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Comparative Immunology
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
The blood vessel walls of fish are permeable to immunoglobulins. As a result, antibodies are found in tissue fluids, in plasma, lymph, and skin mucus. In blood they constitute about forty to fifty percent of the total serum proteins. IgM is also found in the skin-covering mucus of bony fish. It appears to be locally synthesized. Fish antibody in the presence of normal serum as a source of complement is capable of lysing target cells. Likewise, fish antibodies can cause agglutination. There is no evidence that fish antibodies can function as opsonins nor have Fc receptors been detected on fish phagocytes.
Antiepileptic Drug Toxic Emergencies
Published in Stanley R. Resor, Henn Kutt, The Medical Treatment of Epilepsy, 2020
Carbamazepine (CBZ) is a neutral, lipophilic compound that is insoluble in water but soluble in ethanol or chloroform. It is 70 to 80% bound to protein in the blood (24). The only active metabolite is CBZ-10,11-epoxide (25). The metabolism and excretion of CBZ is through a series of reactions that convert the lipophilic parent drug into more hydrophilic compounds, which in turn undergo biliary and renal excretion. Since only hydrophilic metabolites, not the lipophilic parent compound, are excreted, the amount and duration of drug actions from a given dose is regulated by the rate of biotransformation. Patients at risk for inadvertently developing signs and symptoms of toxicity from high blood levels are those taking other medications which slow the rate of biotransformation of CBZ (24). Such other drugs include erythromycin and other antibiotics (26), propoxyphene (27), and cimetidine (24). CBZ is an anticholinergic agent, and poisoning may result in cardiac dysrhythmias; this is of clinical significance only in elderly patients with underlying heart disease (24).
Disorders in tHemostasis System and Changes in the Rheological Properties of the Blood in Ischemic Heart Disease and Diabetes Mellitus Patients
Published in E.I. Sokolov, Obesity and Diabetes Mellitus, 2020
Anticoagulant activity is also associated with protein C and protein S that inhibit factors V and VIII. The rate of inhibition of the factors of coagulation by protein C is regulated by its cofactor — protein S [146, 147]. Protein C is not only an anticoagulant, it raises the fibrinolytic activity by increasing the level of the circulating vessel activator of plasminogen, thus ensuring lysis of a clot, but not causing fibrinogenolysis [61, 93, 94, 207, 208, 209, 514, 560].
Recent trends in next generation immunoinformatics harnessed for universal coronavirus vaccine design
Published in Pathogens and Global Health, 2023
Chin Peng Lim, Boon Hui Kok, Hui Ting Lim, Candy Chuah, Badarulhisam Abdul Rahman, Abu Bakar Abdul Majeed, Michelle Wykes, Chiuan Herng Leow, Chiuan Yee Leow
S protein binds to one another naturally into a homo-trimer, resembling Class I membrane fusion protein [71]. S protein comprises two subunits. The S1 subunit is subdivided into N-terminal domain (NTD) and C-terminal domain (CTD). The RBD is located in the CTD. On the other hand, S2 subunit contains the basic elements responsible for membrane fusion, that are, fusion peptide (FP), heptad repeats (HR), membrane proximal external region (MPER) and transmembrane domain (TM). Full-length S protein, S1 subunit, RBD, NTD and FP have been investigated as potential targets of vaccines. The RBD is the most studied due to the fact that it attaches straight to the ACE2 receptor on the host cells. RBD immunization induced antibodies are capable of blocking this interaction and thus effectively minimize the infection [72]. To elaborate, the RBD is conserved relative to the S1 subunit, plus many neutralizing epitopes are found within this domain, making it an excellent candidate for inclusion in a vaccine [73]. N protein is located inside the virus, where it surrounds the viral RNA and forms a helical nucleocapsid. This protein, the most abundant protein in coronavirus, is relatively more conserved than S protein [74]. It is highly antigenic and suitable as a marker for diagnostic purposes [72]. Studies have stated that E protein is a noticeable virulence factor [75]. Along with S and E proteins, M proteins are also found on the viral envelope and are the major component needed for initiating viral-budding. M protein is abundant on the viral envelope (surface) and is well conserved among different species [76].
Clot activators and anticoagulant additives for blood collection. A critical review on behalf of COLABIOCLI WG-PRE-LATAM
Published in Critical Reviews in Clinical Laboratory Sciences, 2021
G. Lima-Oliveira, L. M. Brennan-Bourdon, B. Varela, M. E. Arredondo, E. Aranda, S. Flores, P. Ochoa
The endogenous anticoagulants are a varied group of proteins that act to limit or minimize coagulation either alone or in concert with each other [37]. In vivo, protein C, protein S, and antithrombin are the most important natural anticoagulants [38]. Protein C is a vitamin K-dependent protein synthesized predominantly in the liver as a single polypeptide chain that circulates as a zymogen; activated protein C inactivates F Va and F VIIIa [39,40] (Figure 2). Protein S, which is also vitamin K-dependent, is a non-enzymatic glycoprotein, a cofactor for activated protein C, that is synthesized by the endothelium and liver and then stored in endothelial cells and platelet alpha granules [41,42]. Protein S circulates in the plasma at a concentration of 350 nmol/L, 40% of which is free and 60%, bound to C4bBP; only the free form acts as a cofactor of protein C [43]. Protein S also has anticoagulant activity that is independent of activated protein C; in association with tissue factor pathway inhibitor, it inhibits F IXa [42,44], (Figure 2). Antithrombin is a serine protease inhibitor that influences the activity of several coagulation factors: F IIa, IXa, Xa, XIa, and XIIa [45–47] (Figure 2). Moreover, heparans, which are glycosaminoglycans expressed on endothelial cell surfaces and are formally known as endogenous heparin, are able to bind and activate antithrombin via allosteric activation [48,49].
Thrombophilia testing in patients with portal vein thrombosis
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2020
Malene Helligsø Kirkeby, Julie Brogaard Larsen, Henning Grønbaek, Anne-Mette Hvas
Thrombophilia investigation was planned to be performed at least three months after the PVT was diagnosed. If investigations showed presence of aPL antibodies, patients had a confirmatory test done after at least 12 weeks. Of note, analysis of cardiolipin antibodies was not included in the thrombophilia investigation up until 2014. Levels of FVIII and fibrin D-dimer had to be increased persistently over a period of at least 12 months before being categorized as increased. If patients received vitamin K antagonists (VKA) at the time of blood sampling, any abnormal results of protein S, protein C, lupus anticoagulant, and INR were excluded from the final results. Deficiency of protein S, protein C, or antithrombin was confirmed by genetic testing. Analyses of kidney and liver function were performed within a month of the time of PVT, i.e. not at the time of thrombophilia investigations.