{"title":"Preclinical Evaluation of Symmetrical Diiodinated Squaraine Dye on Experimental Animal Models","authors":"Soumya Ms","doi":"10.4172/2168-958X.S1-003","DOIUrl":"https://doi.org/10.4172/2168-958X.S1-003","url":null,"abstract":"Photodynamic therapy involves administration of a tumor localizing photosensitizing agent, followed by the activation of the agent by light of a specific wavelength. This therapy results in a sequence of photochemical and photobiological processes that cause irreversible photo damage to the tumor tissue. Only a few photosensitizers have received official approval around the world. But they are with some adverse side effects. Because of these draw backs search for new photosensitizers is in progress. The dye selected in our study- Symmetric diiodinated squaraine- is one of these newly developed photosensitizers. We have examined the in vivo distribution of the dye on normal and skin tumor induced animal models to check the retention time of the dye. The mechanism of action of photosensitizers in selective killing of cancer cells involves the generation of oxidative stress whereby the malignant cells are damaged, in presence of light of appropriate wavelength. Thus we also intended to study whether there is the initiation of oxidative damage in the normal tissues in the body of dye injected mice in the absence of light. The results show that maximum amount of the dye was accumulated in the different organs of the body 4 h after the administration. The compound is tumor specific since after 24 h of injection, it was retained only in the tumor site and in the immediate surroundings of the tumor. This shows the selectivity of the dye to tumor tissue. The administration of the squaraine dye in the system induces no significant change in the level of lipid peroxidation products and activity of antioxidant enzymes when compared to the control mice. This indicates that the squaraine dye does not induce any oxidative stress to the normal tissues in the body and hence the dye can be safely used for photodynamic therapy.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"2013 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2013-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.S1-003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Pseudomyxoma peritonei: Uninvited goblet cells, ectopic MUC2","authors":"A. Amini, Samar Masoumi Moghaddam, A. Ehteda","doi":"10.4172/2168-958X.S1-002","DOIUrl":"https://doi.org/10.4172/2168-958X.S1-002","url":null,"abstract":"Pseudomyxoma peritonei (PMP) is a challenging clinical syndrome characterized by multifocal peritoneal collections of extracellular mucins. Mucins are high molecular weight, heavily glycosylated proteins differentially expressed by various types of epithelial cells. In this pathological condition, goblet cells originating from a mucinous tumor of the appendix gain access to the peritoneal cavity where they secrete mucin ectopically. Secreted mucin thus accumulates and forms the characteristic feature of the disease. Therefore, goblet cells and secreted mucins constitute the two key elements of the disease. MUC2 is the PMP's specific, predominant mucin. It is a highly viscous, gel-forming mucin that accounts for the characteristic appearance of PMP mucinous deposits as compared to the mucinous implants of ovarian origin. Mucin deposits are the real cause of PMP’s morbid complications irrespective of the site of origin, the mechanism of peritoneal spread, or the level of neoplastic transformation. In this article, role of mucin in gastrointestinal physiology and PMP pathology are reviewed and the potential of MUC2 as a therapeutic target are discussed","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"2013 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2013-05-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862756","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sachin M. Eligar, R. Pujari, Mohammed Azharuddin Savanur, Nagaraja N. Nagre, Srikanth Barkeer, A. Ingle, R. Kalraiya, Bale M. Swamy, P. Shastry, S. Inamdar
{"title":"Rhizoctonia Bataticola Lectin (RBL) Induces Apoptosis in Human Ovarian Cancer PA-1 Cells and Suppresses Tumor Growth In Vivo","authors":"Sachin M. Eligar, R. Pujari, Mohammed Azharuddin Savanur, Nagaraja N. Nagre, Srikanth Barkeer, A. Ingle, R. Kalraiya, Bale M. Swamy, P. Shastry, S. Inamdar","doi":"10.4172/2168-958X.S1-001","DOIUrl":"https://doi.org/10.4172/2168-958X.S1-001","url":null,"abstract":"Background: A lectin from the plant pathogenic fungus Rhizoctonia bataticola (RBL) has shown unique sugarbinding specificity towards the complex N-glycans, which are known to be expressed in many cancers, including ovarian cancer. Previous studies have demonstrated that RBL exerts cytotoxic effects on human ovarian cancer PA-1 cells. In the present study, we determined the signaling mechanism of RBL-induced cytotoxicity in PA-1 cells upon binding to cell surface receptors and also assessed the anti-tumor activity of RBL in NOD-SCID mice bearing ovarian xenografts. Methods: Cytotoxicity was determined by MTT assay, Cell cycle analysis, Annexin V staining, and expression of caspase-3 was determined by flow cytometry using specific fluorescent detection reagents. Western blotting was carried out to observe the intermediates of apoptotic pathway. Results: Treatment of PA-1 cells with RBL decreased their viability in a dose- and time- dependent manner. Cell cycle analysis revealed an increase in the hypo diploid population in response to lectin treatment. RBL-treated cells stained with Annexin V and PI showed an increase in both the early and late apoptotic populations. The mechanism of RBL-induced apoptosis in PA-1 cells was assessed by the observed decrease in MMP (ΔΨm), release of cytochrome-c, activation of caspase-9 and -3, and cleavage of PARP. Specific pharmacological inhibitors revealed the involvement of caspase-9 and -3 but not caspase-8. RBL at a subtoxic concentration (50 μg/mouse) suppressed tumor growth in NOD-SCID mice bearing PA-1 xenografts. Conclusions: The present study demonstrates that, RBL induced cytotoxicity in PA-1 cells is mediated by intrinsic apoptotic pathway. The present study strengthens the merit of RBL for its potential application in ovarian cancer research.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"2013 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2013-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862668","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Koichiro Yamamoto, Hideo Hori, Yoshihiro Yamamoto, Kazuo Takahashi, Y. Yuzawa, Y. Hiki
