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Animal Lectins: Form, Function and Clinical Applications

Tags: Animal bioscience , Cellular biology , Lectin function , Immunology and biochemistry. Under the editorial guidance of two leading protein chemistry experts and with contributions from well-recognized field authorities, Animal Lectins: A Functional View, logically and systematically discusses both intracellular and extracellular lectin functions.

It is an essential springboard for future field research and a clear and concise knowledge base that glycobiology, biochemistry, and immunology researchers cannot afford to be without. Animal Lectins: A Functional View. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters.

In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function.

Role of lectins in clinical settings Kapoor C, Vaidya S, Kaur H, Jain A - Clin Cancer Investig J

Key words: Bothrops moojeni , kidney, platelet aggregation, insulin, antibacterial activity. Bothrops moojeni , a type of venomous pit viper, is found in warm dry regions of several Brazilian states 1.

Snake venoms comprised a complex pool of organic and inorganic compounds. Furthermore, some venom contains toxins that act on integrins in the C-type lectin, disintegrin, and metalloprotease families 2, 3.

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Snake venoms with C-type lectin domains contain the conserved carbohydrate recognition domain CRD of other animal C-type lectins and share significant primary structure similarities with them; however, they do not necessarily bind to carbohydrate molecules nor require calcium ions for their activity Thus, lectins isolated from venom differ from other classical C-type lectins.

These classical lectins are a type of carbohydrate-binding protein domain. The C-type designation refers to their requirement of calcium for binding to this carbohydrate domain. Proteins that contain C-type lectin domains have a diverse range of functions, including cell-to-cell adhesion, immune response to pathogens and apoptosis. The C-type lectins used to be classified into seven subgroups I to VII based on the order of the various protein domains in each protein 7, 8.

One such domain has been purified from Bothrops jararacussu , Bothrops jararaca and Crotalus atrox venom and characterized as a C-type galactoside-binding lectin 9, They have erythrocyte-agglutinating activity and other properties, such as adhesion to plasmatic proteins that affect blood homeostasis by inhibiting or activating specific platelet membrane receptors and blood coagulation factors 11, These proteins i. Other effects have also been reported for these proteins, including mitogenic activity on lymphocytes, release of cell calcium stores, inhibition of cell proliferation, renal effects and antimicrobial activity Previously, it has been observed that crotacetin from the venom of C.

Previously, our group described the renal effects of C-type lectin isolated from Bothrops pirajai, such as the reduction of renal flow and glomerular filtration rate The C-type proteins have been described as an important component of these venoms, which are responsible for their biological effects. The study of the C-type galactoside-specific lectin isolated from Bothrops moojeni may contribute to the discovery of pharmacological tools. Despite the biological importance of snake venom lectins, the aim of the present work was to study the effects of lectin isolated from Bothrops moojeni venom on platelet aggregation, insulin secretion, antibacterial activity and the functions of isolated kidneys.

Purification of Lectin from Bothrops moojeni Venom. The lectin from B. For the first fractionation, whole venom was purified following the protocols described by dos Santos et al. After complete dissolution, the venom was homogenized and clarified by ultracentrifugation at x g for five minutes. The affinity chromatography was carried out with lactose 0. The lectin was eluted using a gradient of 0. The lectin-like fraction was pooled, extensively dialyzed against an ammonium bicarbonate buffer 0. The purification homogeneity of the eluted protein was evaluated by reverse phase HPLC 0.

One milligram of the lectin-like fraction from the affinity chromatography was dissolved in mL of buffer A and centrifuged at 4, x g for two minutes. The supernatant was then applied to the analytical reverse phase HPLC and equilibrated with buffer A 0. Elution of the protein was subsequently conducted using a linear gradient of buffer B The degree of purity of the lectin-like substance was assayed using two dimensional 2D and mass spectrometry. Characterization of Lectin Isolated from B.

Amino acid analysis of BmLec was performed using approximately 1 nM of purified protein hydrolyzed with 6N HCl mL in the presence of 10 mL of phenol. After this time, the excess HCl was removed and the resulting hydrolyzed amino acids were re-dried with an aqueous solution of ethanol:water:triethylamine The post-column derivatization was carried out with an aqueous solution of phenylisothiocyanate ethanol:water:triethylamine:phenylisothiocyanate; by volume.

After amino acid analysis, a new aliquot of BmLec was used for amino acid sequence determination. In this protocol, 10 mg of purified protein were dissolved in mL of 6 M guanidine chloride Merck, Germany containing 0. Nitrogen was flushed over the top of the protein solution for 15 minutes and then reduced with DTT 6 M, mL and carboxymethylated with 14 C-iodoacetic acid and cold iodoacetic acid. Nitrogen was again flushed over the surface of the solution, and the reaction tube was sealed.

One sample of this RC-protein 4. The elution profile was monitored at nm and the peptides were lyophilized. The elution profile was monitored at nm, and the peptides were lyophilized. Venous blood was collected with informed consent from healthy volunteers who denied taking any medication in the previous 14 days.

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Initially, whole blood was centrifuged to obtain the platelet-rich plasma PRP. After removing the PRP, the remaining blood was centrifuged at 3, x g for five minutes to obtain washed platelet. The platelet aggregation assays were conducted with a washed platelet preparation that was left for one hour at room temperature to recover its sensitivity to aggregation agents. The aggregation was recorded after seven minutes from the application of the lectin Insulin secretion was measured in rat islets that were isolated by collagenase EC 3. The pancreas was inflated with Hanks' balanced salt solution containing 0.

The digested tissue was washed four times and the islets were separated using a siliconized stretched Pasteur pipette.

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After this incubation, the medium was replaced with fresh buffer and the islets incubated for one hour in the presence of 2. Antibacterial Activity against Xanthomonas axonopodis pv. The Xanthomonas axonopodis. We then evaluated the effect of BmLec on the bacterial membrane of Xanthomonas axonopodis pv passiflorae incubated with lectin using scanning electron microscopy.

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