Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Galanthus: A plant genus in the family LILIACEAE (sometimes classified as Amaryllidaceae). Galanthus nivalis L. is the source of GALANTHAMINE.Liliaceae: A monocot family within the order Liliales. This family is divided by some botanists into other families such as Convallariaceae, Hyacinthaceae and Amaryllidaceae. Amaryllidaceae, which have inferior ovaries, includes CRINUM; GALANTHUS; LYCORIS; and NARCISSUS and are known for AMARYLLIDACEAE ALKALOIDS.Artocarpus: A plant genus of the family MORACEAE. Puag-haad extract, from A. lakoocha, contains STILBENES and related 4-substituted RESORCINOLS.Wheat Germ Agglutinins: Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.Plants, Genetically Modified: PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.Calystegia: A plant genus of the family CONVOLVULACEAE. Members contain calystegine and calystegins.Concanavalin A: A MANNOSE/GLUCOSE binding lectin isolated from the jack bean (Canavalia ensiformis). It is a potent mitogen used to stimulate cell proliferation in lymphocytes, primarily T-lymphocyte, cultures.Agglutinins: Substances, usually of biological origin, that cause cells or other organic particles to aggregate and stick to each other. They include those ANTIBODIES which cause aggregation or agglutination of particulate or insoluble ANTIGENS.Mannose-Binding Lectins: A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE.Galectins: A class of animal lectins that bind specifically to beta-galactoside in a calcium-independent manner. Members of this class are distiguished from other lectins by the presence of a conserved carbohydrate recognition domain. The majority of proteins in this class bind to sugar molecules in a sulfhydryl-dependent manner and are often referred to as S-type lectins, however this property is not required for membership in this class.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Agglutination: The clumping together of suspended material resulting from the action of AGGLUTININS.Plant Roots: The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)Genes, Plant: The functional hereditary units of PLANTS.Carbohydrate Metabolism: Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)Plant Extracts: Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard.Plant Shoots: New immature growth of a plant including stem, leaves, tips of branches, and SEEDLINGS.Plants, Medicinal: Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.PolysaccharidesPhytohemagglutinins: Mucoproteins isolated from the kidney bean (Phaseolus vulgaris); some of them are mitogenic to lymphocytes, others agglutinate all or certain types of erythrocytes or lymphocytes. They are used mainly in the study of immune mechanisms and in cell culture.DNA, Plant: Deoxyribonucleic acid that makes up the genetic material of plants.Plant Development: Processes orchestrated or driven by a plethora of genes, plant hormones, and inherent biological timing mechanisms facilitated by secondary molecules, which result in the systematic transformation of plants and plant parts, from one stage of maturity to another.Plants, Toxic: Plants or plant parts which are harmful to man or other animals.Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Plant Cells: Basic functional unit of plants.Plant Stems: Parts of plants that usually grow vertically upwards towards the light and support the leaves, buds, and reproductive structures. (From Concise Dictionary of Biology, 1990)Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Genome, Plant: The genetic complement of a plant (PLANTS) as represented in its DNA.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Plants, Edible: An organism of the vegetable kingdom suitable by nature for use as a food, especially by human beings. Not all parts of any given plant are edible but all parts of edible plants have been known to figure as raw or cooked food: leaves, roots, tubers, stems, seeds, buds, fruits, and flowers. The most commonly edible parts of plants are FRUIT, usually sweet, fleshy, and succulent. Most edible plants are commonly cultivated for their nutritional value and are referred to as VEGETABLES.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Plant Structures: The parts of plants, including SEEDS.Lectins, C-Type: A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Plant Growth Regulators: Any of the hormones produced naturally in plants and active in controlling growth and other functions. There are three primary classes: auxins, cytokinins, and gibberellins.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.Glycoconjugates: Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Peanut Agglutinin: Lectin purified from peanuts (ARACHIS HYPOGAEA). It binds to poorly differentiated cells and terminally differentiated cells and is used in cell separation techniques.Plant Immunity: The inherent or induced capacity of plants to withstand or ward off biological attack by pathogens.Tobacco: A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.Galactosides: Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of galactose with an alcohol to form an acetal. They include both alpha- and beta-galactosides.Fabaceae: The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.Acetylgalactosamine: The N-acetyl derivative of galactosamine.Plant Epidermis: A thin layer of cells forming the outer integument of seed plants and ferns. (Random House Unabridged Dictionary, 2d ed)Fetuins: A family of calcium-binding alpha-globulins that are synthesized in the LIVER and play an essential role in maintaining the solubility of CALCIUM in the BLOOD. In addition the fetuins contain aminoterminal cystatin domains and are classified as type 3 cystatins.Plant Stomata: Closable openings in the epidermis of plants on the underside of leaves. They allow the exchange of gases between the internal tissues of the plant and the outside atmosphere.Angiosperms: Members of the group of vascular plants which bear flowers. They are differentiated from GYMNOSPERMS by their production of seeds within a closed chamber (OVARY, PLANT). The Angiosperms division is composed of two classes, the monocotyledons (Liliopsida) and dicotyledons (Magnoliopsida). Angiosperms represent approximately 80% of all known living plants.Receptors, Mitogen: Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.Hemagglutination: The aggregation of ERYTHROCYTES by AGGLUTININS, including antibodies, lectins, and viral proteins (HEMAGGLUTINATION, VIRAL).Plant Preparations: Material prepared from plants.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.

