Cartilage oligomeric matrix protein (COMP) is a potential biomarker for joint destruction associated with osteoarthritis, which is first and best investigated biomarkers to reflect osteoarthritis occurs, progress and the prognosis. In this article, multiple uses and related reports of COMP are summarized briefly to promote further investigation of COMP.
Biomarkers ; blood ; Cartilage Oligomeric Matrix Protein ; Extracellular Matrix Proteins ; blood ; chemistry ; metabolism ; Glycoproteins ; blood ; chemistry ; metabolism ; Humans ; Matrilin Proteins ; Osteoarthritis ; blood ; diagnosis ; Prognosis

Blood compatibility is one of the most important factors for biomaterials applied in blood-contacting environment, which is determined by a series of complicated interactions of biomaterials surfaces with both soluble and cellular components in blood. As the development of molecular biology technology and emergence of new characterization methods for changes of protein conformation structure and function, more and more researchers are making intensive efforts to understand hemocompatibility of biomaterials at molecular and cellular levels. In this paper, developments in understanding of interactions between blood and materials surfaces, especially the changes of plasma protein conformation structure and activation of platelets induced by biomaterials surfaces, are reviewed.
Biocompatible Materials ; chemistry ; Blood ; metabolism ; Blood Proteins ; chemistry ; Humans ; Materials Testing ; methods ; Platelet Activation ; drug effects ; Surface Properties

OBJECTIVETo study the plasma protein binding rate of isopropylidene-shikimic acid.

METHODThe ultrafiltration was employed to determine the plasma protein binding rate of isopropylidene-shikimic acid. The plasma concentrations of isopropylidene-shikimic acid were measured by HPLC.

RESULTThe plasma protein binding rate of isopropylidene-shikimic acid with dog plasma at the concentration of 0.3, 0.15 g x L(-1) and 0.5 mg x L(-1) were (4.36 +/- 0.02)%, (4.12 +/- 0.19)% and (2.23 +/- 0.59)%, respectively. While the plasma protein binding rate of isopropylidene-shikimic acid with normal human plasma at the above concentrations were (11.23 +/- 0.01)%, (10.06 +/- 0.69)% and (9.72 +/- 0.59)%, respectively.

CONCLUSIONThe binding rate of isopropylidene-shikimic acid with plasma protein is low.

Alkenes ; chemistry ; Animals ; Blood Proteins ; metabolism ; Chromatography, High Pressure Liquid ; Dogs ; Humans ; Protein Binding ; Shikimic Acid ; chemistry ; metabolism ; Species Specificity

To clarify the reason causing difference of serum proteins adsorbability on different carbonaceous materials, FT-IR-ATR spectra of human serum albumin (HSA) and human serum fibrinogen(HFG) before and after adsorbing on diamond like carbon film (DLC),diamond film (DF) and graphite were analyzed. It has been shown that there are hydrogen bond because of -NH at the interfaces of HSA-DLC, HFG-DF and HFG-graphite. Based on the results, earlier research conclusion that the adsorbability of HSA on DLC higher than that on DF and graphite, but on DF and graphite the adsorption of HFG takes precedence can be explained rationally.
Adsorption ; Blood Proteins ; metabolism ; Diamond ; chemistry ; Graphite ; chemistry ; Humans ; Hydrogen Bonding ; In Vitro Techniques ; Membranes, Artificial ; Spectroscopy, Near-Infrared

Red blood cell substitutes are a group of oxygen carriers designed to temporarily replace transfused blood. Current developing products include perfluorocarbon-based and hemoglobin-based oxygen carrier. Each product is unique in its limitations and advantages. A number of products are in advanced clinical trials and nearing market. When they are available for use it is likely that development will accelerate and even better products will substantially alleviate the world-wide shortage of blood for transfusion.
Blood Substitutes ; chemistry ; pharmacology ; therapeutic use ; Fluorocarbons ; chemistry ; pharmacology ; therapeutic use ; Hemoglobins ; chemistry ; pharmacology ; therapeutic use ; Humans ; Oxygen ; metabolism ; Recombinant Proteins ; chemistry ; pharmacology ; therapeutic use

In order to investigate peptide mimics of carbohydrate blood group A antigen, a phage display 12-mer peptide library was screened with a monoclonal antibody against blood group A antigen, NaM87-1F6. The antibody-binding properties of the selected phage peptides were evaluated by phage ELISA and phage capture assay. The peptides were co-expressed as glutathione S-transferase (GST) fusion proteins. RBC agglutination inhibition assay was performed to assess the natural blood group A antigen-mimicking ability of the fusion proteins. The results showed that seven phage clones selected bound to NaM87-1F6 specifically, among which, 6 clones bore the same peptide sequence, EYWYCGMNRTGC and another harbored a different one QIWYERTLPFTF. The two peptides were successfully expressed at the N terminal of GST protein. Both of the fusion proteins inhibited the RBC agglutination mediated by anti-A serum in a concentration-dependent manner. These results suggested that the fusion proteins based on the selected peptides could mimic the blood group A antigen and might be used as anti-A antibody-adsorbing materials when immunoabsorption was applied in ABO incompatible transplantation.
Adsorption ; Bacteriophages ; Blood Group Antigens/*chemistry ; Enzyme-Linked Immunosorbent Assay ; Epitopes/chemistry ; Glutathione Transferase/metabolism ; Peptide Library ; Peptides/*chemistry ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry

OBJECTIVESTo detect the cholesterol ester transfer protein (CETP) levels in semen of infertile patients and evaluate the correlation between CETP in semial plasma and infertility.

