Animal Galectins and Plant Lectins as Tools for Studies in Neurosciences

Abstract

Lectins are proteins or glycoproteins of non-immunological origin capable of reversibly and specifically binding to glycoconjugates. They exist in free form or associated with cells and are widely distributed in nature, being found in plants, microorganisms, and animals. Due to their characteristics and mainly due to the possibility of reversible binding to glycoconjugates, lectins have stood out as important tools in research involving Neurobiology. These proteins have the ability to modulate molecular targets in the central nervous system (CNS) which may be involved with neuroplasticity, neurobehavioral effects, and neuroprotection. The present report integrates existing information on the activity of animal and plant lectins in different areas of Neuroscience, presenting perspectives to direct new research on lectin function in the CNS, providing alternatives for understanding neurological diseases such as mental disorders, neurodegenerative, and neuro-oncological diseases, and for the development of new drugs, diagnoses and therapies in the field of Neuroscience.

β-1,3-Glucan recognition by Acanthamoeba castellanii as a putative mechanism of amoeba-fungal interactions

“…Invertebrates such as insects, devoid of acquired immunity, boast powerful mechanisms in response to the parasite invasion that rely on the insect's innate immune cell expression of β-1,3-glucan-binding proteins to recognize microbial surface polysaccharides ( 41 ). β-1,3-Glucan-binding proteins have been identified in various species ( 40 , 42 – 46 ). Typically, these proteins showcase two distinct domains: a C-terminal glucanase-like domain exhibiting homology with glucanases like xylanase or starch hydrolyzing enzymes and an N-terminal β-1,3-glucan recognition domain ( 39 , 41 , 47 ).…”

Recovery of Bioactive Compounds from Marine Organisms: Focus on the Future Perspectives for Pharmacological, Biomedical and Regenerative Medicine Applications of Marine Collagen

“…As oxidative stress has been considered to play an essential role in the onset and progression of neurodegeneration, there has been a significant scientific focus on the development of antioxidant compounds for neuroprotection [ 108 ]. Marine polysaccharides, in particular, chitosan derived from the hydrolysis of chitin, alginate extracted from algae [ 109 , 110 ], marine glycosaminoglycans such as hyaluronic acid (HA), chondroitin sulfate (CS), heparin and heparan sulfate (HS) obtained from mussels, codfish bones, tuna eyeballs, and shark fins [ 111 , 112 ], and marine glycoproteins [ 113 ] and glycolipids [ 114 , 115 ], are the most physiologically important biocompounds involved in neuroprotective activities that can be extracted from marine sources.…”

Marine Biocompounds for Neuroprotection—A Review

“…So far, lectins have been isolated from a variety of marine animals, such as sponges (Aplysina lactuca, Cliona varians, Suberites domuncula, Axinella corrugata, and Chondrilla caribensis), annelids (Cinachyrella apion, Chaetopterus variopedatus and Serpula vermicularis), mollusks (Aplysia dactylomela, Mytilus galloprovincialis, Argopecten irradians, Ruditapes philippinarum, Madiolus modiolus, and Crenomytilus grayanus), arthropods (Tachypleus tridentatus and Penaeus monodon), sea cucumbers (Holothuria scabra, Holothuria grisea, and Cucumaria echinata), ascidians (Didemnum ternatanum), amphioxus (Branchiostoma belcheri and Branchiostoma japonicum), and fish (Aristichtys nobilis, Silurus asotus, Oncorhynchus tshawytscha, Epinephelus coioides, Oncorhynchus mykiss, Rachycentron canadum, and Paralichthys olivaceus) [157,158]. As they have the ability to modulate molecular targets in the central nervous system, lectins might be involved in processes associated with neuroplasticity, neurobehavioral effects, and neuroprotection [159]. Therefore, galectin-3, a β-galactoside-binding lectin, could modulate the innate immunity and induce a therapeutic shift in microglia polarization, significantly reducing the infarct size, in the context of ischemic injury [160].…”