Molecular characterization and crystallization of Diocleinae lectins. (1/1622)

Molecular characterization of seven Diocleinae lectins was assessed by sequence analysis, determination of molecular masses by mass spectrometry, and analytical ultracentrifugation equilibrium sedimentation. The lectins show distinct pH-dependent dimer-tetramer equilibria, which we hypothesize are due to small primary structure differences at key positions. Lectins from Dioclea guianensis, Dioclea virgata, and Cratylia floribunda seeds have been crystallized and preliminary X-ray diffraction analyses are reported.  (+info)

Lectins as membrane components of mitochondria from Ricinus communis. (2/1622)

1. Mitochondria were isolated from developing endosperm of Ricinus communis and were fractionated into outer membrane and inner membrane. The relative purity of the two membrane fractions was determined by marker enzymes. The fractions were also examined by negative-stain electron microscopy. 2. Membrane fractions were sequentially extracted in the following way. (a) Suspension in 0.5M-potassium phosphate, pH7.1; (b)suspension in 0.1M-EDTA (disodium salt)/0.05M-potassium phosphate, pH7.1; (c) sonication in 0.05M-potassium phosphate, pH7.1;(d)sonication in aq. Triton X-100 (0.1%). The membranes were pelleted by centrifugation at 100 000g for 15 min, between each step. Agglutination activity in the extracts was investigated by using trypsin-treated rabbit erythrocytes. 3. The addition of lactose to inner mitochondrial membrane resulted in the solubilization of part of the lectin activity, indicating that the protein was attached to the membrane via its carbohydrate-binding site. Pretreatment of the membranes with lactose before tha usual extraction procedure showed that lactose could extract lectins that normally required more harsh treatment of the membrane for solubilization. 4. Lectins extracted from inner membranes were purified by affinity chromatography on agarose gel. Polyacrylamide-gel electrophoresis of purified samples in sodium dodecyl sulphate indicated that at least part of the lectin present in inner mitochondrial membrane was identical with the R. communis agglutinin of mol.wt. 120 000.  (+info)

Post-translational processing of two alpha-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris. (3/1622)

Mass spectrometric methods were used to investigate the proteolytic processing and glycopeptide structures of three seed defensive proteins from Phaseolus vulgaris. The proteins were the alpha-amylase inhibitors alphaAI-1 and alphaAI-2 and arcelin-5, all of which are related to the seed lectins, PHA-E and PHA-L. The mass data showed that the proteolytic cleavage required for activation of the amylase inhibitors is followed by loss of the terminal Asn residue in alphaAI-1, and in all three proteins, seven or more residues were clipped from the C-termini, in the manner of the seed lectins. In most instances, individual glycoforms could be assigned at each Asn site, due to the unique masses of the plant glycopeptides. It was found that alphaAI-1 and alphaAI-2 differed significantly in their glycosylation patterns, despite their high sequence homology. These data complement the previous X-ray studies of the alpha1-amylase inhibitor and arcelin, where many of the C-terminal residues and glycopeptide residues could not be observed.  (+info)