{"title":"Development of a Polyclonal Antibody Against Synthetic Human Immunoglobulin A1 Hinge Glycopeptide","authors":"Koichiro Yamamoto, Hideo Hori, Yoshihiro Yamamoto, Kazuo Takahashi, Y. Yuzawa, Y. Hiki","doi":"10.4172/2168-958X.1000103","DOIUrl":"https://doi.org/10.4172/2168-958X.1000103","url":null,"abstract":"Background: Undergalactosylated IgA1 has been found to be increased in IgA nephropathy (IgAN) by an ELISA assay using Helix aspersa agglutinin (HAA) that recognizes N-acetylgalactosamine (GalNAc). In this study, we developed a polyclonal antibody (anti-sHGP antibody) against a synthetic IgA1 hinge peptide with five GalNAc residues. \u0000Methods: The specificity of the anti-sHGP antibody was evaluated through the incremental treatment of IgA with corresponding glycosidases. Then, the susceptibility of the IgA to anti-sHGP antibody was compared among IgAN patients (n=39), patients with other forms of kidney diseases (OKD, n= 36) and healthy controls (n=37), using ELISA assay. The association of the binding abilities between anti-sHGP antibody and HAA were evaluated blindly using same 85 sera. \u0000Results: The binding ability of the anti-sHGP antibody was increased relative to the incremental treatments of neuraminidase (desialo-IgA), galactosidase (desialo/degalacto IgA). The binding levels of anti-sHGP antibody against serum IgA were significantly higher in IgAN patients compared to both healthy controls (P=0.008) and those with OKD (P=0.049). The binding levels of anti-sHGP antibody were closely related to those of HAA ELISA in the same patient sera (RR2=0.5964). \u0000Conclusions: It was certified that the anti-sHGP antibody recognized GalNAc residues in the hinge peptide of human IgA1 as well as HAA. The increased antigenicity of IgA against the antibody in IgAN suggested that a serum IgA1 exposing GalNAc residue was increased in IgAN. It would be necessary to identify the precise structure of O-glycans specific to IgAN for developing a more specific antibody.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"2012 1","pages":"1-3"},"PeriodicalIF":0.0,"publicationDate":"2012-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70858613","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Fucanome and Galactanome: Marine Glycomics Contribution","authors":"V. Pomin","doi":"10.4172/2168-958X.1000101","DOIUrl":"https://doi.org/10.4172/2168-958X.1000101","url":null,"abstract":"Following the genome, transcriptome and proteome, the glycome has currently launched in biology bringing apparently more challenges than the first projects. The long major conception of carbohydrates as just energetically involved class of biomolecules has fallen apart as innumerable essential biological actions have been raised, impossible to be enlisted all together at once. Such actions involve not only vital roles in cell and physiology but within a different context they also include potent therapeutic actions in coagulation, thrombosis, inflammation, virosis, pathogenesis, tumorigenesis, metastasis and angiogenesis. Glycomics is so extensive project that subdivision is necessary for its progress. Specific segments of research have been created about particular bioactive sugar classes such as sialome for sialic acids, and heparanomics for heparan bioactive domains. Fucanome and galactanome must be also included in the recent glycomics age with respect to the relatively new class of marine fucose- or galactose-composing polysaccharides named sulfated fucans and sulfated galactans. These glycans are very biologically relevant since they show potent pharmacological properties in many of the above-mentioned systems; besides in sea-urchins they are responsible to control a very rare case of carbohydrate-mediated cell signaling event, the acrosome reaction. The structure of these glycans is very restricted to phyla or species of occurrence. Among all marine organisms, only invertebrates and red algae have been known so far to express high molecular weight polymers composed of well-defined structures. These structural features are unique and very rare among any bioactive polysaccharide ever studied. This would make fucanome and galactanome differential glycomics subprojects in terms of structure and phylogeny. This paper not only brings out novel segments and their respective contribution to glycomics but also highlights the great relevance of pharmacological effects of these new glycans in the current glycome era.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2012-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70858542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Luis A. Pérez-García, D. F. Díaz-Jiménez, Adolfo López-Esparza, H. Mora-Montes
{"title":"Role of Cell Wall Polysaccharides during Recognition of Candida albicans by the Innate Immune System","authors":"Luis A. Pérez-García, D. F. Díaz-Jiménez, Adolfo López-Esparza, H. Mora-Montes","doi":"10.4172/2168-958X.1000102","DOIUrl":"https://doi.org/10.4172/2168-958X.1000102","url":null,"abstract":"Candida albicans is a dimorphic, opportunistic fungal pathogen responsible for most of the systemic candidiasis reported worldwide. The cell wall is the outermost component of this pathogen, which protects the cell from sudden changes in the external environment, is in close contact with host tissues and cells, and is elaborated by polysaccharides that are not synthesized by human cells. Thus, it is not surprising that the wall is the main source of pathogen-associated molecular patterns that are recognized by immune cells, and recognition of such components is critical for the establishment of a protective anti-Candida response. Here we summarize the current information related to the C. albicans innate immune sensing, underlying the importance of cell wall polysaccharides for the recognition of this pathogen.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2012-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70858596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}