Syndecan 1 (CD138) serum levels: A novel biomarker in predicting liver fibrosis stage in patients with hepatitis C
Syndecan 1 (CD 138) is a cell surface proteoglycan shed by cells in several pathological conditions, including wound healing. The aim of this study was to test whether CD138 could serve as a non-invasive marker for detection of liver fibrosis and thereby reduce the need for liver biopsy.
An estimation set of 134 patients and a validation set of 67 patients with chronic hepatitis C were studied. There were 80 normal healthy volunteers. Patients were staged according to liver biopsies (Metavir fibrosis staging, stage F0, n=35; F1, n=40; F2, n=37, F3, n=39; F4, n=51). Serum CD138 levels were retrospectively measured by enzyme-linked immunoabsorbent assay the same day of the liver biopsy. The primary endpoints were the diagnostic values of CD138 for F2-F4, F3-F4 and F4.
Respective areas under receiver operating characteristic curve of CD138 for F2-F4, F3-F4 and F4 diagnosis were 0.82, 0.76 and 0.81. CD138 had a positive predictive value of 82% for F2-F4 diagnosis and a high negative predictive value (86%) and specificity (84%) for exclusion of F4.
CD138 is a new simple non-invasive marker for predicting liver fibrosis in patients with chronic hepatitis C. The relevance of this marker in combination with other fibrosis markers should be explored.
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Available from: Pyong Woo Park
- "Soluble syndecan-1 and -4 ectodomains are detected in inflamed or infected body fluids, indicating a physiological role for shedding in diseases (Subramanian et al. 1997; Wang et al. 2008; Zvibel et al. 2009). Syndecan ectodomains are replete with all of their HS chains and are thought to maintain their ability to interact with the same ligands as the cell surface syndecans, and thus act as soluble autocrine or paracrine effectors. "
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ABSTRACT: To cause infections, microbial pathogens elaborate a multitude of factors that interact with host components. Using these
host–pathogen interactions to their advantage, pathogens attach, invade, disseminate, and evade host defense mechanisms to
promote their survival in the hostile host environment. Many viruses, bacteria, and parasites express adhesins that bind to
cell surface heparan sulfate proteoglycans (HSPGs) to facilitate their initial attachment and subsequent cellular entry. Some
pathogens also secrete virulence factors that modify HSPG expression. HSPGs are ubiquitously expressed on the cell surface
of adherent cells and in the extracellular matrix. HSPGs are composed of one or several heparan sulfate (HS) glycosaminoglycan
chains attached covalently to specific core proteins. For most intracellular pathogens, cell surface HSPGs serve as a scaffold
that facilitates the interaction of microbes with secondary receptors that mediate host cell entry. Consistent with this mechanism,
addition of HS or its pharmaceutical functional mimic, heparin, inhibits microbial attachment and entry into cultured host
cells, and HS-binding pathogens can no longer attach or enter cultured host cells whose HS expression has been reduced by
enzymatic treatment or chemical mutagenesis. In pathogens where the specific HS adhesin has been identified, mutant strains
lacking HS adhesins are viable and show normal growth rates, suggesting that the capacity to interact with HSPGs is strictly
a virulence activity. The goal of this chapter is to provide a mechanistic overview of our current understanding of how certain
microbial pathogens subvert HSPGs to promote their infection, using specific HSPG–pathogen interactions as representative
Glycans in Diseases and Therapeutics, 04/2011: pages 31-62;
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ABSTRACT: We investigated the xylosyltransferase (XT) activity in the serum of liver fibrotic patients with hepatitis C virus induced liver fibrosis at different stages as determined according to the scoring system of Desmet and Scheuer.
Measurement of XT activity was performed by liquid chromatography-tandem mass spectrometry.
We found that serum XT activity in males (n=59, median+/-SD, 27.2+/-2.8 mU/L, p<0.001) and females (n=54, 23.6+/-3.0 mU/L, p<0.01) with liver fibrosis is significantly elevated in comparison to a corresponding healthy control cohort of males (n=50, 23.9+/-2.8 mU/L) and females (n=52, 21.5+/-3.7 mU/L), respectively. Of note, independent from gender, serum XT activity positively correlated with the stage of fibrosis but declined again in patients with histologically proven cirrhosis.
XT activity is increased in the serum of patients with liver fibrosis at different stages, pointing to a possible pathogenetic role in elevated proteoglycan biosynthesis in fibrotic remodeling of this organ during chronic injury.
Clinica chimica acta; international journal of clinical chemistry 09/2009; 409(1-2):123-6. DOI:10.1016/j.cca.2009.09.013 · 2.82 Impact Factor
Available from: Mark W M Schellings
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ABSTRACT: Syndecan-1 (Synd1) is a transmembrane heparan sulfate proteoglycan that functions as a coreceptor for various growth factors and modulates signal transduction. The present study investigated whether Synd1, by affecting growth factor signaling, may play a role in hypertension-induced cardiac fibrosis and dysfunction. Expression of Synd1 was increased significantly in mouse hearts with angiotensin II-induced hypertension, which was spatially related to cardiac fibrosis. Angiotensin II significantly impaired fractional shortening and induced cardiac fibrosis in wild-type mice, whereas these effects were blunted in Synd1-null mice. Angiotensin II significantly increased cardiac expression of connective tissue growth factor and collagen type I and III in wild-type mice, which was blunted in Synd1-null mice. These findings were confirmed in vitro, where angiotensin II induced the expression of both connective tissue growth factor and collagen I in fibroblasts. The absence of Synd1 in either Synd1-null fibroblasts, after knockdown of Synd1 by short hairpin RNA, or after inhibition of heparan sulfates by protamine attenuated this increase, which was associated with reduced phosphorylation of Smad2. In conclusion, loss of Synd1 reduces cardiac fibrosis and dysfunction during angiotensin II-induced hypertension.
Hypertension 02/2010; 55(2):249-56. DOI:10.1161/HYPERTENSIONAHA.109.137885 · 6.48 Impact Factor
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