Type Lectin Research Articles

Characterization of a common carp intelectin gene with bacterial binding and agglutination activity

Intelectin (ITLN) is a type of glycan-binding lectin involved in many physiological processes and some human diseases. Here we report a common carp intelectin (cITLN). Like other orthologs, cITLN also contains a conserved fibrinogen-related domain (FReD) and a unique intelectin domain, expresses in all the tissues tested with the highest level in the hindgut, and responds to bacterial challenge in the acute phase. We also expressed cITLN in Escherichia coli (E. coli) system, and the purified recombinant cITLN could neither affect the surface of bacteria nor inhibit the growth of bacteria, but it can agglutinate both gram-positive and gram-negative bacteria in a calcium-dependent manner. The cITLN's ability of agglutination of gram-positive bacteria is stronger than that of gram-negative bacteria. This is probably because recombinant cITLN could binding peptidoglycan (PGN) with a higher degree to lipopolysaccharide (LPS). Our results of cITLN provided new insight into the function of intelectin in the intestinal mucosal immunity.

Siglec-7 is a predictive biomarker for the efficacy of cancer vaccination against metastatic colorectal cancer.

Cancer immunotherapy, including vaccination, is considered a major scientific and medical breakthrough. However, cancer immunotherapy does not result in durable objective responses against colorectal cancer (CRC). To improve the efficacy of immunotherapy, the present study investigated several biomarkers for selecting patients who were expected to respond well to immunotherapy. Firstly, a comprehensive proteomic analysis was performed using tumor tissue lysates from patients enrolled in a phase II study, in which five human leukocyte antigen (HLA)-A*24:02-restricted peptides were administered. Sialic acid-binding immunoglobulin type lectin (Siglec)-7 was identified as a potential predictive biomarker. Subsequently, this biomarker was validated using western blot analysis, and immunofluorescence using tissue samples from the patients enrolled in the phase II study. The expression levels of Siglec-7 detected by immunofluorescence were quantified and their association with overall survival (OS) in patients treated with the peptide vaccine was examined. Furthermore, considering the important role of tumor-infiltrating lymphocytes (TILs) for CRC prognosis, the densities of CD3+, CD4+, CD8+ and forkhead box P3 (FOXP3)+ T cells in CRC tissues were examined and compared with Siglec-7 expression. The mean expression levels of Siglec-7 were significantly higher in patients with poor prognosis, with an OS of ≤2 years, as shown in comprehensive proteomic analysis (P=0.016) and western blot analysis (P=0.025). Immunofluorescence analysis demonstrated that Siglec-7 was expressed in intratumoral macrophages. The OS in patients with high Siglec-7 expression was significantly shorter than in that in patients with low Siglec-7 expression (P=0.017) in the HLA-A*24:02-matched patients. However, this difference was not observed in the HLA-unmatched patients. There was no significant difference in OS between patients according to the numbers of TILs, nor significant correlation between TILs and Siglec-7 expression. In conclusion, Siglec-7 expression in macrophages in tumor tissue may be a novel predictive biomarker for the efficacy of immunotherapy against metastatic CRC.

Affinity Control of Monosaccharide Conjugated Peptides against Lectins with a Set of Amino Acid Substitutions on α-Helical Structures.

Saccharides are well-known to play important roles in various biological events through specific interactions with target molecules such as carbohydrate-binding proteins (so-called lectins). Although characterization and identification of lectin molecules with saccharides are essential to understand biological events, they are still difficult due to weak interactions of saccharides, especially with monosaccharides. Herein, we demonstrate enhancement and control of monosaccharide affinity toward lectin proteins using chemical conjugation of monosaccharides with structurally regulated peptide and amino acid substitution. Thermodynamic analyses of the interactions by isothermal calorimetry measurements were performed to characterize the interactions between monosaccharide-conjugated peptide and the lectin molecules in detail. Conjugation with α-helical 16-mer short peptides drastically enhanced the affinity to lectins as compared with peptides with random coil structures, indicating that the α-helical peptide-based scaffold cooperatively interacted with lectins through additional interactions by suitable amino acids. Furthermore, suitable arrangement of the amino acids surrounding the monosaccharides on the α-helix afforded the conjugated peptides with varied affinities for two types of lectins. Our results indicate that the affinity of monosaccharide-conjugated peptides toward lectins is generally designable by appropriate conjugation of a simple monosaccharide with designed peptides, leading to the construction of a monosaccharide-modified peptide microarray toward high-throughput identification and/or screening of lectins in various biological events.

Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-type Lectin (MGL).

Simple SummaryChanges in glycosylation occur during cancer transformation, altering the interaction among tumor, immune cells and microenvironment and impacting the anti-tumor immune response. The Macrophage galactose-like C-type lectin (MGL), expressed by dendritic cells (DCs), is the immune receptor recognizing the tumor Tn carbohydrate antigen. Recently, Tn/STn-CA125 glycoforms have been proposed as a promising tumor-associated biomarker and the targeting of MGL-Tn axis has been shown to be a valid therapeutic approach in ovarian cancer mouse model. Here we designed a chromatography method to identify glycoproteins relevant in DCs-tumor cell interaction by probing the ovarian cancer O-glycoproteome by means of MGL. The potential MGL binders identified were located on the cell membrane and in the intracellular compartment and matrisome, suggesting that MGL may play a role in sensing microenvironmental cues. These results may be relevant to investigate immune system-tumor interactions and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions.Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type O-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer O-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn O-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the O-glycopeptidome by MGL and Vicia villosa agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions.

The role of Garcinol in abrogating cyclophosphamide/radiation nephrotoxicity via suppressing Mincle/Syk/NF-κB signaling pathway

Radiation and chemotherapy are toxic agents; their clinical utility, nevertheless, and curative effect are restricted by toxic side consequences such as nephrotoxicity. This study aims to determine the potential protective effects of Garcinol (G) (10 mg/kg/orally/daily for 4 weeks), a natural polyisoprenylated benzophenone, against renal injury in cyclophosphamide (CA) (150 mg/kg i.p. single-dose) and/or radiation (R) delivered as fractionated doses of 2 Gy/week up to total cumulative dose of 6 Gy to induce toxicity in rats. Kidney injury has been examined by histopathological investigation. Garcinol treatment showed amelioration by a significant decrease in the inflammatory markers (IL-1β and IL-6). Similarly, Garcinol-injected rats exhibited a significant decline in monocyte chemotactic protein-1(MCP-1), macrophage inducible c type lectin (Mincle), spleen tyrosine kinase (Syk), transcriptional factor (NF-kB), and toll-like receptor (TLR-4) compared to the CA + R group. Additionally, histopathological and immunohistochemical examination showed that the administration of CA and/or γ-irradiated rats induced severe injury in kidney, and a decrease in Cyclin d1 immunostain level compared to the control group. Finally, this work may verify the protective role of Garcinol significantly shielding the kidney from damage by inhibiting Mincle expression, which also promotes M1 to M2, and prevents Syk and TLR-4/NF-kB activation.

Mechanism of inflammatory response in associated comorbidities in COVID-19

Background and aimsThe outbreak of the new coronavirus, SARS-CoV-2, causes a respiratory disease and individuals with pre-existing cardiometabolic disorders display worse prognosis through the infection course. The aim of this minireview is to present epidemiological data related to metabolic comorbidities in association with the SARS-CoV-2. MethodsThis is a narrative mini-review with Pubmed search until April 23, 2020 using the keywords COVID-19, SARS-CoV-2, treatment of coronavirus and following terms: diabetes mellitus, obesity, arterial hypertension, ACE-inhibitors, cytokine storm, immune response and vitamin D. ResultsStudies indicate that obese individuals are more likely to develop infections, and that adipose tissue serves as a pathogen reservoir. In diabetic individuals higher rate of inflammatory processes is seen due to constant glucose recognition by C type lectin receptors. Hypertensive individuals, usually grouped with other conditions, are treated with drugs to reduce blood pressure mostly through ACEi and ARB, that leads to increased ACE2 expression, used by SARS-CoV-2 for human’s cell entry. Until now, the studies have shown that individuals with those conditions and affected by COVID-19 present an uncontrolled release of pro-inflammatory cytokines and an unbalanced immune response, leading to the cytokine storm phenomenon. Vitamin D is highlighted as a potential therapeutic target, because in addition to acting on the immune system, it plays an important role in the control of cardiometabolic diseases. ConclusionCurrently, since there is no proven and effective antiviral therapy for SARS-CoV-2, the efforts should focus on controlling inflammatory response and reduce the risks of associated complications.

