N-glycosylation status of β-haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects

Seung Yeol Park, Seon Joo Yoon, Yeon Tae Jeong, Jin Man Kim, Ji Yeon Kim, Bradford Bernert, Thomas A. Ullman, Steven H. Itzkowitz, Jung Hoe Kim, Sen Itiroh Hakomori

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

N-glycosylation status of purified β-haptoglobin from sera of 17 patients, and from sera of 14 healthy volunteer subjects, was compared by blotting with various lectins and antibodies. Patients in this study were diagnosed as having colon cancer through histological examination of each tumor tissue by biopsy. Blotting index of serum β-haptoglobin with Aleuria aurantia lectin (AAL) was clearly higher for cancer patients than for healthy subjects. No such distinction was observed for blotting with three other lectins and two monoclonal antibodies. To determine tumor-associated reactivity of AAL binding as compared to inflammatory processes in colonic tissues, β-haptoglobin separated from sera of 5 patients with Crohn's disease (CD), and 4 patients with ulcerative colitis (UC), was studied. All these cases, except one case of UC, showed AAL index lower than that in cancer cases, similarly to healthy subjects. The higher AAL binding of β-haptoglobin in colon cancer patients than in healthy subjects appeared to be due to α-L-fucosyl residue, since it was eliminated by bovine kidney α-fucosidase treatment. N-linked glycans of serum haptoglobin from colon cancer patients vs. healthy subjects were released by N-glycanase, fluorescence-labeled, and subjected to normal-phase high performance liquid chromatography (NP-HPLC). Glycan structures were determined based on glucose unit (GU) values and their changes upon sequential treatment with various exoglycosidases. Glycosyl sequences and their branching status of glycans from 14 cases of serum β-haptoglobin were characterized. The identified glycans were sialylated or nonsialylated, bi-antennary or tri-antennary structures, with or without terminal fucosylation.

Original languageEnglish (US)
Pages (from-to)142-155
Number of pages14
JournalInternational Journal of Cancer
Volume126
Issue number1
DOIs
StatePublished - Jan 1 2010
Externally publishedYes

Fingerprint

Haptoglobins
Glycosylation
Colonic Neoplasms
Chronic Disease
Healthy Volunteers
Polysaccharides
Serum
Ulcerative Colitis
Lectins
Neoplasms
alpha-L-Fucosidase
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Glycoside Hydrolases
Crohn Disease
Fluorescence
High Pressure Liquid Chromatography
Monoclonal Antibodies
Kidney
Biopsy
Glucose

Keywords

  • Colon cancer
  • Haptoglobin
  • HPLC
  • Lectin blotting
  • N-linked glycan

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

N-glycosylation status of β-haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects. / Park, Seung Yeol; Yoon, Seon Joo; Jeong, Yeon Tae; Kim, Jin Man; Kim, Ji Yeon; Bernert, Bradford; Ullman, Thomas A.; Itzkowitz, Steven H.; Kim, Jung Hoe; Hakomori, Sen Itiroh.

In: International Journal of Cancer, Vol. 126, No. 1, 01.01.2010, p. 142-155.

Research output: Contribution to journalArticle

Park, SY, Yoon, SJ, Jeong, YT, Kim, JM, Kim, JY, Bernert, B, Ullman, TA, Itzkowitz, SH, Kim, JH & Hakomori, SI 2010, 'N-glycosylation status of β-haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects', International Journal of Cancer, vol. 126, no. 1, pp. 142-155. https://doi.org/10.1002/ijc.24685
Park, Seung Yeol ; Yoon, Seon Joo ; Jeong, Yeon Tae ; Kim, Jin Man ; Kim, Ji Yeon ; Bernert, Bradford ; Ullman, Thomas A. ; Itzkowitz, Steven H. ; Kim, Jung Hoe ; Hakomori, Sen Itiroh. / N-glycosylation status of β-haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects. In: International Journal of Cancer. 2010 ; Vol. 126, No. 1. pp. 142-155.
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