By Gerardo R. Vasta PhD, Hafiz Ahmed PhD
Introduces Groundbreaking ways for Assessing Lectin Function
Lectins and their ligands are below really a heavy microscope because of their power purposes to pharmacology, immunology, melanoma treatment, and agriculture. With transforming into curiosity within the glycobiology box, the physique of study regarding lectin roles has grown at an explosive cost, quite some time past twenty years. Animal Lectins: A practical View provides the main updated research of those carbohydrate-binding, and very likely lifesaving, proteins in a single entire quantity.
This standard-setting source provides new insights into the organic roles of so much animal lectins, together with their functionality in an infection prevention via innate immunity. It additionally discusses such lectin behaviors as:
- Glycoprotein folding
- Sorting and targeting
- Cell adhesion
- Cell-cell interactions and signaling
Describes the Structural foundation of Protein-Carbohydrate Interactions
Under the editorial assistance of 2 top protein chemistry specialists and with contributions from well-recognized box experts, this booklet logically and systematically discusses either intracellular and extracellular lectin features. it really is an important springboard for destiny box study and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't find the money for to be without.
Read or Download Animal Lectins: A Functional View PDF
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Additional resources for Animal Lectins: A Functional View
And Resheff, G. 1975 A β-Dgalactoside binding protein from electric organ tissue of Electrophorus electricus. Proc. Natl Acad. Sci. USA 72, 1383–1387. 16. I. J. 1965 Specific binding of concanvalin A to cross-linked dextran gels. Biochem. J. 96, 23C–25C. 17. M. 2001 The ABO blood group system: Historical background. Transfus. Med. 11, 243–265. 18. Kocourek, J. 1986 Historical background. J. ), The Lectins: Properties, Functions and Applications in Biology and Medicine. Academic Press, Orlando, FL, pp.
The Ig-V domain contains the carbohydrate-binding site and the ensuing Ig-C domains appear to function as spacers separating the carbohydrate binding site from the membrane. The first domain contains several residues that are well-conserved in Siglecs: an arginine residue that forms a salt bridge with the carboxyl group of sialic acid, two aromatic residues (one near the N-terminal and the other after the conserved arginine), and three cysteines, one of which forms an unusual interdomain disulfide bridge with a cysteine in the second Ig domain.
Describe mannan-binding lectin (MBL) polymorphisms and infectious diseases. They consult several published studies to investigate a possible connection between MBL deficiency and susceptibility to infections by bacteria, viruses, fungi, and parasites, and conclude that MBL deficiency appears to be linked to increased susceptibility to infections. Palaniyar et al. (Chapter 23) discuss on immunoregulatory roles of two collectins, lung surfactant proteins A and D. These two collectins serve as endogenous antibiotics and mediators of inflammation and thus have emerged as effector molecules of the innate immune system.
Animal Lectins: A Functional View by Gerardo R. Vasta PhD, Hafiz Ahmed PhD