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[PMID]: 29324242
[Au] Autor:Vishweshwaraiah YL; Prakash B; Gowda LR
[Ad] Address:Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute, Mysore 570020, India.
[Ti] Title:Expression profiling of the Dolichos lablab lectin during germination and development of the seed.
[So] Source:Plant Physiol Biochem;124:10-19, 2018 Mar.
[Is] ISSN:1873-2690
[Cp] Country of publication:France
[La] Language:eng
[Ab] Abstract:The temporal expression of the field bean (Dolichos lablab) galactose specific lectin, DLL-II, during germination, post-germination and seed development was evaluated using Native-PAGE followed by activity staining, immunodetection and quantitative Real Time PCR (qPCR). A rapid and steep decline in the polyphenol oxidase (PPO) and hemagglutinating activity during the initial stages of germination, which did not correlate with the slow decline in total protein was observed. During post germination period, PPO and hemagglutination activities were negligible, whereas a rapid resorption of the protein was evident. These results suggest that DLL-II is not a storage protein. The presence of mRNA in the quiescent seed and initial stages of germination are indicative of a very stable mRNA. DLL-II was expressed in high copies during seed development and increased dramatically between 10 and 20 days after flowering (DAF), suggesting a switch over stage in DLL-II expression. Transcript levels reached a maximum at the mature stage of seed development. Among the non-seed tissues examined, root showed the highest level. The high affinity binding to kinetin and indole acetic acid, the key hormones that regulate root development and its vascular differentiation add a new dimension to the physiological role of DLL-II in the seed. This finding, coupled with the PPO and hemagglutinating activity makes DLL-II, truly a multifunctional protein.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180212
[Lr] Last revision date:180212
[St] Status:In-Process

  2 / 1096 MEDLINE  
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[PMID]: 29357431
[Au] Autor:Qureshi SH; Patel NN; Murphy GJ
[Ad] Address:Cardiac surgery, Nottingham City Hospital, United Kingdom.
[Ti] Title:Vascular endothelial cell changes in post cardiac surgery acute kidney injury.
[So] Source:Am J Physiol Renal Physiol;, 2017 Dec 20.
[Is] ISSN:1522-1466
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: Acute Kidney Injury (AKI) is common complication of cardiac surgery however the phenotype of this condition is poorly defined. The aim of this study was to characterize changes in endothelial structure and function that underlie post cardiopulmonary bypass (CPB) AKI. METHODS: Adult pigs (N=16) were randomised to undergo following procedures; (n=8 per group); Group 1: sham operation-neck dissection with 2.5hr of general anesthesia and Group 2: CPB-2.5hr of cardiopulmonary bypass. RESULTS: CPB resulted in the depletion of specific epitopes of glycosaminoglycans side chains of the endothelial glycocalyx; Dolichos biflorus agglutinin; mean difference (MD)(95% Confidence Interval (CI)) P value: -0.26 (-0.42, -0.09), P=0.0024, Triticum vulgaris (wheat germ) agglutinin: -0.83(-1.2, -0.38), P=0.0005 and Ulex europaeus agglutinin 1: -0.25(-0.49, -0.009), P=0.041, endothelial membrane proteins; thrombomodulin: -3.13(-5.6, -0.65), P=0.02 and adherens junctions; VE-Cadherin: -1.06(-1.98, -0.145), P=0.02. CPB also resulted in reductions in microvascular cortical perfusion: -0.62(-1.02, -0.22), P= 0.006, and increased renal cortex adenosine levels: 2.32(0.83, 3.8), P=0.0059. These changes were accompanied by significant reduction in creatinine clearance at 1.5hr post intervention, mean difference (MD) 95% confidence interval (CI); -51.7 (-99.7, -3.7), P=0.037 and at 24hr, MD (95% CI): -47.3 (-87.7, -7.6), P= 0.023, and proteinuria immediately post intervention MD (95%CI): 18.79 (2.17, 35.4), P= 0.03 vs. sham. CONCLUSION: In our experimental CPB model, endothelial injury was associated with loss of autoregulation, increase in microvascular permeability and reduced glomerular filtration. Interventions that promote endothelial homeostasis may have clinical utility in the prevention of post cardiac surgery AKI.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180131
[Lr] Last revision date:180131
[St] Status:Publisher
[do] DOI:10.1152/ajprenal.00319.2017

  3 / 1096 MEDLINE  
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[PMID]: 29159968
[Au] Autor:Bosi G; DePasquale JA; Manera M; Castaldelli G; Giari L; Sayyaf Dezfuli B
[Ad] Address:Department of Health, Animal Science and Food Safety, Università degli Studi di Milano, Milan, Italy.
