No Abstract Available.
Heparitin Sulfate* ; Orientia tsutsugamushi*

No abstract available.
Glomerular Basement Membrane* ; Heparan Sulfate Proteoglycans* ; Heparitin Sulfate*

Heparan sulfate (HS) is ubiquitously expressed on the surfaces and in the extracellular matrix of virtually all cell types, making it an ideal receptor for viral infection. Compared with wild-type viruses, cell culture-adapted laboratory strains exhibit more efficient binding to cellular HS receptors. HS-binding viruses are typically cleared faster from the circulation and cause lower viremia than their non-HS-binding counterparts, suggesting that the HS-binding phenotype is a tissue culture adaptation that lowers virus fitness in vivo. However, when inoculated intracranially, efficient cell attachment through HS binding can contribute to viral neurovirulence. The primary aim of this review is to discuss the roles of HS binding in viral pathogenicity, including peripheral virulence and neurovirulence. Understanding how heparan sulfate functions during virus infection in vivo may prove critical for elucidating the molecular mechanism of viral pathogenesis, and may contribute to the development of therapeutics targeting HS.
Heparitin Sulfate ; physiology ; Humans ; Receptors, Virus ; physiology ; Virulence ; Viruses ; pathogenicity

Heparinases can produce biologically active oligosaccharides by specifically cleaving the α-(1,4) glycosidic linkages of heparin and heparan sulphate. Heparinases are divided into heparinase and heparanase. Because heparinase is an effective biocatalyst, more and more researchers pay attention to the application of heparinase in medical field in the recent years. Combined with the related research work in our group, the application value of heparinase in the medical field was summarized, such as the determination of the structure of heparin, the preparation of low-molecular-weight heparin and ultra-low-molecular-weight heparin, tumor therapy and as a heparin antagonist. In addition, we summarized the definition, source of heparinase and its application in the medicine field. Heparinases have a great application prospect in the field of medicine.
Heparin ; Heparin Lyase ; metabolism ; Heparitin Sulfate ; Oligosaccharides ; Polysaccharide-Lyases

Gingival fibroblasts are embedded in an extracellular matrix. The matrixs have influence on the development, polarity, and behavior of nearby cells. The major component of periodontal extracellular matrix is a glycosaminoglycan. The glycosaminoglycan are large carbohydrates that are composed of repeating disaccharide units and exist in three main form: dermatan sulfate, chondrotitin sulfate, heparan sulfate. The purpose of present study is to examine the biologic effects of glycosaminoglycan on human gingival fibroblast. Human gingival fibroblasts were supplemented with each glycosaminoglycan, and cellular attachment and proliferation was determined by MTT assay. Dermatan sulfate and chondroitin sulfate did not stimulate the attachment and proliferation of human gingival fibroblasts, but heparan sulfate increased the proliferation and attachment in a time- and dose- dependent manner. These results indicated that heparan sulfate seems to have a high potential for gingival regeneration and root surface attachment.
Carbohydrates ; Chondroitin Sulfates ; Dermatan Sulfate ; Extracellular Matrix ; Fibroblasts* ; Heparitin Sulfate ; Humans* ; Regeneration

HSPG, a component of size-and charge-selective barrier of glomerular basement membrane, is one of important matrix proteins which has been known to be reduced in the kidney of diabetic patients or animals. To examine the effects of glucose and AGE on the HSPG production by cultured GEC, we cultured rat GEC on the AGE- or BSA-coated plate under normal(5mM) and high glucose.(30mM) conditions and measured the change of HSPG production by sandwich-ELISA assay and northern blot analysis at 2 days and one week incubation periods. There was no difference in proliferation between 2 different conditions of culture plate surface. We measured the relative amount of the extracted HSPC and observed significant decreases in high glucose condition at one week incubation, and particularly on the AGE-coated surface as compared to the results of BSA-coated condition, by 22% and 5%, respectively. The expression of mRNA for perlecan promoter was decreased in condition of high glucose and AGE-coated surface by 20Yo at 2 days and 61i at one week. Even in normal glucose condition, the expression of mRNA was reduced by 30Yo at one week if the plate was coated with AGE. In conclusion, both high glucose and AGE have reducing effects on the production of HSPG by GEC in vitro. Their effects seem to be additive, however, the role of AGE is greater than that of glucose, This means that the effort to inhibit AGE formation is more important than short-term glucose control for the prevention of diabetic proteinuria.
Animals ; Blotting, Northern ; Diabetic Nephropathies ; Glomerular Basement Membrane ; Glucose* ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate* ; Humans ; Kidney ; Proteinuria ; Rats* ; RNA, Messenger

