The glycosylation of haptoglobin in rheumatoid arthritis

Thompson, Stephen; Dargan, Everett L.; Griffiths, I. D.; Kelly, Carol; Turner, G. A.

doi:10.1016/0009-8981(93)90011-r

Cited by 44 publications

(25 citation statements)

References 14 publications

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“…Acute phase reactant proteins, such as haptoglobin, have been shown to circulate at higher levels in patients with inflammatory diseases and cancer (Thompson et al, 1993;Shah et al, 2010). Haptoglobin is synthesized in the liver, and higher concentrations of haptoglobin have been observed in tumor tissues (Ahmed et al, 2004;Takeda et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Haptoglobin Levels in Turkish Patients with Bladder Cancer and its Association with Clinicopathological Features

Kaba

Pirinççi

Benli̇³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Section: Discussionmentioning

confidence: 99%

Haptoglobin Levels in Turkish Patients with Bladder Cancer and its Association with Clinicopathological Features

Kaba

Pirinççi

Benli̇³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…This is consistent with many previous observations on increased levels of acute phase proteins such as haptoglobin in the sera of patients with inflammatory diseases and cancer. 19,30,31 This may be due to the epithelial-mesenchymal transition phenomenon. Furthermore, actively-growing tumor cells show many similar properties to inflammatory cells, particularly activated fibroblasts.…”

Section: Discussionmentioning

confidence: 99%

Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects

Fujimura

Shinohara

Tissot

et al. 2007

Intl Journal of Cancer

114

115

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We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results. (i) Haptoglobin level was enhanced significantly in sera of prostate cancer. (ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan. The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease. (iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis x/a antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the b-chain of prostate cancer, and were minimal in benign prostate disease. Fucosylated glycans were not observed in normal subjects. A minor tri-antennary N-linked glycan was observed at N241 of the b-chain in prostate cancer, which was absent in benign prostate disease. (iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcb4(NeuAca3)Galb3(NeuAca6)GlcNAcbGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2. (v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time. Monoand disialyl core Type 1 O-linked structures were identified after reductive b-elimination followed by methylation and mass spectrometric analysis. No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this Oglycan core. In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its b-chain are characterized by enhanced branching as well as antenna fucosylation. ' 2007 Wiley-Liss, Inc.

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“…AGP increases in RA, and alteration in its glycans detected by lectin binding has been reported [3]. Another major glycoprotein, transferrin, accounts for a small proportion of the tri-antennary oligosaccharides found in healthy adults [22], and IgG and haptoglobin reportedly exhibit bi-antennary [23,24] rather than tri-antennary oligosaccharides. However, alteration in AGP N-glycans in RA is reported to involve only fucosylation, and proteomic analysis of serum in RA using 2-D PAGE and lectins shows changes in IgG, haptoglobin, and two unknown glycoproteins, but not in AGP [8].…”

Section: Discussionmentioning

confidence: 99%

Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients

Nakagawa

Hato

Takegawa

et al. 2007

Journal of Chromatography B

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Altered N-glycosylation occurs in many diseases. In rheumatoid arthritis (RA), for example, reduction in galactose residues in IgG and an increase in fucose residues in α1-acid glycoprotein have been observed. To further analysis of N-glycans in disease, we show N-glycan profiling from whole serum employing reversed phase high performance liquid chromatography/negative-ion mode by sonic spray ionization ion trap mass spectrometry with pyridylamination. Profiles from female 15 RA patients and 18 aged-matched healthy women were compared. The most significant change seen in RA was decreased levels of mono-galactosyl bi-antennary N-glycans, in agreement with previous reports regarding IgG.We also show previously unreported differences between isomers and increased tri-antennary oligosaccharides. These results indicate that LC-MS analysis of whole serum N-glycans can identify N-glycan alterations in RA and that this is a promising method both for studies of RA mechanisms and diagnosis.

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The glycosylation of haptoglobin in rheumatoid arthritis

Cited by 44 publications

References 14 publications

Haptoglobin Levels in Turkish Patients with Bladder Cancer and its Association with Clinicopathological Features

Haptoglobin Levels in Turkish Patients with Bladder Cancer and its Association with Clinicopathological Features

Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects

Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients

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