Complement C3 deficiency exacerbates development of cardiovascular lesions in the LCWE-induced Kawasaki Disease Vasculitis

Abstract Background Kawasaki disease (KD) is an acute febrile systemic vasculitis of childhood, mostly affecting the coronary arteries. A central feature of acute KD is the activation of the innate and adaptive immune systems. Serum complement component C3 is significantly increased in children during the acute stages of KD, and a polymorphism of a C type lectin, mannose binding lectin (MBL), has been associated with KD vasculitis and coronary artery lesions. However, the role of the complement pathway in KD vasculitis remains unclear. Objective Determine if the complement system contributes to KD pathogenesis in the Lactobacillus casei cell wall extract (LCWE)-mediated murine model of KD vasculitis. Methods and Results Serum levels of various complement proteins were elevated in LCWE-injected mice. We observed that the LCWE extract, rich in rhamnose and a TLR2 ligand, was able to bind both C3 and MBL in-vitro. Genetic deletion of C3 exacerbated LCWE-induced aortitis, coronary arteritis and abdominal aorta dilation and aneurysm. Furthermore, in-vivo blockade of C5 with a C5aR1 antagonist (PMX205) also increased these cardiovascular lesions in LCWE mice. Conclusions Blocking key components of the complement system, such as C3 and C5aR, significantly enhanced cardiovascular lesions in the LCWE-induced KD vasculitis mouse model. Thus, C3 or downstream activation fragments may play a protective role in the development of KD cardiovascular lesions. Whether this protection is due to complement mediated increased clearance of immune complexes or common carbohydrate pathogen molecules will need to be determined and may help our current understanding of the immunopathologic mechanisms of KD vasculitis. (Supported by NIH grant AI072726 to MA)

A comparative review of intelectins.

Intelectin (ITLN) is a new type of glycan-binding lectin. It has been demonstrated to agglutinate bacteria probably due to its carbohydrate-binding capacity, suggesting its role in an innate immune response. It is involved not only in many physiological processes but also in some human diseases such as asthma, heart disease, inflammatory bowel disease, chronic obstructive pulmonary disease and cancer. Up to now, intelectin orthologs have been identified in placozoans, urochordatas, cephalochordates and several vertebrates, such as cyclostomata, fish, amphibians and mammals. Although the sequences of intelectins in different species are conserved, their expression patterns, quaternary structures and functions differ considerably among and within species. We summarize the evolution of the intelectin gene family, the tissue distribution, structure and functions of intelectins. We conclude that intelectin plays a role in innate immune response and there are still potential functions of intelectin awaiting discovery.

Sialic Acid-Siglec-E Interactions During Pseudomonas aeruginosa Infection of Macrophages Interferes With Phagosome Maturation by Altering Intracellular Calcium Concentrations.

Pseudomonas aeruginosa (PA) is commonly associated with nosocomial and chronic infections of lungs. We have earlier demonstrated that an acidic sugar, sialic acid, is present in PA which is recognized and bound by sialic acid binding immunoglobulin type lectins (siglecs) expressed on neutrophils. Here, we have tried to gain a detailed insight into the immunosuppressive role of sialic acid-siglec interactions in macrophage-mediated clearance of sialylated PA (PA+Sia). We have demonstrated that PA+Sia shows enhanced binding (~1.5-fold) to macrophages due to additional interactions between sialic acids and siglec-E and exhibited more phagocytosis. However, internalization of PA+Sia is associated with a reduction in respiratory burst and increase in anti-inflammatory cytokines secretion which is reversed upon desialylation of the bacteria. Phagocytosis of PA+Sia is also associated with reduced intracellular calcium ion concentrations and altered calcium-dependent signaling which negatively affects phagosome maturation. Consequently, although more PA+Sia was localized in early phagosomes (Rab5 compartment), only fewer bacteria reach into the late phagosomal compartment (Rab7). Possibly, this leads to reduced phagosome lysosome fusion where reduced numbers of PA+Sia are trafficked into lysosomes, compared to PA−Sia. Thus, internalized PA+Sia remain viable and replicates intracellularly in macrophages. We have also demonstrated that such siglec-E-sialic acid interaction recruited SHP-1/SHP-2 phosphatases which modulate MAPK and NF-κB signaling pathways. Disrupting sialic acid-siglec-E interaction by silencing siglec-E in macrophages results in improved bactericidal response against PA+Sia characterized by robust respiratory burst, enhanced intracellular calcium levels and nuclear translocation of p65 component of NF-κB complex leading to increased pro-inflammatory cytokine secretion. Taken together, we have identified that sialic acid-siglec-E interactions is another pathway utilized by PA in order to suppress macrophage antimicrobial responses and inhibit phagosome maturation, thereby persisting as an intracellular pathogen in macrophages.