[Ti] Title:Histochemical and immunohistochemical characterization of rodlet cells in the intestine of two teleosts, Anguilla anguilla and Cyprinus carpio.
[So] Source:J Fish Dis;, 2017 Nov 21.
[Is] ISSN:1365-2761
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Rodlet cells (RC) are characterized by a distinctive cell cortex and conspicuous inclusions named "rodlets." These cells are particularly abundant and large in size in intestine of eels. Histochemical, immunohistochemical and ultrastructural investigations were carried out on European eel Anguilla anguilla and Common carp Cyprinus carpio from Northern Italy. Eight biotinylated lectins were used to probe for specific carbohydrate residues in deparaffinized, hydrated intestinal sections of eel and carp. Five antibodies were tested on intestinal sections of both fish species: inducible nitric oxide synthase (i-NOS), leu-enkephalin, lysozyme, serotonin and tumour necrosis factor-α. Lectin histochemistry revealed rodlet cells (RCs) of the eel intestine to react with two of the eight lectins tested, specifically Concanavalin A (ConA) and Sambucus Nigra Agglutinin (SNA). This contrasted to lectin staining of RCs in the intestine of common carp, where four of the eight lectins showed a positive reaction; Dolichos Biflorus Agglutinin (DBA), Wheat Germ Agglutinin (WGA), SNA and ConA. RCs in eel and carp intestine were immunoreactive with antibodies to lysozyme and i-NOS. The occurrence of the inflammatory peptides lysozyme and i-NOS in RCs of the eel and common carp poses in favour that these cells are involved in the mechanism of defence against pathogens.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 171121
[Lr] Last revision date:171121
[St] Status:Publisher
[do] DOI:10.1111/jfd.12751

  4 / 1096 MEDLINE  
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[PMID]: 29159657
[Au] Autor:Basu S; Ghosh M; Bhunia RK; Ganguly J; Banik BK
[Ad] Address:Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Howrah, West Bengal, India.
[Ti] Title:Polysaccharides from Dolichos biflorus Linn and Trachyspermum ammi Linn seeds: isolation, characterization and remarkable antimicrobial activity.
[So] Source:Chem Cent J;11(1):118, 2017 Nov 21.
[Is] ISSN:1752-153X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Polysaccharides are structurally complex and essential constituents of life, and therefore, studies directed to these kinds of molecules have received scientific attention. Despite an easy availability of Dolichos biflorus Linn and Trachyspermum ammi (Linn) seeds isolation, characterization and antimicrobial studies of polysaccharides derived from these two natural sources have not been investigated. Therefore, we report here isolation of polysaccharides, their purification and characterization from Dolichos biflorus Linn and Trachyspermum ammi (Linn) seeds. Gel permeation chromatography, GC-MS, SEM, XRD, EDX and FT-IR analyses show the presence of three pentose sugar such as D-ribose, D-arabinose, D-xylose and hexose sugar such as D-mannose, D-galactose and D-glucose. Unprecedented antimicrobial activity of these polysaccharides against Gram positive bacteria such as Staphylococcus aureus and Bacillus subtilis and Gram negative bacteria such as Escherichia coli and Pseudomonas aeruginosa are established.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 171121
[Lr] Last revision date:171121
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.1186/s13065-017-0349-2

  5 / 1096 MEDLINE  
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[PMID]: 29090980
[Au] Autor:Im AR; Kim YH; Kim YH; Yang WK; Kim SH; Song KH
[Ad] Address:1 KM Convergence Research Division, Korea Institute of Oriental Medicine , Daejeon, Korea.