OBJECTIVE: We evaluated whether serum total bilirubin levels were related to large artery atherosclerosis (LAA), classified by the Trial of Org 10172 in Acute Stroke Treatment (TOAST) classification, and stroke severity at admission in acute ischemic stroke. METHODS: We analyzed clinical features, laboratory tests, and radiologic findings such as brain MRI and MR angiography of patients admitted to our hospital within 24 hours of the onset of ischemic stroke between January 2004 and June 2007. By TOAST classification, 237 patients [115 with LAA and 122 with small artery occlusion (SAO)] were selected. We divided serum total bilirubin levels into three groups: Low (<0.6 mg/dL), Middle (0.6~0.9 mg/dL), and High (1.0~1.2 mg/dL). Stroke severity was assessed using the National Institutes of Health Stroke Scale (NIHSS) at admission. We divided NIHSS scores into three groups: Mild (0-6), Moderate (7-15), and Severe group (>15). RESULTS: Total bilirubin levels were significantly higher in the Mild group than other groups, and high-sensitivity C reactive protein (hsCRP) levels were significantly higher in the Severe group than other groups in LAA. There were no differences for these factors in SAO. We found a significant correlation between total bilirubin levels and stroke severity in LAA (p=0.005). CONCLUSION: Higher serum total bilirubin levels were associated with lower stroke severity at admission in LAA but not SAO.
Angiography ; Arteries ; Atherosclerosis ; Bilirubin ; Brain ; C-Reactive Protein ; Chondroitin Sulfates ; Dermatan Sulfate ; Heparitin Sulfate ; Humans ; National Institutes of Health (U.S.) ; Stroke

Mucopolysaccharidosis type III (MPS III) is a rare genetic disorder caused by lysosomal storage of heparan sulfate. MPS IIIB results from a deficiency in the enzyme alpha-N-acetyl-D-glucosaminidase (NAGLU). Affected patients begin showing behavioral changes, progressive profound mental retardation, and severe disability from the age of 2 to 6 years. We report a patient with MPS IIIB with a long-term follow-up duration. He showed normal development until 3 years. Subsequently, he presented behavioral changes, sleep disturbance, and progressive motor dysfunction. He had been hospitalized owing to recurrent pneumonia and epilepsy with severe cognitive dysfunction. The patient had compound heterozygous c.1444C>T (p.R482W) and c.1675G>T (p.D559Y) variants of NAGLU. Considering that individuals with MPS IIIB have less prominent facial features and skeletal changes, evaluation of long-term clinical course is important for diagnosis. Although no effective therapies for MPS IIIB have been developed yet, early and accurate diagnosis can provide important information for family planning in families at risk of the disorder.
Diagnosis ; Epilepsy ; Family Planning Services ; Follow-Up Studies ; Heparitin Sulfate ; Humans ; Intellectual Disability ; Lysosomal Storage Diseases ; Mucopolysaccharidoses* ; Mucopolysaccharidosis III* ; Pneumonia