The distribution of sugar chains on the vomeronasal epithelium observed with an atomic force microscope. (4/1622)

The distribution of sugar chains on tissue sections of the rat vomeronasal epithelium, and the adhesive force between the sugar and its specific lectin were examined with an atomic force microscope (AFM). AFM tips were modified with a lectin, Vicia villosa agglutinin, which recognizes terminal N-acetyl-D-galactosamine (GalNAc). When a modified tip scanned the luminal surface of the sensory epithelium, adhesive interactions between the tip and the sample surface were observed. The final rupture force was calculated to be approximately 50 pN based on the spring constant of the AFM cantilever. Distribution patterns of sugar chains obtained from the force mapping image were very similar to those observed using fluorescence-labeled lectin staining. AFM also revealed distribution patterns of sugar chains at a higher resolution than those obtained with fluorescence microscopy. Most of the adhesive interactions disappeared when the scanning solution contained 1 mM GaINAc. The adhesive interactions were restored by removing the sugar from the solution. Findings suggest that the adhesion force observed are related to the binding force between the lectin and the sugars distributed across the vomeronasal epithelium.  (+info)

A gene encoding a hevein-like protein from elderberry fruits is homologous to PR-4 and class V chitinase genes. (5/1622)

We isolated SN-HLPf (Sambucus nigra hevein-like fruit protein), a hevein-like chitin-binding protein, from mature elderberry fruits. Cloning of the corresponding gene demonstrated that SN-HLPf is synthesized as a chimeric precursor consisting of an N-terminal chitin-binding domain corresponding to the mature elderberry protein and an unrelated C-terminal domain. Sequence comparisons indicated that the N-terminal domain of this precursor has high sequence similarity with the N-terminal domain of class I PR-4 (pathogenesis-related) proteins, whereas the C terminus is most closely related to that of class V chitinases. On the basis of these sequence homologies the gene encoding SN-HLPf can be considered a hybrid between a PR-4 and a class V chitinase gene.  (+info)

Selective killing of CD8+ cells with a 'memory' phenotype (CD62Llo) by the N-acetyl-D-galactosamine-specific lectin from Viscum album L. (6/1622)

As reported previously by our group, among the toxic proteins from Viscum album L. only the mistletoe lectins (MLs) induce the apoptotic killing pathway in human lymphocytes. Although one may expect a homogenous distribution of carbohydrate domains on cell surface receptors for the carbohydrate binding B chains of the toxic protein, the sensitivity of cells to these B chains obviously differ. Here we report a selective killing of CD8+ CD62Llo cells from healthy individuals by the galNAc-specific ML III (and RCA60, which binds to gal and galNAc), while the gal-specific ML I was less effective. This selective killing is not sufficiently explained by protein synthesis inhibition alone, since this subset was not affected by other ribosome inhibiting proteins such as the lectin from Ricinus communis (RCA120), lectin from Abrus precatorus (APA), abrin A, and inhibitors of RNA, DNA and/or protein synthesis such as actinomycin D, mitomycin C, and cycloheximide. We conclude that CD8+ cells with 'memory' phenotype (CD62Llo) are more sensitive to the ML III-mediated killing than their CD8+ CD62Lhi counterparts, CD4+ T cells, and CD19+ B cells. These cells probably express a distinct receptor with galNAc domains that is missing or not active on CD8+ cells with a 'naive' phenotype.  (+info)

Underglycosylation of IgA1 hinge plays a certain role for its glomerular deposition in IgA nephropathy. (7/1622)

