No abstract available.
Acute Coronary Syndrome* ; Blood Platelets* ; Glycoproteins*

Blood Platelets ; Humans ; Platelet Membrane Glycoproteins ; Thrombosis

No abstract available.
Aged* ; Blood Platelets* ; Glycoproteins* ; Humans ; Myocardial Infarction* ; Percutaneous Coronary Intervention*

No abstract available.
Blood Platelets* ; Electrophoresis, Polyacrylamide Gel* ; Membrane Glycoproteins* ; Membranes* ; Thrombasthenia*

OBJECTIVETo identify specific serum glycoprotein profiles that correspond to the carcinogenic process of primary liver cancer (PLC) by analyzing a population with high-incidence of PLC using lectin affinity microarray.

METHODSSerum samples were collected from individuals classified as high risk for PLC (including patients with liver cirrhosis and hepatitis B) and development of PLC was recorded. Healthy individuals served as normal controls. The serum samples were subjected to glycoprotein profling by using lectin microarrays and the results were confirmed by lectin blot. Between-group differences were statistically analyzed.

RESULTSPLC carcinogenesis was found to be correlated with enhanced affinity for AAL, ACL, ConA, LCA, MPL, NML, PHA-E, PHA-L, PSA, RCA-I, STL, VAL,WGA, and SNA (P less than 0.05). These data implied that changes in specific glycan structures, such as aFuc, GlcNAc, GalNAc, mannose, bisecting GlcNAc and terminal beta1-4 Gal, may be involved in PLC carcinogenesis . The PLC group showed significantly different results for all detected lectins, except SNA (P less than 0.05). However, among the PLC group, the SNA affinity was not significantly different for the hepatitis B group (P =0.443, P more than 0.05).

CONCLUSIONGlycans may be associated with the carcinogenic process of PLC and may be developed as diagnostic and prognostic biomarkers of PLC in the future.

Carcinogenesis ; Chromatography, Affinity ; Cohort Studies ; Glycoproteins ; blood ; Humans ; Lectins ; blood ; Liver Neoplasms ; blood ; pathology

BACKGROUND: A previous history of transfusion has been known to be associated with production of anti-HLA class I antibodies. However, platelet glycoproteins are the main target of idiopathic thrombocytopenic purpura (ITP). The mechanism of antibody production is known to differ significantly between glycoproteins and anti-HLA class I. The aim of this study was to evaluate the clinical significance of anti-HLA class I antibodies in childhood ITP. METHODS: Enrollment for the normal control group targeted 48 people who visited Gyeongsang National University Hospital from 1990 to 2010, and 48 young children with ITP. Anti-glycoproteins and anti-HLA class I antibodies were tested using the Modified Antigen Capture Enzyme-linked immunosorbent assay (MACE) kit. RESULTS: The positive rate of anti-HLA antibodies was significantly different [36/39 (92.3%) vs 29/46 (63%)] [ITP group vs normal control group] (P=0.002). The mean positive S/C ratio of anti-HLA antibodies was also significantly different (3.55 vs 1.51) [ITP group vs normal control group] (P=0.0000). The positive rate of anti-HLA did not differ significantly between the transfused group and the non-transfused group [12/12 (100%) vs 24/27 (88%)] [transfused ITP vs non-transfused ITP]. The mean positive S/C ratio of anti-HLA antibodies did not differ significantly between the transfused ITP group and the non-transfused ITP group (4.30 vs 3.25) [transfused ITP vs non-transfused ITP]. Consecutive testing showed that positive rate and positive S/C ratio of anti-HLA antibodies did not change significantly between sampling times in both groups [transfused ITP vs non-transfused ITP] (P=1.00 and P=0.15). CONCLUSION: Anti-HLA class I antibodies may be involved in childhood ITP. Transfusion did not affect the course of childhood ITP.
Antibodies* ; Antibody Formation ; Blood Platelets* ; Child* ; Enzyme-Linked Immunosorbent Assay ; Glycoproteins ; Humans ; Platelet Membrane Glycoproteins ; Purpura, Thrombocytopenic, Idiopathic*

Biomarkers ; blood ; Clinical Laboratory Techniques ; Glycoproteins ; blood ; Humans ; Liver Cirrhosis ; diagnosis