[Ti] Title:Dolichos lablab Protects Against Nonalcoholic Fatty Liver Disease in Mice Fed High-Fat Diets.
[So] Source:J Med Food;, 2017 Nov 01.
[Is] ISSN:1557-7600
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Hyacinth bean, Dolichos lablab or Lablab purpureus, has been used for centuries in India and China as an edible pod and animal forage, as well as to treat diarrhea and other gastrointestinal disease in traditional Korean medicine. Recently, we have demonstrated that D. lablab extract (DLL-Ex) prevented free fatty acid-induced lipid accumulation in an in vitro cellular nonalcoholic fatty liver disease (NAFLD) model. In this study, we, thus, aimed at clarifying the hepatoprotective effects of DLL-Ex in a high-fat diet-induced in vivo animal NAFLD model, as well as at elucidating underlying mechanisms of identified effects. Sixty, 6-week-old, male C57BL/6J mice were randomly divided into six groups: a control group fed a low-fat diet, four high-fat diet (HFD) groups, three receiving daily oral supplementation of DLL-Ex (25, 50, and 100 mg/kg/day), and one HFD group receiving daily oral supplementation of MILK (100 mg/kg/day). Effects of DLL-Ex supplementation were evaluated by histopathological and histochemical assessments. DLL-Ex supplementation inhibited HFD-induced increases in body weight and body fat mass and ameliorated increases in body weight, manifested as decreased liver function tests, lower serum triglycerides and cholesterol levels, and increased serum adiponectin levels. The expression of hepatic genes involved in lipid droplet accumulation and in fatty acid uptake was also decreased. We provide evidence of a protective effect of DLL-Ex against HFD-induced fatty liver disease in an animal model.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 171101
[Lr] Last revision date:171101
[St] Status:Publisher
[do] DOI:10.1089/jmf.2017.4036

  6 / 1096 MEDLINE  
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[PMID]: 29084238
[Au] Autor:Li D; Yu H; Lin Q; Liu Y
[Ad] Address:Tianjin Medical University General Hospital, Tianjin, China.
[Ti] Title:Doliroside A from Dolichos falcata Klein suppressing amyloid ß-protein 42 fibrillogenesis: An insight at molecular level.
[So] Source:PLoS One;12(10):e0186590, 2017.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:A bioactive chemical constituent, doliroside A, from Chinese traditional herbal medicine Dolichos falcata Klein was isolated, purified and identified by 60% ethanol extraction, thin layer chromatography (TLC), high performance liquid chromatography (HPLC) and nuclear magnetic resonance (NMR) spectroscopy. Molecular interaction mechanism between doliroside and amyloid ß42 protein was evaluated by thioflavin T fluorescence (ThT), circular dichroism (CD), atomic force microscope (AFM), and differential scanning calorimeter (DSC) from the aspects of kinetics, secondary structure, morphology, and thermodynamics, respectively. Results show that the purity of doliroside A is 99.9% by HPLC, and its chemical structure is identified by 1H- and 13C-NMR. Doliroside A is observed to be concentration-dependent inhibiting the fibrillation of Aß42 with the IC50 value of 26.57 ± 1.6 µM. CD and DSC results imply that doliroside A can bind to the nuclei and oligomers of Aß42 to form a stable complex and suppress Aß42 fibrillation. AFM images show that doliroside A, after bound to the nuclei and oligomers, redirect Aß42 into off-pathway, amorphous oligomers. These findings not only provide a full insight into the molecular interaction mechanisms between Aß42 and doliroside A, but also facilitate the development of new native anti-AD drug of doliroside A compound.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171110
[Lr] Last revision date:171110
[St] Status:In-Process
[do] DOI:10.1371/journal.pone.0186590

  7 / 1096 MEDLINE  
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[PMID]: 28864014
[Au] Autor:Jones CJP; Silvia WJ; Hamilton CH; Geary TW; Zezeski AL; Wooding FBP
[Ad] Address:Maternal and Fetal Health Research Centre, Division of Developmental Biology and Medicine, School of Medical Sciences, Faculty of Biology, Medicine and Health, University of Manchester, St Mary's Hospital, Oxford Road, Manchester M13 9WL, UK. Electronic address: carolyn.jones@manchester.ac.uk.
