The glycosylation sites and structural characteristics of oligosaccharides on recombinant human thrombomodulin

Edano, Toshiyuki; Kumai, Natuyo; Mizoguchi, Toshimi; Ohkuchi, Masao

doi:10.1016/s1357-2725(97)00078-2

Cited by 12 publications

(6 citation statements)

References 23 publications

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“…TM glycosylation in relation to biological activity has been discussed in several papers (12)(13)(14), but to understand the structure and biological activities of the glycoprotein, detailed knowledge of the sugar structures is essential. Recently, the structures of N-linked sugar chains have been reported (15). During the course of studies on N-and O-linked sugar chains of uTM, we have detected new structures with xylose at the reducing ends.…”

mentioning

confidence: 80%

Novel Proteoglycan Linkage Tetrasaccharides of Human Urinary Soluble Thrombomodulin, SO4-3GlcAβ1–3Galβ1–3(±Siaα2–6)Galβ1–4Xyl

Wakabayashi¹,

Natsuka²,

Mega³

et al. 1999

Journal of Biological Chemistry

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O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied. Sugar chains were liberated by hydrazinolysis followed by N-acetylation and tagged with 2-aminopyridine. Two fractions containing pyridylaminated Xyl as a reducing end were collected. Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO 4 -3GlcA␤1-3Gal␤1-3(؎Sia␣2-6)Gal␤1-4Xyl. These sugar chains could bind to an HNK-1 monoclonal antibody. This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.

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mentioning

confidence: 80%

Novel Proteoglycan Linkage Tetrasaccharides of Human Urinary Soluble Thrombomodulin, SO4-3GlcAβ1–3Galβ1–3(±Siaα2–6)Galβ1–4Xyl

Wakabayashi¹,

Natsuka²,

Mega³

et al. 1999

Journal of Biological Chemistry

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“…A serine/threonine‐rich region extends between the sixth EGF module and the transmembrane domain, and contains several target sites for post‐translational N ‐ and O ‐glycosylation, in particular addition of a chondroitin sulfate moiety [20,21]. Soluble TM isolated from urine, and some forms of recombinant soluble TM do not contain this sugar chain [22–28]. The short cytoplasmic tail does not possess any similarity to protein domains with known function in signal transduction or protein–protein interactions.…”

Section: Thrombomodulin Function and Structurementioning

confidence: 99%

Thrombomodulin

and

Isermann

2003

Journal of Thrombosis and Haemostasis

245

196

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Summary. Since its discovery as a critical cofactor in the initiation of the protein C (PC) anticoagulant pathway [1,2], biochemical and structural investigations, combined with in vivo analyses of genetically engineered mice have revealed new, and in part PC‐ and thrombin‐independent aspects of thrombomodulin (TM) function in fibrinolysis and inflammation, and in embryogenesis. This review summarizes more recent structural and functional investigations of TM, gives an overview of the association of TM gene polymorphisms with human disease, and provides a synopsis of what is know about TM function in disease states of thrombosis, stroke, arteriosclerosis, and cancer. Newly emerging aspects of TM function in inflammation and embryogenesis are presented and discussed in detail.

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“…In our study the mean level of U-TM was 28 folds higher than P-TM in the normal control group. The difference in the level of TM in plasma and urine in normal subjects could be attributed to their different origin [11,12].…”

Section: Discussionmentioning

confidence: 99%

“…The level of circulating P-TM may be useful as a critical marker of vascular endothelial damage, disease recurrence and angiogenesis in certain malignancies [9]. The electrophoretic mobility of U-TM was found to be similar to that of P-TM and lack 29 amino acid of the c-terminal sequence of cellular thrombomodulin [12]. According to studies conducted in the National Cancer Institute of Egypt: bladder cancer continues to be the most frequent cancer today in Egyptian men and 32% of all malignant tumor registered in the NCI.…”

Section: Introductionmentioning

confidence: 96%

Urinary thrombomodulin is down regulated in schistosomiasis associated bladder cancer

Refaat

Ali

Hassan

et al. 2012

Journal of Genetic Engineering and Biotechnology

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Background: Thrombomodulin (TM) is a surface glycoprotein and expressed in many cancers. The aim of the present study was to detect the expression levels of TM in plasma and urine of bladder cancer patients and to compare these levels to the clinicopathological data of the patients as well as the ploidy status of their exfoliated urinary cells. We studied the levels of TM in plasma and urine samples of 57 bladder cancer patients and 10 controls using the (ELISA) assay and compared the results to the ploidy status of the cells taken from the patents urine samples as well as their clinicopathological profile.Results: Urinary TM was significantly down regulated while plasma TM was significantly up regulated in bladder cancer patients. Plasma TM was significantly higher in SCC than TCC patients. The sensitivity and specificity of urinary TM were 90% and 86%, respectively. While the sensitivity and specificity of plasma TM were 76% and 80%, respectively.Conclusion: Urinary TM is significantly down regulated, while plasma TM is significantly up regulated in bladder cancer as compared to the control group. Urinary TM has superior sensitivity and specificity over plasma TM. Urinary TM could be used as a predictive marker in bladder cancer. Further studies are needed to detect the prognosis significance of thrombomodulin in schistosomiasis associated bladder cancer.

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The glycosylation sites and structural characteristics of oligosaccharides on recombinant human thrombomodulin

Cited by 12 publications

References 23 publications

Novel Proteoglycan Linkage Tetrasaccharides of Human Urinary Soluble Thrombomodulin, SO4-3GlcAβ1–3Galβ1–3(±Siaα2–6)Galβ1–4Xyl

Novel Proteoglycan Linkage Tetrasaccharides of Human Urinary Soluble Thrombomodulin, SO4-3GlcAβ1–3Galβ1–3(±Siaα2–6)Galβ1–4Xyl

Thrombomodulin

Urinary thrombomodulin is down regulated in schistosomiasis associated bladder cancer

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