Concanavalin A Enhanced Proliferation and Osteogenic Differentiation of Dental Pulp Stem Cells.

Objective Dental pulp stem cells (DPSCs) can be used as a component in the formation of regenerative dentine during direct pulp capping therapy. Concanavalin A (ConA) is a type of lectin with a molecular weight of 26 kDa derived from the Canavalia ensiformis plant. Lectins possess strong proliferation and differentiation abilities in various animal cells including lymphocytes, osteoblasts, and chondrocytes. The aim of study was to determine the effect of ConA on the proliferation and osteogenic differentiation of DPSCs in vitro . Materials and Methods In this in vitro study, DPSCs were isolated from third molars before ConA induction was performed at concentrations of 5 and 10 μg/mL. The proliferation assay was determined by 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) assay. Osteogenic differentiation was determined by means of mineralization. Statistical Analysis Data were analyzed using analysis of variance and a Student’s t -test. The p -value was set at 0.05. Results The addition of 5 and 10 µg/mL of ConA to DPSCs can significantly increase the proliferation and osteogenic differentiation of DPSCs ( p ≤0.05). Conclusion ConA can increase the proliferation and osteogenic differentiation of DPSCs.

A method for detecting tumor cells derived from colorectal cancer by targeting cell surface glycosylation with affinity capillary electrophoresis

Circulating tumor cells (CTCs) are involved in metastasis; thus, one of the most important approaches for identifying metastatic cancer is to detect CTCs in blood. In the present study, we examined whether directly analyzing cells with capillary electrophoresis (CE) could distinguish cancer cells from normal cells, based on differences in cell surface glycosylation. We compared human colorectal cancer (CRC) cell lines to a normal colon epithelium cell line. Our results demonstrated that direct CE analysis could successfully distinguish between CRC and normal cells with high reproducibility, based on migration times. We found that the weighted-average migration time was significantly shorter for CRC cells than for normal cells. Next, we observed changes in the electrophoretic behaviors of CRC cells by adding five different types of lectins. When Aleuria aurantia lectin was added, migration delays were observed in CRC cells, but not in normal colon cells. Therefore, by focusing on shifts in migration time after adding specific lectins, we could distinguish cancer cells from normal cells. These findings suggested that this diagnostic method of directly analyzing cells with CE after adding specific lectin(s) could be useful for detecting the difference in the sugar moieties on a surface of normal and cancer cells.

Galectin-3 as a modifier of anti-microbial immunity: Unraveling the unknowns.

Galectins play diverse roles in pathophysiology of infectious diseases and cancers. Galectin-3 is one of the most studied family member and the only chimeric type lectin. Many aspects of its biogenesis, range of activities, and the disease-modifying potential particularly during microbial infections are yet to be known. We review our current understanding of these issues and also highlight gaps in better defining the immune modulatory potential of galectin-3 during different stages of host responsiveness when an infection sets in. Additionally, we discuss commonly used strategies to disrupt galectin-3 functions both extracellulalry and intracellularly. Existing and improved novel strategies could help fine-tune immune responses to achieve better prognosis of infectious diseases.

Purification of Sugar-Binding Peptides from L-Type Lectins.

L-type lectin is the most famous plant lectin family, and purification of many kinds of L-type lectins were reported previously. In general, this type of lectin is a major component of the seed proteins, and it is purified from the seeds. Recently, affinity carriers immobilized with haptenic sugars are generally used for purification.

A sugar-lectin rich interface between soft tissue and the stiff byssus of Atrina pectinata.

Maintaining durable adhesion between soft tissues and relatively hard implant materials is one of the most elusive technological difficulties in bionic devices due to contact damage between mechanically mismatched materials. Although there are many examples of coexistence of soft and hard tissues in living organisms, relatively little is known about the mechanisms used to overcome mechanical mismatches occurring at the interface between soft and hard tissues. Among the various creatures possessing mechanically mismatched biological tissues, Atrina pectinata is a good model system where the interface between stiff byssal threads and soft tissues is distributed all over an extended organ. In this study, we found a wide distribution of various types of carbohydrates and lectins at the mechanically mismatched interface of the byssus of Atrina using histological methods and proteomics. Reversible and robust interactions between the carbohydrate and lectins at the interface would play a major role in mitigating the contact damage at the Atrina interface. Based on these results, the adhesion between sugar and lectin would be useful to overcome a wide range of contact damage observed in research studies on bionic devices.