[Ti] Title:Glycosylation and immunocytochemistry of binucleate cells in pronghorn (Antilocapra americana, Antilocapridae) show features of both Giraffidae and Bovidae.
[So] Source:Placenta;57:216-222, 2017 Sep.
[Is] ISSN:1532-3102
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Although the pronghorn (Antilocapra americana) resembles an antelope, its nearest relatives are the giraffe and okapi. In this study we have examined the placentae of 6 pronghorns using lectin- and immunocytochemistry to identify giraffid and bovid features. Binucleate cells (BNC) of the placenta exhibited features intermediate between those of the giraffe and bovine; Dolichos biflorus agglutinin binding - strong in the bovine BNC and absent in the giraffe - was evident in only a subpopulation of BNC while binding to blood vessels, as in the giraffe. Binding of Phytolacca americana agglutinin resembled that of the giraffe and okapi whereas many other glycans were found in all four clades. PAG antigens were similar to bovine and okapi but not giraffe. In summary, although the pronghorn outwardly resembles an antelope, placental BNC show giraffid features. Although each clade has its own individual characteristics, there are far more similarities than differences between them, emphasizing the common ancestry of all four clades.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 170902
[Lr] Last revision date:170902
[St] Status:In-Process

  8 / 1096 MEDLINE  
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[PMID]: 28543850
[Au] Autor:Summers EL; Cumming MH; Oulavallickal T; Roberts NJ; Arcus VL
[Ad] Address:School of Science, University of Waikato, Private Bag 3105, Hamilton, 3240, New Zealand.
[Ti] Title:Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.
[So] Source:Protein Sci;26(8):1627-1638, 2017 Aug.
[Is] ISSN:1469-896X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Extracellular nucleoside triphosphate diphosphohydrolases (NTPDases) are enzymes that hydrolyze extracellular nucleotides to the respective monophosphate nucleotides. In the past 20 years, NTPDases belonging to mammalian, parasitic and prokaryotic domains of life have been discovered, cloned and characterized. We reveal the first structures of NTPDases from the legume plant species Trifolium repens (7WC) and Vigna unguiculata subsp. cylindrica (DbLNP). Four crystal structures of 7WC and DbLNP were determined at resolutions between 1.9 and 2.6 Å. For 7WC, structures were determined for an -apo form (1.89 Å) and with the product AMP (2.15 Å) and adenine and phosphate (1.76 Å) bound. For DbLNP, a structure was solved with phosphate and manganese bound (2.60 Å). Thorough kinetic data and analysis is presented. The structure of 7WC and DbLNP reveals that these NTPDases can adopt two conformations depending on the molecule and co-factor bound in the active site. A central hinge region creates a "butterfly-like" motion of the domains that reduces the width of the inter-domain active site cleft upon molecule binding. This phenomenon has been previously described in Rattus norvegicus and Legionella pneumophila NTPDaseI and Toxoplasma gondii NTPDaseIII suggesting a common catalytic mechanism across the domains of life.