METHODSOne hundred and sixty-three infertile patients and fifteen fertile males were selected randomly. The routine examination of ejaculates was fulfilled by computer aided semen analysis (CASA). The CETP levels in all seminal plasma samples and fifty-five serum samples were detected by ELISA method.

RESULTSThe CETP levels in infertile patients and fertile males were (2.21 +/- 1.23) microgram/L and (1.40 +/- 0.45) microgram/L, respectively. There were no significant differences between the two groups(P > 0.05). And there were no significant differences of CETP levels in seminal plasma among groups of azoospermia(n = 29), oligoasthenozoospermia (n = 58), oligospermia(n = 15), asthenozoospermia(n = 44) and normozoospermia(n = 17) in the infertile patients(P > 0.05). The CETP in seminal plasma and serum were detected in 55 infertile patients, and there was no correlation between CETP levels in seminal plasma and serum using Spearman analysis(r = 0.009, P > 0.05). The mean CETP level in seminal plasma was almost 1/1,000 of that in serum.

CONCLUSIONSThe CETP level in seminal plasma is extremely low and has no relation with the changes of sperm density or motility. It may ensure the integrity of sperm membrane before the sperm enters into female genital tract.

Adult ; Carrier Proteins ; analysis ; blood ; Cholesterol Ester Transfer Proteins ; Glycoproteins ; Humans ; Infertility, Male ; metabolism ; Male ; Middle Aged ; Semen ; chemistry

Thrombophilia that is common among Caucasians is caused by genetic polymorphisms of coagulation factor V Leiden (R506Q) and prothrombin G20210A. Unlike that in Caucasians, thrombophilia that is common in the Japanese and Chinese involve dysfunction of the activated protein C (APC) anticoagulant system caused by abnormal protein S and protein C molecules. Approximately 50% of Japanese and Chinese individuals who develop venous thrombosis have reduced activities of protein S. The abnormal sites causing the protein S molecule abnormalities are distributed throughout the protein S gene, PROS1. One of the most common abnormalities is protein S Tokushima (K155E), which accounts for about 30% of the protein S molecule abnormalities in the Japanese. Whether APC dysfunction occurs in other Asian countries is an important aspect of mapping thrombophilia among Asians. International surveys using an accurate assay system are needed to determine this.
Asian Continental Ancestry Group ; Blood Coagulation ; Blood Proteins/genetics/metabolism ; Humans ; Protein C/genetics/*metabolism ; Protein S/chemistry/genetics/metabolism ; Thrombophilia/epidemiology/*etiology ; Venous Thrombosis/etiology/genetics

OBJECTIVETo determine the plasma protein binding rates of brucine and strychnine in total alkaloids from the seed of Strychnou nux-vomica, and make comparison with the single components at the same concentration.

METHODUltrafiltration was employed to determine the rat the plasma protein binding rate of the alkaloids from the seed of S. nux-vomica. The plasma concentrations were measured by RP-HPLC.

RESULTThe protein binding rates of brucine were (65.60 3.01)%, (68.20 +/- 7.80)%, (59.58 +/- 3.78)% when the plasma concentrations was 0.520, 1.300, 2.600 mg x L(-1), respectively. The protein binding rates of strychnine was (66.17 +/- 6.36)%, (67.10 +/- 2.52)%, (57.21 +/- 0.79)% when the plasma concentrations were 0.936, 2.340, 4.680 mg x L(-1) respectively. As to the total alkaloids from the seed of S. nux-vomica, The protein binding rate of brucine was (62.19 +/- 2.45)%, (69.55 +/- 5.84)%, (61.76 +/- 3.68)% when the plasma concentrations were 0.519, 1.288, 2.607 mg x L(-1), respectively. And the protein binding rates of strychnine were (54.79 +/- 3.55)%, (57.13 +/- 4.49)%, (59.31 +/- 3.65)% when the plasma concentrations were 0.940, 2.338, 4.674 mg x L(-1), respectively.

CONCLUSIONBrucine and strychnine have medium capacity in binding to plasma protein. In comparison with the single component of the same concentration, the protein binding rate of brucine in total alkaloids shows little difference, while there seems to be an obvious decrease for strychnine.

Alkaloids ; analysis ; pharmacokinetics ; Animals ; Blood Proteins ; chemistry ; metabolism ; Drugs, Chinese Herbal ; analysis ; pharmacokinetics ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; Seeds ; chemistry ; Strychnos ; chemistry

AIMTo determine in vitro the rat plasma protein binding rate by using microdialysis method.

METHODSThe binding rate was determined by using microdialysis probe as sampling tools and zero-net flux method as calibrating method. The regression equation was made by the difference of concentrations between the dialysis sample and the perfusate. The x-intercept of regression equation was the free drug concentration (Cf). The plasma protein binding rate was calculated by using the following equation: f = ( C0 - Cf)/C0.

RESULTThe binding rate was kept relatively stable in the studied concentration range.

CONCLUSIONIt is feasible that the plasma protein binding rate can be determined by using microdialysis method.

Animals ; Blood Proteins ; metabolism ; Chromatography, High Pressure Liquid ; Male ; Microdialysis ; methods ; Morphinans ; isolation & purification ; metabolism ; Plants, Medicinal ; chemistry ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; Regression Analysis ; Sinomenium ; chemistry