This study was performed to isolate and investigate the IgA1 that could accumulate in glomeruli (glomerulophilic IgA1). IgA1 was fractionated by the electric charge and the reactivity to Jacalin. Serum IgA1 of IgA nephropathy patients was separated and fractionated using a Jacalin column and subsequent ion-exchange chromatography. The fractions were divided into three groups of relatively cationic (C), neutral (N), and anionic (A). IgA1 was also divided into Jacalin low (L), intermediate (I), and high (H) affinity fractions by serial elution using 25, 100, and 800 mM galactose. The left kidneys of Wistar rats were perfused with 2, 5, or 10 mg of each group of IgA1. The rats were sacrificed 15 min, 30 min, 3 h, or 24 h after the perfusion. The accumulation of each IgA1 in the glomeruli was then observed by immunofluorescence. The IgA1 of the fractions N and H separated by the two methods was definitely accumulated in the rat glomeruli with a similar pattern. The electrophoresis revealed that the macromolecular IgA1 was increased in fraction H compared with other fractions. Therefore, Jacalin high-affinity IgA1(fraction H) was applied on a diethylaminoethyl column and divided into electrically cationic (HC), neutral (HN), and anionic (HA). Only the asialo-Galbeta1,3GalNAc chain was identified in the fraction HN IgA1 by gas-phase hydrazinolysis. Furthermore, the IgA1 fraction was strongly recognized by peanut agglutinin, Vicia Villosa lectins, and antisynthetic hinge peptide antibody. These results indicated that the IgA1 molecules having the underglycosylated hinge glycopeptide played a certain role in the glomerular accumulation of IgA1 in IgA nephropathy.  (+info)

Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells. (8/1622)

BACKGROUND: Dietary lectins can alter the proliferation of colonic cells. Differentiation is regulated by adhesion molecules which, being glycosylated, are targets for lectin binding. AIMS: To examine the effects of dietary lectins on differentiation, adhesion, and proliferation of colorectal cancer cells. METHODS: Differentiation was assessed in three dimensional gels, adhesion by aggregation assay, and proliferation by 3H thymidine incorporation. The role of the epithelial cell adhesion molecule (epCAM) was studied using a specific monoclonal antibody in blocking studies and Western blots. The human colon cancer cell lines LS174T, SW1222, and HT29 were studied. RESULTS: The cell line LS174T differentiated in the presence of Vicia faba agglutinin (VFA) into gland like structures. This was inhibited by anti-epCAM monoclonal antibody. Expression of epCAM itself was unaffected. VFA as well as wheat germ agglutinin (WGA) and the edible mushroom lectin (Agaricus bisporus lectin, ABL) significantly aggregated LS174T cells but peanut agglutinin (PNA) and soybean agglutinin (SBA) did not. All lectins aggregated SW1222 and HT29 cells. Aggregation was blocked by the corresponding sugars. Aggregation of cells by VFA was also inhibited by anti-epCAM. VFA, ABL, and WGL inhibited proliferation of all the cell lines; PNA stimulated proliferation of HT29 and SW1222 cells. In competition studies all sugars blocked aggregation and proliferation of all cell lines, except that the addition of mannose alone inhibited proliferation. CONCLUSION: VFA stimulated an undifferentiated colon cancer cell line to differentiate into gland like structures. The adhesion molecule epCAM is involved in this. Dietary or therapeutic VFA may slow progression of colon cancer.  (+info)