[Mh] MeSH terms primary: Adenosine Monophosphate/chemistry
Adenosine Triphosphate/chemistry
Apyrase/chemistry
Plant Proteins/chemistry
Trifolium/chemistry
Vigna/chemistry
[Mh] MeSH terms secundary: Adenosine Monophosphate/metabolism
Adenosine Triphosphate/metabolism
Amino Acid Sequence
Animals
Apyrase/genetics
Apyrase/metabolism
Catalytic Domain
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli/genetics
Escherichia coli/metabolism
Gene Expression
Isoenzymes/chemistry
Isoenzymes/genetics
Isoenzymes/metabolism
Kinetics
Legionella pneumophila/chemistry
Legionella pneumophila/enzymology
Manganese/chemistry
Manganese/metabolism
Models, Molecular
Phosphates/chemistry
Phosphates/metabolism
Plant Proteins/genetics
Plant Proteins/metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Rats
Recombinant Proteins/chemistry
Recombinant Proteins/genetics
Recombinant Proteins/metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Toxoplasma/chemistry
Toxoplasma/enzymology
Trifolium/enzymology
Vigna/enzymology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Isoenzymes); 0 (Phosphates); 0 (Plant Proteins); 0 (Recombinant Proteins); 415SHH325A (Adenosine Monophosphate); 42Z2K6ZL8P (Manganese); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.5 (Apyrase)
[Em] Entry month:1708
[Cu] Class update date: 170824
[Lr] Last revision date:170824
[Js] Journal subset:IM
[Da] Date of entry for processing:170526
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3199

  9 / 1096 MEDLINE  
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[PMID]: 28438092
[Au] Autor:Gómez-Santos L; Alonso E; Díaz-Flores L; Madrid JF; Sáez FJ
[Ad] Address:Department of Cell Biology and Histology, Training and Research Unit: Reproduction, Development, Aging and Cancer (TRU/UFI 11/44), School of Medicine and Nursing, University of the Basque Country UPV/EHU, Leioa, Vizcaya, Spain (LG-S, EA, FJS).
[Ti] Title:Characterization by Lectin Histochemistry of Two Subpopulations of Parietal Cells in the Rat Gastric Glands.
[So] Source:J Histochem Cytochem;65(5):261-272, 2017 05.
[Is] ISSN:1551-5044
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Parietal cells undergo a differentiation process while they move from the isthmus toward the pits and the base region of the gastric gland. The aim of this work was to analyze the rat gastric glands by lectin histochemistry to show the glycans expressed by upper (young) and lower (old) parietal cells. We used lectins recognizing the most frequent sugar moieties in mammals. Each lectin was assayed alone and in combination with several deglycosylation pretreatments: (1) ß-elimination, which removes O-linked oligosaccharides; (2) incubation with Peptide-N-glycosidase F, to remove N-linked glycans; (3) acid hydrolysis, which removes terminal sialic acid moieties; (4) methylation-saponification, to remove sulfate groups from sugar residues; and (5) glucose oxidase, a technique carried out with the lectin concanavalin A to convert glucose into gluconic acid. The lectins from Helix pomatia, Dolichos biflorus (DBA), Glycine max (soybean), Maclura pomifera, Arachis hypogaea (peanut), Bandeiraea simplicifolia (lectin I-B ), and Datura stramonium showed a different glycan expression in the parietal cells throughout the gastric gland. This difference supports that parietal cells undergo a maturation/degeneration process while the cells descend along the gland. The role of DBA as a marker of parietal cells previously reported should be taken with caution because these cells showed different reactivity for the lectin, ranging from negative to strong labeling.
[Mh] MeSH terms primary: Parietal Cells, Gastric/cytology
Plant Lectins/chemistry
Polysaccharides/analysis
[Mh] MeSH terms secundary: Animals
Histocytochemistry
Hydrolysis
Male
Oligosaccharides/chemistry
Parietal Cells, Gastric/chemistry
Rats, Sprague-Dawley
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Oligosaccharides); 0 (Plant Lectins); 0 (Polysaccharides)
[Em] Entry month:1706
[Cu] Class update date: 170823
[Lr] Last revision date:170823
[Js] Journal subset:IM
[Da] Date of entry for processing:170426
[St] Status:MEDLINE
[do] DOI:10.1369/0022155417694871

  10 / 1096 MEDLINE  
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[PMID]: 28268243
[Au] Autor:Vigneshwaran V; Thirusangu P; Vijay Avin BR; Krishna V; Pramod SN; Prabhakar BT
[Ad] Address:Molecular Biomedicine Laboratory, Postgraduate Department of Studies and Research in Biotechnology, Sahyadri Science College (Autonomous), Kuvempu University, Shivamogga, Karnataka, India.