PURPOSE: The serum levels of soluble triggering receptor expressed on myeloid cells-1 (sTREM-1) have recently been shown to be correlated highly with disease activity in patients with intestinal Behcet's disease (BD). However, it remains unclear whether sTREM-1 levels reflect endoscopic activity in intestinal BD. This study aimed to evaluate the correlation of sTREM-1 levels with endoscopic activity in intestinal BD. MATERIALS AND METHODS: A total of 84 patients with intestinal BD were enrolled. Endoscopic activity was compared with sTREM-1 levels as well as other laboratory findings, including erythrocyte sedimentation rate (ESR) and C-reactive protein (CRP). RESULTS: sTREM-1 levels were significantly increased in intestinal BD patients compared with controls (37.98+/-27.09 pg/mL vs. 16.65+/-7.76 pg/mL, p=0.002), however, there was no difference between endoscopically quiescent and active diseases (43.53+/-24.95 pg/mL vs. 42.22+/-32.68 pg/mL, p=0.819). Moreover, serum sTREM-1 levels did not differ in terms of number, shape, depth, size, margin, or type of ulcer in patients with intestinal BD. However, mean ESR and CRP levels in patients with active disease were significantly higher than those in patients with quiescent disease (p=0.001, p<0.001, respectively). In addition, endoscopic activity scores for intestinal BD were correlated significantly with both CRP levels (gamma=0.329) and ESR (gamma=0.298), but not with sTREM-1 levels (gamma=0.166). CONCLUSION: Unlike CRP levels and ESR, serum sTREM-1 levels were not correlated with endoscopic activity in patients with intestinal BD.
Adult ; Behcet Syndrome/*blood/*pathology ; Biological Markers/blood ; Blood Sedimentation ; C-Reactive Protein/metabolism ; Female ; Humans ; Intestinal Diseases/*blood/*pathology ; Male ; Membrane Glycoproteins/*blood ; Receptors, Immunologic/*blood

BACKGROUND: Ulinastatin, a urinary trypsin inhibitor, is widely used to treat acute systemic inflammatory disorders. However, the effects of ulinastatin, especially on the potential for hemostasis, have not been fully elucidated. This study examined whether ulinastatin had any beneficial effects on blood loss and blood transfusion requirements in patients undergoing major orthopedic surgery. METHODS: Eighty patients, aged 18 to 75 years, scheduled for major orthopedic surgery were enrolled in this study and were divided into the ulinastatin (n = 40) and control (n = 40) groups. Following the induction of general anesthesia, and immediately before the surgical incision, the patients in the ulinastatin group were given 5,000 units/kg of ulinastatin, which were mixed in 100 ml normal saline intravenously over 30 min, while those in the control group received the same volume of normal saline. The amounts of blood loss, infused fluid, and transfused blood products were measured throughout the study period. Blood samples for coagulation parameters were obtained before inducing anesthesia (T1), at the end of surgery (T2), and 12 h after surgery (T3). RESULTS: The amounts of blood loss and infused fluid during surgery were not significantly different between the two groups. However, 12 h postoperative blood loss was significantly less in the ulinastatin group than in the control group (255.0 +/- 133.2 ml VS. 395.4 +/- 338.4 ml, P < 0.05). CONCLUSIONS: Our data suggest that a single infusion of ulinastatin in major orthopedic surgery is associated with decreased blood loss in the early postoperative period.
Aged ; Anesthesia ; Anesthesia, General ; Blood Transfusion ; Glycoproteins ; Hemostasis ; Humans ; Orthopedics ; Postoperative Hemorrhage ; Postoperative Period ; Trypsin

The binding of microorganisms to platelets is a critical step in the development of infective endocarditis. In Streptococcus gordonii, this binding is mediated in part by serine-rich repeat proteins, which interact directly with sialic acid residues located on GPIIb receptors in the platelet membrane. In this study, we found that S. gordonii DL1 strain binds to platelets through bridging between sialic acid residue of fibronectin and serine-rich repeat protein (Hsa). Pretreatment of fibronectin with sialidases specific for alpha(2-3)-linked sialic acids was shown to significantly inhibit binding of the DL1 strain and the binding region(BR) of Hsa protein. Similarly, pre-incubation of bacteria or BR of Hsa with alpha(2-3)-sialyl-N-acetyllactosamine blocked fibronectin binding in the DL1 strain, but not the M99 strain. Together, these data show that the alpha(2-3)-sialic acid residues of fibronectin play an important role in the binding of S. gordonii DL1 to fibronectin through interactions with the Hsa receptor. This interaction is thought to play an important role in the development of pathogenic endocarditis, and may represent an important therapeutic target for the treatment of infective endocarditis.
Bacteria ; Blood Platelets ; Endocarditis ; Etorphine ; Fibronectins* ; Membrane Glycoproteins* ; Membranes ; N-Acetylneuraminic Acid* ; Sialic Acids ; Streptococcus gordonii*