  • Plant lectins are broadly divided into six classes based on their subunit folds. (
  • Almost everyone has antibodies to some dietary lectins in their body. (
  • The effects of dietary lectins only extend for as long as they are in the body, and the effects can be reduced by eating a variety of fruits, vegetables (rather than high amounts of one type) and foods with beneficial bacteria (e.g., fermented foods). (
  • Some researchers believe that dietary lectins can raise the risk of autoimmune disease. (
  • For much more detail, see Dr. Freed's patient handout on "Rheumatic Patches" and how intolerance of dietary lectins may drive their development. (
  • CCL2-induced intestinal brush border defects in C. elegans are similar to the damage observed previously in rats after feeding the dietary lectins wheat germ agglutinin or concanavalin A. The evolutionary conserved reaction of the brush border between mammals and nematodes might allow C. elegans to be exploited as model organism for the study of dietary lectin-induced intestinal pathology in mammals. (
  • As lectins cause leaky gut and are readily absorbed into the bloodstream, most people develop antibodies against dietary lectins (R, R2). (
  • Wheat gliadin, which causes coeliac disease, contains a lectin like substance that binds to human intestinal mucosa, and this has been debated as the "coeliac disease toxin" for over 20 years. (
  • Scientists know that a lectin found in wheatgerm binds to the polysaccharide, chitin. (
  • Each lectin binds specifically to a certain sugar sequence in oligosaccharides and glycopeptides. (
  • We have previously shown that the Coprinopsis cinerea lectin 2 (CCL2), which binds to α1,3-fucosylated N-glycan cores, is toxic to Caenorhabditis elegans and results in developmental delay and premature death. (
  • Though naturally occurring, Miriam Amselem , holistic nutritionist, fitness trainer, and yoga instructor, explains that lectin binds to the cells on the gut wall. (
  • In the spring of 2017 a book called The Plant Paradox was written by a cardiologist named Dr. Steven Gundry. (
  • The Plant Paradox diet presented by Dr Gundry does have some pretty convincing evidence, especially when it comes to the autoimmune and inflammation connections, but I'm still a little on the fence when it comes to the 'lectin free' diet protocol as a diet for everyone. (
  • The main issue proposed by Dr Gundry is that lectins damage the gut and trigger an autoimmune response. (
  • Interestingly Dr Gundry talks about many of the same conditions that respond well to our herbal detox protocol, which also just happens to avoid many high lectin foods. (
  • Clarkson says she learned about it from reading the book ' The Plant Paradox ' by Dr. Steven Gundry. (
  • 33 of the Best Gundry-Approved Wines High in Polyphenols Yes, You Can Drink Wine on The Plant Paradox Diet! (
  • 15 Lectin-Free Superfoods Dr. Gundry Recommends Superfoods have exceptionally high concentrations of polyphenols and other antioxidants, earning them ORAC (Oxygen Radical Absorbance Capacity) scores that greatly surpass most other healthy foods. (
  • Lectin-Free Fats & Oils Your Plant Paradox Diet Demands If you're on the Plant Paradox diet, you've probably noticed that Dr. Gundry recommends a wide variety of healthy fats and oils, many of which you likely don't already have in your pantry. (
  • In the book, The Plant Paradox: The Hidden Dangers In 'Healthy Foods' That Cause Disease And Weight Gai n , Dr. Steven Gundry sets out to demystify long-held myths about plant-based foods. (
  • Gundry offers a diet that eliminates lectins, GMOs, and other toxins. (
  • From bestselling writer Dr. Steven Gundry, a fast and very easy overview to The Plant Mystery program that gives viewers the devices to take pleasure in the benefits of lectin-free consuming in simply thirty days. (
  • Now, in The Plant Paradox Quick and Easy, Dr. Gundry makes it simpler than ever before to go lectin cost-free. (
  • In The Plant Paradox Book, Dr. Steven Gundry presents detailed information on the different myths surrounding plant based foods. (
  • From renowned cardiac surgeon and acclaimed author Dr. Steven R. Gundry, the companion cookbook to New York Times bestselling The Plant Paradox , offering 100 easy-to-follow recipes and four-color photos. (
  • In the New York Times bestseller The Plant Paradox , Dr. Steven Gundry introduced readers to the hidden toxins lurking in seemingly healthy foods like tomatoes, zucchini, quinoa, and brown rice: a class of plant-based proteins called lectins. (
  • Now, in The Plant Paradox Cookbook , Dr. Gundry breaks down lectin-free eating step by step and shares one hundred of his favorite healthy recipes. (