[Ti] Title:Immunomodulatory glc/man-directed Dolichos lablab lectin (DLL) evokes anti-tumour response in vivo by counteracting angiogenic gene expressions.
[So] Source:Clin Exp Immunol;189(1):21-35, 2017 Jul.
[Is] ISSN:1365-2249
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Neovascularization and jeopardized immunity has been critically emphasized for the establishment of malignant progression. Lectins are the diverse class of carbohydrate interacting proteins, having great potential as immunopotentiating and anti-cancer agents. The present investigation sought to demonstrate the anti-proliferative activity of Dolichos lablab lectin (DLL) encompassing immunomodulatory attributes. DLL specific to glucose and mannose carbohydrate moieties has been purified to homogeneity from the common dietary legume D. lablab. Results elucidated that DLL agglutinated blood cells non-specifically and displayed striking mitogenicity to human and murine lymphocytes in vitro with interleukin (IL)-2 production. The DLL-conditioned medium exerted cytotoxicity towards malignant cells and neoangiogenesis in vitro. Similarly, in-vivo anti-tumour investigation of DLL elucidated the regressed proliferation of ascitic and solid tumour cells, which was paralleled with blockade of tumour neovasculature. DLL-treated mice showed an up-regulated immunoregulatory cytokine IL-2 in contrast to severely declined levels in control mice. Mechanistic validation revealed that DLL has abrogated the microvessel formation by weakening the proangiogenic signals, specifically nuclear factor kappa B (NF-κB), hypoxia inducible factor 1α (HIF-1 α), matrix metalloproteinase (MMP)-2 and 9 and vascular endothelial growth factor (VEGF) in malignant cells leading to tumour regression. In summary, it is evident that the dietary lectin DLL potentially dampens the malignant establishment by mitigating neoangiogenesis and immune shutdown. For the first time, to our knowledge, this study illustrates the critical role of DLL as an immunostimulatory and anti-angiogenic molecule in cancer therapeutics.
[Mh] MeSH terms primary: Mitogens/pharmacology
Neoplasms/drug therapy
Neovascularization, Pathologic/drug therapy
Plant Lectins/administration & dosage
Plant Lectins/pharmacology
[Mh] MeSH terms secundary: A549 Cells
Agglutination
Animals
Aorta/drug effects
Cell Culture Techniques
Chorioallantoic Membrane/drug effects
Cornea/blood supply
Cornea/drug effects
Disaccharides
Humans
Hypoxia-Inducible Factor 1, alpha Subunit/metabolism
Immunomodulation
Interleukin-2/metabolism
Matrix Metalloproteinase 3/metabolism
Matrix Metalloproteinase 9/metabolism
Mice
Mice, Inbred BALB C
Mitogens/immunology
Plant Lectins/immunology
Rats
Rats, Wistar
Seeds/chemistry
Vascular Endothelial Growth Factor A/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Disaccharides); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Interleukin-2); 0 (Mitogens); 0 (Plant Lectins); 0 (Vascular Endothelial Growth Factor A); 0 (dolichos Lablab lectin); 15761-61-2 (4-glucopyranosylmannose); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Entry month:1708
[Cu] Class update date: 170802
[Lr] Last revision date:170802
[Js] Journal subset:IM
[Da] Date of entry for processing:170308
[St] Status:MEDLINE
[do] DOI:10.1111/cei.12959


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