Bombay and Lewis phenotype testing in correlation with leukocyte adhesion deficiency type II: The blood bank's role in diagnosis

Leukocyte adhesion deficiency type II (LAD II) is a rare hereditary disorder caused by the mutation in the guanosine diphosphate-fucose transporter gene (SLC35C1). LAD II is characterized by inexpression of ABO antigens (i.e., Bombay phenotype) and the lack of Lewis red blood cell (RBC) antigens. In addition to high neutrophil counts, patients also manifest recurrent infections with developmental delays and stunted growth. Blood bank laboratory tests such as blood grouping, RBC phenotyping, antibody screening and identification of the nature of the antibody were conducted in order to confirm the consequences associated with this gene anomaly in this case report. Type and screen results initially identified the patient as group “O” Rh positive with pan-reactive antibody screening cells and identification panel cells. The patient plasma showed significant incompatibility to all O-positive donors' RBCs. The patient's RBCs were tested against anti-H lectin and Lewis (Lea, Leb) typing antisera and showed no reaction, which meant that the patient does not express neither Lewis antigens nor H antigen on his red cell. The presence of anti-H (in a Bombay phenotype individual) explained the reactivity to reagent red cells and crossmatched incompatibility of Group O units as these cells naturally contained the H antigen.

Neutrophils activated by BJcuL, a C-type lectin isolated from Bothrops jararacussu venom, decrease the invasion potential of neuroblastoma SK-N-SH cells in vitro.

ABSTRACTBackground:Neuroblastoma is a pediatric tumor with a mortality rate of 40% in the most aggressive cases. Tumor microenvironment components as immune cells contribute to the tumor progression; thereby, the modulation of immune cells to a pro-inflammatory and antitumoral profile could potentialize the immunotherapy, a suggested approach for high-risk patients. Preview studies showed the antitumoral potential of BJcuL, a C- type lectin isolated from Bothrops jararacussu venom. It was able to induce immunomodulatory responses, promoting the rolling and adhesion of leukocytes and the activation of neutrophils.Methods:SK-N-SH cells were incubated with conditioned media (CM) obtained during the treatment of neutrophils with BJcuL and fMLP, a bacteria-derived peptide highly effective for activating neutrophil functions. Then we evaluated the effect of the same stimulation on the co-cultivation of neutrophils and SK-N-SH cells. Tumor cells were tested for viability, migration, and invasion potential.Results:In the viability assay, only neutrophils treated with BJcuL (24 h) and cultivated with SK-N-SH were cytotoxic. Migration of tumor cells decreased when incubated directly (p < 0.001) or indirectly (p < 0.005) with untreated neutrophils. When invasion potential was evaluated, neutrophils incubated with BJcuL reduced the total number of colonies of SK-N-SH cells following co-cultivation for 24 h (p < 0.005). Treatment with CM resulted in decreased anchorage-free survival following 24 h of treatment (p < 0.001).Conclusion:Data demonstrated that SK-N-SH cells maintain their migratory potential in the face of neutrophil modulation by BJcuL, but their invasive capacity was significantly reduced.

MGL1 Receptor Plays a Key Role in the Control of T. cruzi Infection by Increasing Macrophage Activation through Modulation of ERK1/2, c-Jun, NF-κB and NLRP3 Pathways.

Macrophage galactose-C type lectin (MGL)1 receptor is involved in the recognition of Trypanosoma cruzi (T. cruzi) parasites and is important for the modulation of the innate and adaptive immune responses. However, the mechanism by which MGL1 promotes resistance to T. cruzi remains unclear. Here, we show that MGL1 knockout macrophages (MGL1−/− Mφ) infected in vitro with T. cruzi were heavily parasitized and showed decreased levels of reactive oxygen species (ROS), nitric oxide (NO), IL-12 and TNF-α compared to wild-type macrophages (WT Mφ). MGL1−/− Mφ stimulated in vitro with T. cruzi antigen (TcAg) showed low expression of TLR-2, TLR-4 and MHC-II, which resulted in deficient splenic cell activation compared with similar co-cultured WT Mφ. Importantly, the activation of p-ERK1/2, p-c-Jun and p-NF-κB p65 were significantly reduced in MGL1−/− Mφ exposed to TcAg. Similarly, procaspase 1, caspase 1 and NLRP3 inflammasome also displayed a reduced expression that was associated with low IL-β production. Our data reveal a previously unappreciated role for MGL1 in Mφ activation through the modulation of ERK1/2, c-Jun, NF-κB and NLRP3 signaling pathways, and to the development of protective innate immunity against experimental T. cruzi infection.