  • Dr. Gundry will offer an overview of his Plant Paradox program and show readers how to overhaul their pantries and shopping lists to make delicious, simple, seasonal, lectin-free meals. (
  • In the New York Times bestseller The Plant Paradox , renowned cardiologist Dr. Steven Gundry introduced readers around the world to the hidden toxins lurking in seemingly healthy foods: a class of plant-based proteins known as lectins. (
  • Now, in The Plant Paradox Cookbook , Dr. Gundry gives fans of The Plant Paradox what they've been asking for: more recipes! (
  • In this easy-to-follow cookbook, Dr. Gundry shows readers how simple and delicious it is to live lectin-free (or at least lectin-reduced). (
  • In addition to an overview of the Plant Paradox program, a pantry guide, and sample meal plans, Dr. Gundry shares more than one hundred recipes designed to help heal the gut, promote weight loss, and quell inflammation. (
  • and Truffled Mushroom Mac and Cheese, and decadent desserts such as Chocolate Mint Cookies, Pistachio Ice Cream, and Olive Oil Rosemary Cake, Dr. Gundry makes it easy for everyone to clean up their diets and live lectin-free. (
  • From bestselling author Dr. Steven Gundry, a quick and easy guide to The Plant Paradox program that gives readers the tools to enjoy the benefits of lectin-free eating in just 30 days.In Dr. Steven Gundrys breakout bestseller The Plant Paradox, readers learned the surprising truth about foods that have long been regarded as healthy. (
  • According to the founder of the diet, California cardiologist Steven Gundry, M.D., a diet containing lectins leads to inflammation and weight gain. (
  • When someone suffers from Crohn's disease or irritable bowel syndrome, the gut lining seems to be more sensitive to food lectins. (
  • 18, 19 Certain plant food lectins may also help prevent cancer development by blocking the actions of angiogenesis-promoting lectins on human cells. (
  • Also, bacterial infections, inflammatory bowel disease (IBD), colon cancer, or autoimmune illnesses may alter intestinal cells in a way that makes usually harmless food lectins problematic. (
  • But the really disturbing finding came with the discovery in 1989 that some food lectins get past the gut wall and deposit themselves in distant organs. (
  • The first lectin to be purified on a large scale and available on a commercial basis was concanavalin A, which is now the most-used lectin for characterization and purification of sugar-containing molecules and cellular structures. (
  • Fractionation of these proteins by affinity chromatography using α-D-methylmannopyranoside (MMP) immobilized on agarose resulted in the isolation of lectins stimulating germination. (
  • The results of CLBA were in accordance with the results obtained from the lectin affinity chromatography and electrophoresis, where multiple glycoforms of the IR and IGFRs were shown to exist. (
  • The mannose-specific plant lectins from the Amaryllidaceae family (e.g. (
  • Based on prior studies on coronaviruses such as SARS-CoV and MERS-CoV, mannose-specific plant lectins can be used to investigate antiviral properties of the novel coronavirus SARS-CoV-2, the virus that causes COVID-19. (
  • Indeed, researchers speculate that many apparent causes of bacterial food poisoning may actually be lectin poisoning. (
  • So the three main pathogenic factors for peptic ulcer-acid stimulation, failure of the mucous defence layer, and abnormal bacterial proliferation ( Helicobacter pylori ) are all theoretically linked to lectins. (
  • Four main groups of Pseudomonas bacteriocins have been identified so far, all of which equally occur in other bacterial genera: tailocins, modular bacteriocins, B-type microcins and lectin-like bacteriocins (Supplementary Table S1 ). (
  • Raw kidney beans contain from 20,000 to 70,000 lectin units, while fully cooked beans usually contain between 200 and 400 units. (
  • This action of lectins is most likely a contributing factor to the pro-weight loss and anti-diabetes effects of beans and other plant foods. (
  • And that's not the only one: similar results have been found for lectins from fava beans, soybeans, bananas, buckwheat, jackfruit, and wheat. (
  • It is acceptable to have a theory, but this idea about lectins being "disease-causing" and that people need to avoid beans, vegetable and nuts in order to get healthy and lose weight, has been thoroughly disproven by the thousands of studies documenting the health and longevity benefits of these foods. (
  • The same cooking process that reduces the gas-causing tendencies of beans also reduces their lectin content to a safe level. (
  • Canned beans have been prepared using this process, so they are not high in lectins. (
  • Green (immature) beans and peas have low levels of lectins. (