PURPOSE: We describe the changes of rat glomerular epithelial cells when exposed to high levels of glucose and advanced glycosylation endproducts(AGE) in the in vitro diabetic condition. We expect morphological alteration of glomerular epithelial cells and permeability changes experimentally and we may correlate the results with a mechanism of proteinuria in DM. METHODS: We made 0.2 M glucose-6-phsphate solution mixed with PBS(pH 7.4) containing 50 mg/mL BSA and protease inhibitor for preparation of AGE. As control, we used BSA. We manufactured and symbolized five culture dishes as follows; B5 - normal glucose(5 mM) + BSA, B30 - high glucose(30 mM) + BSA, A5 - normal glucose(5 mM) + AGE, A30 - high glucose(30 mM) + AGE, A/B 25 - normal glucose(5 mM) + 25 mM of mannitol(osmotic control). After the incubation period of both two days and seven days, we measured the amount of heparan sulfate proteoglycan(HSPG) in each dish by ELISA and compared them with the B5 dish at 2nd and 7th incubation days. We observed the morphological changes of epithelial cells in each culture dish using scanning electron microscopy(SEM). We tried the permeability assay of glomerular epithelial cells using cellulose semi-permeable membrane measuring the amount of filtered BSA through the apical chamber for 2 hours by sandwich ELISA. RESULTS: On the 2nd incubation day, there was no significant difference in the amount of HSPG between the 5 culture dishes. But on the 7th incubation day, the amount of HSPG increased by 10% compared with the B5 dish on the 2nd day except the A30 dish(P<0.05). Compared with the B5 dish on the 7th day the amount of HSPG in A30 and B30 dish decreased to 77.8% and 95.3% of baseline, respectively(P>0.05). In the osmotic control group (A/B 25) no significant correlation was observed. On the SEM, we could see the separated intercellular junction and fused microvilli of glomerular epithelial cells in the culture dishes where AGE was added. The permeability of BSA increased by 19% only in the A30 dish on the 7th day compared with B5 dish on the 7th day in the permeability assay(P<0.05). CONCLUSION: We observed not only the role of a high level of glucose and AGE in decreasing the production of HSPG of glomerular epithelial cells in vitro, but also their additive effect. However, the role of AGE is greater than that of glucose. These results seems to correlate with the defects in charge selective barrier. Morphological changes of the disruption of intercellular junction and fused microvilli of glomerular epithelial cells seem to correlate with the defects in size-selective barrier. Therefore, we can explain the increased permeability of glomerular epithelial units in the in vitro diabetic condition.
Animals ; Cellulose ; Enzyme-Linked Immunosorbent Assay ; Epithelial Cells ; Glucose* ; Glycosylation* ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate ; Intercellular Junctions ; Membranes ; Microvilli ; Permeability* ; Protease Inhibitors ; Proteinuria ; Rats

It is well known that the glomerular basement membrane heparan sulfate proteoglycan(GBM HSPG) synthesized by glomerular epithelial cell(GEC) has an important role in the permeability of glomerular basement membrane and cyclic AMP(cAMP) is involved in regulation of a wide variety of genes maybe including GBM HSPG gene. The direct effect of cAMP on GBM HSPG gene expression and metabolism was not evaluated as yet. Proteinuria represents an impairment of permselectivity function of glomerular basement membrane regulated by GBM HSPG and could be associated with increased glomerular level of cAMP in nephrotic syndrome of diverse causes. RPD-I(rat GBM HSPG core protein domain-I) detected a >9.5kb transcript of GBM HSPG in RNA of rat GEC. Emp1oying a riboprobe synthesized from RPD-I in RNase protection assay, we examined whether cAMP regulated perlecan expression in the GEC. At l, 6, 24 and 48 hrs of incubation, l mM cAMP caused 43%, 32%, 47% and 40% reduction in mRNA expression of perlecan, respectively. Immunoprecipitation showed a corresponding reduction of 51%, 70% and 68% in the synthesis of 35SO4 labeled GBM HSPG by the GEC fol1owing l2, 24 and 48 hrs of incubation with cAMP. Our results show that decrease in GBM HSPG gene expression and synthesis by cAMP may be of relevance to proteinuric states characterized by activation of these mediators.
Animals ; Cyclic AMP* ; Epithelial Cells* ; Gene Expression ; Glomerular Basement Membrane* ; Heparan Sulfate Proteoglycans* ; Heparitin Sulfate* ; Immunoprecipitation ; Metabolism ; Nephrotic Syndrome ; Permeability ; Proteinuria ; Rats* ; Ribonucleases ; RNA ; RNA, Messenger