A GM1b/asialo-GM1 oligosaccharide-binding R-type lectin from purplish bifurcate mussels Mytiliseptavirgata and its effect on MAP kinases.

A 15‐kDa lectin, termed SeviL, was isolated from Mytilisepta virgata (purplish bifurcate mussel). SeviL forms a noncovalent dimer that binds strongly to ganglio‐series GM1b oligosaccharide (Neu5Acɑ2‐3Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc) and its precursor, asialo‐GM1 (Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc). SeviL also interacts weakly with the glycan moiety of SSEA‐4 hexaose (Neu5Acα2‐3Galβ1‐3GalNAcβ1‐3Galα1‐4Galβ1‐4Glc). A partial protein sequence of the lectin was determined by mass spectrometry, and the complete sequence was identified from transcriptomic analysis. SeviL, consisting of 129 amino acids, was classified as an R(icin B)‐type lectin, based on the presence of the QxW motif characteristic of this fold. SeviL mRNA is highly expressed in gills and, in particular, mantle rim tissues. Orthologue sequences were identified in other species of the family Mytilidae, including Mytilus galloprovincialis, from which lectin MytiLec‐1 was isolated and characterized in our previous studies. Thus, mytilid species contain lectins belonging to at least two distinct families (R‐type lectins and mytilectins) that have a common β‐trefoil fold structure but differing glycan‐binding specificities. SeviL displayed notable cytotoxic (apoptotic) effects against various cultured cell lines (human breast, ovarian, and colonic cancer; dog kidney) that possess asialo‐GM1 oligosaccharide at the cell surface. This cytotoxic effect was inhibited by the presence of anti‐asialo‐GM1 oligosaccharide antibodies. With HeLa ovarian cancer cells, SeviL showed dose‐ and time‐dependent activation of kinase MKK3/6, p38 MAPK, and caspase‐3/9. The transduction pathways activated by SeviL via the glycosphingolipid oligosaccharide were triggered apoptosis.DatabaseNucleotide sequence data have been deposited in the GenBank database under accession numbers MK434191, MK434192, MK434193, MK434194, MK434195, MK434196, MK434197, MK434198, MK434199, MK434200, and MK434201.

Characterization of Lectin from Colpomenia Sinuosa and Effect of Physico Chemical Parameters on Haemagglutination Activity

Lectin is a protein which has the ability to bind carbohydrates and named as haemagglutinin. Lectins with specific carbohydrate specificity have been purified from various plant tissues and other organisms and exploited extensively in many aspects of biochemistry and biomedicine. Similar to land plants, lectins from marine algae appear to be useful in some biological applications. Although several studies on lectins from marine algae have been reported till date, few lectins from algae have been characterized in detail. The present study was focused on the lectin isolated from C.sinuosa. The algal lectin has high sugar specificity with N-acetylglucosamine and higher enzyme activity with trypsin. This lectin was identified as CaCl2 dependent – ‘C’ type lectin and was sensitive to EDTA. Higher H.A titre value was observed with CaCl2 and the lower with MnCl2 and ZnCl2 . Significant lectin activity was observed between pH 7 to 8 and temperature between 20 to 40 O C

Glycosylation changes in inflammatory diseases.

Glycosylation is one of the most important modifications of proteins and lipids, and cell surface glycoconjugates are thought to play important roles in a variety of biological functions including cell-cell and cell-substrate interactions, bacterial adhesion, cell immunogenicity and cell signaling. Alterations of glycosylation are observed in a number of inflammatory diseases. Pro-inflammatory cytokines have been shown to modulate cell surface glycosylation by regulating the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of glycan chains, inducing the expression of specific carbohydrate antigens at the cell surface that can be recognized by different types of lectins or by bacterial adhesins, contributing to the development of diseases. Glycosylation can also regulate biological functions of immune cells by recruiting leukocytes to inflammation sites with pro- or anti-inflammatory effects. Cell surface proteoglycans provide a large panel of binding sites for many mediators of inflammation, and regulate their bio-availability and functions. In this review, we summarize the current knowledge of the glycosylation changes occurring in mucin type O-linked glycans, glycosaminoglycans, as well as in glycosphingolipids, with a particular focus on cystic fibrosis and neurodegenerative diseases, and their consequences on cell interactions and disease progression.