  • Eating raw kidney beans can lead to lectin poisoning, the main symptoms of which include severe abdominal pain, vomiting and diarrhea ( 8 ). (
  • In one study, lectins in soybeans were mostly eliminated when the beans were boiled for only 5 to 10 minutes ( 14 ). (
  • Legume lectins such as white kidney beans. (
  • With grocery store checklists, meal plans, time-saving food preparation approaches, all-new recipes, and support for families as well as those adhering to specialized diets (consisting of ketogenic and vegan), The Plant Paradox Quick as well as Easy is the all-in-one source Plant Paradox followers and also newcomers alike need to start outcomes gain the health advantages of living lectin-free. (
  • In addition to these four large families the jacalin-related lectins, the amaranthin family, and the Cucurbitaceae phloem lectins are now recognized as separate subgroups. (
  • We investigated soybean lectin gene structure and expression in a genetic line that accumulates normal levels of seed lectin (Le+ line) and in a mutant line that produces no detectable seed lectin (Le- line). (
  • Runoff transcription experiments with isolated nuclei showed that the reduced RNA levels are caused by decreased lectin gene transcription. (
  • Westar) were produced in which the pea lectin gene under control of the pollen-specific promoter Sta44-4 was introduced. (
  • The major proteins at pI 4.85 and 4.77 had also common amino acid sequence at N-terminus, TLVKIGPWGGNGGSAQDISV, which is almost identical to salt and drought stress-inducible salT gene products in rice plant. (
  • One of them is homologous to a stress-inducible salT gene' The Plant Cell. (
  • Most important, you can see if you have the lectin sensitive gene, and if you do, find out ways to reduce lectin sensitivity. (
  • With using SelfDecode, I've been able to figure out that the cannabinoid gene is the most important for lectin sensitivity. (
  • Here, we demonstrate that a soybean-derived lectin (SBL) with GalNAc-binding affinity could potently suppress HIV infection of macrophages in a dose-dependent fashion. (
  • Here, we demonstrate that GalNAc-specific soybean lectin (SBL) triggers antiviral signaling via recognition of the cell surface galactosyl group of macrophages, which results in the suppression of HIV at multiple steps. (
  • Data concerning the role of lectins in regulation of oxidative stress and stress-induced cytoskeleton rearrangements are presented. (
  • The degree of resistance to the plant lectins was invariably correlated with an increasing number of mutated glycosylation sites in gp120. (
  • The periodic acid-Schiff staining and ferric-orcinol assay for pentose, as well as its HA activity inhibition by chitosan oligomers further confirmed the purified lectin as a potato chitin-binding lectin. (
  • Also, there are no government recommendations specifically for the amounts of lectins we should or shouldn't eat. (
  • Frequent consumption of large amounts of lectins has been shown to damage the lining of the digestive system ( 1 ). (
  • Repeated exposure to large amounts of lectins may increase gut permeability. (
  • It's important to reiterate how little is really known about lectins. (
  • Each genetic line contains two lectin genes, L1 and L2. (
  • Boulter D, Edwards GA, Gatehouse AMR, Gatehouse JA and Hilder VA (1990) Additive protective effects of different plant-derived insect resistance genes in transgenic tobacco plants. (
  • Recent advances in the structural analysis of lectins and molecular cloning of lectin genes enable subdividision of plant lectins in a limited number of subgroups of structurally and evolutionary related proteins. (
  • The lectin induced expression of interleukin (IL)-1α, IL-1β, IL-6, tumor necrosis factor-α, interferon-γ, granulocyte-monocyte colony-stimulating factor and IL-10 genes but no expression of IL-2 and IL-5 genes could be detected. (
  • The results showed that only Dioclea violacea lectin (DVL) was able to interact with midgut glycans, unlike Cratylia floribunda lectin (CFL) and Canavalia gladiata lectin (CGL). (
  • In recent years, the use of lectins for screening of potential biomarkers has gained increased importance in cancer research, given the development in glycobiology that highlights altered structural changes of glycans in cancer associated processes. (
  • Fermenting markedly reduces lectins. (
  • So far, the U.S. Food and Drug Administration (FDA) hasn't put together a list of foods with lectins and what the amounts are, which would be different for raw and cooked foods, because cooking reduces lectins. (
  • Approximately 30% of our food contains lectins, some of which may be resistant enough to digestion to enter the circulation. (