmon resonance. These results show that type III intermediate filament proteins possess GlcNAc-binding activities on cell surfaces. These findings provide important insights into novel cellular functions and physiological significance of type III intermediate filaments.",
author = "Hirohiko Ise and Sadanori Yamasaki and Kazuaki Sueyoshi and Yoshiko Miura",
year = "2017",
month = "10",
doi = "10.1111/gtc.12535",
language = "English",
volume = "22",
pages = "900--917",
journal = "Genes to Cells",
issn = "1356-9597",
publisher = "Wiley-Blackwell",
number = "10",

}

TY - JOUR

T1 - Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers

AU - Ise, Hirohiko

AU - Yamasaki, Sadanori

AU - Sueyoshi, Kazuaki

AU - Miura, Yoshiko

PY - 2017/10

Y1 - 2017/10

N2 - Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin belong to type III intermediate filament family and are expressed in mesenchymal cells, skeletal muscle cells, astrocytes and peripheral neurons, respectively. Vimentin and desmin possess N-acetyl-d-glucosamine (GlcNAc)-binding properties on cell surfaces. The rod II domain of these proteins is a GlcNAc-binding site, which also exists in GFAP and peripherin. However, the GlcNAc-binding activities and behaviors of these proteins remain unclear. Here, we characterized the interaction and binding behaviors of these proteins, using various well-defined GlcNAc-bearing polymers synthesized by radical polymerization with a reversible addition-fragmentation chain transfer reagent. The small GlcNAc-bearing polymers strongly interacted with HeLa cells through vimentin expressed on the cell surface and interacted with vimentin-, desmin-, GFAP- and peripherin-transfected vimentin-deficient HeLa cells. These proteins present high affinity to GlcNAc-bearing polymers, as shown by surface plasmon resonance. These results show that type III intermediate filament proteins possess GlcNAc-binding activities on cell surfaces. These findings provide important insights into novel cellular functions and physiological significance of type III intermediate filaments.

AB - Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin belong to type III intermediate filament family and are expressed in mesenchymal cells, skeletal muscle cells, astrocytes and peripheral neurons, respectively. Vimentin and desmin possess N-acetyl-d-glucosamine (GlcNAc)-binding properties on cell surfaces. The rod II domain of these proteins is a GlcNAc-binding site, which also exists in GFAP and peripherin. However, the GlcNAc-binding activities and behaviors of these proteins remain unclear. Here, we characterized the interaction and binding behaviors of these proteins, using various well-defined GlcNAc-bearing polymers synthesized by radical polymerization with a reversible addition-fragmentation chain transfer reagent. The small GlcNAc-bearing polymers strongly interacted with HeLa cells through vimentin expressed on the cell surface and interacted with vimentin-, desmin-, GFAP- and peripherin-transfected vimentin-deficient HeLa cells. These proteins present high affinity to GlcNAc-bearing polymers, as shown by surface plasmon resonance. These results show that type III intermediate filament proteins possess GlcNAc-binding activities on cell surfaces. These findings provide important insights into novel cellular functions and physiological significance of type III intermediate filaments.

UR - http://www.scopus.com/inward/record.url?scp=85031503177&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85031503177&partnerID=8YFLogxK

U2 - 10.1111/gtc.12535

DO - 10.1111/gtc.12535

M3 - Article

C2 - 28898551

AN - SCOPUS:85031503177

VL - 22

SP - 900

EP - 917

JO - Genes to Cells

JF - Genes to Cells

SN - 1356-9597

IS - 10

ER -