Journal of glycobiology最新文献_第8页

Simple Novel Assays in Glycobiology 糖生物学中简单新颖的检测方法

Journal of glycobiology Pub Date : 2014-11-17 DOI: 10.4172/2168-958X.1000112

S. Oppenheimer

{"title":"Simple Novel Assays in Glycobiology","authors":"S. Oppenheimer","doi":"10.4172/2168-958X.1000112","DOIUrl":"https://doi.org/10.4172/2168-958X.1000112","url":null,"abstract":"In response to an invitation from this journal, I am providing this mini-review of recent work from the Oppenheimer lab. Over the past 4 decades we have developed many assays that help us examine the role of specifc glycans in cellular interactions. Recently we have used two model systems for this work, the sea urchin embryo and yeast (Saccharomyces cerevisiae). We have developed two assays using the sea urchin embryo. One involves a microplate method where living sea urchin embryos are incubated with specific glycans or glycosidases. A specific set of cellular interactions, development of the primitive gut…archenteron, is examined over time in the presence and absence of the sugars or enzymes in living embryos. L-rhamnose and polyglucans have been identified as playing a role in mediating these cellular interactions. The second assay involves microdissection of the primitive gut away from the blastocoel roof to which it adheres. Using independently characterized glycosidases, we showed that polyglucans appear to mediate this cellular interaction. In the second system using yeast, we examine yeast disaggregation from lectin-derivatized agarose beads in the presence and absence of specific glycans using a quantitative, kinetic graphic profile assay. We found that D-melezitose was the best adhesion inhibitor and may be therapeutically useful in anti-adhesion venues of pathogen binding to cells and in cancer cell binding.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"3 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859303","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}

引用次数: 0

Modified, Rapid, and Accurate Method for the Quantification of Mucopolysaccharides in Urine 改进、快速、准确测定尿液中粘多糖的方法

Journal of glycobiology Pub Date : 2014-10-21 DOI: 10.4172/2168-958X.1000111

Zouhair Habbal M and Mohamad A Cherry

引用次数: 3

Progress in HIV-Carbohydrate Interactions: Infectivity of CCR5-Tropic HIV-1 is Enhanced by GP120 from CXCR4-Tropic Virus hiv -碳水化合物相互作用的研究进展:来自CXCR4-Tropic病毒的GP120增强了CCR5-Tropic HIV-1的感染性

Journal of glycobiology Pub Date : 2014-09-01 DOI: 10.4172/2168-958X.1000110

Birco Schwalbe, H. Hauser, M. Schreiber

引用次数: 1

Alterations of Heparan Sulfate Proteoglycans in Cancer 硫酸肝素蛋白聚糖在癌症中的改变

Journal of glycobiology Pub Date : 2014-07-18 DOI: 10.4172/2168-958X.1000109

I. Fernández-Vega, B. García, O. García-Suárez, S. Castañón, L. Quirós

引用次数: 9

Exploring the Protein Glycosylation Pathways to Find New TherapeuticAlternatives 探索蛋白质糖基化途径寻找新的治疗方案

Journal of glycobiology Pub Date : 2014-06-27 DOI: 10.4172/2168-958X.1000E108

H. Mora-Montes

引用次数: 2

Targeted Shifting of Protein Glycosylation Profiles in Mammalian Cell Culture through Media Supplementation of Cobalt 在哺乳动物细胞培养中通过补充钴靶向转移蛋白糖基化谱

Journal of glycobiology Pub Date : 2014-06-11 DOI: 10.4172/2168-958X.1000108

Patrick Hossler, Christopher Racicot, Sean McDermott

{"title":"Targeted Shifting of Protein Glycosylation Profiles in Mammalian Cell Culture through Media Supplementation of Cobalt","authors":"Patrick Hossler, Christopher Racicot, Sean McDermott","doi":"10.4172/2168-958X.1000108","DOIUrl":"https://doi.org/10.4172/2168-958X.1000108","url":null,"abstract":"Protein glycosylation has had a long storied history towards impacting various structural, functional, and physiochemical properties of the proteins they are attached to. This important and often critical post-translational modification is thus monitored closely during the manufacturing of recombinant proteins, especially those destined for clinical use where the levels are often required to be maintained within an acceptable historically-proven range. In the present work, we highlight a systematic study towards the selective use of cobalt for the targeted shifting of protein glycosylation profiles on recombinant proteins through cell culture media supplementation. Cobalt was found to considerably increase the percentage of galactosylated N-glycan species, and thus support an increase in the overall extent of terminal protein glycosylation. These aforementioned results were found to be reproducible across different cell lines expressing different proteins, and cultured at different scales. Through the selective supplementation of cobalt, the targeted shifting of protein glycosylation profiles is demonstrated, as well as a potential means for ensuring biologic comparability.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"3 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2014-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000108","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70858948","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}

引用次数: 9

Immune Response Modulation by Tumor-Secreted Glycosphingolipids 肿瘤分泌的鞘糖脂调节免疫反应

Journal of glycobiology Pub Date : 2014-04-25 DOI: 10.4172/2168-958X.1000107

R. Lardone, Ingrid Cely, P. Sieling, Delphine J. Lee

引用次数: 3

Novel Cancer Vaccination System Based on Human Endo-Β-N-Acetyl Glucosaminidase Gene Delivery 基于人Endo-Β-N-Acetyl氨基葡萄糖酶基因传递的新型癌症疫苗接种系统

Journal of glycobiology Pub Date : 2014-04-12 DOI: 10.4172/2168-958X.1000106

Satoshi Watanabe, S. Haraguchi, Shingo Nakamura, T. Sakurai, S. Mugikura, K. Kajiwara, M. Kimura, Masahiro Sato

{"title":"Novel Cancer Vaccination System Based on Human Endo-Β-N-Acetyl Glucosaminidase Gene Delivery","authors":"Satoshi Watanabe, S. Haraguchi, Shingo Nakamura, T. Sakurai, S. Mugikura, K. Kajiwara, M. Kimura, Masahiro Sato","doi":"10.4172/2168-958X.1000106","DOIUrl":"https://doi.org/10.4172/2168-958X.1000106","url":null,"abstract":"Cancer vaccination elicits an immune response against specific glycans or proteins expressed on the cell surface after gene transfer has occurred. We previously demonstrated that N-acetylglucosamine (GlcNAc) residues exposed after digestion with endo-β-galactosidase, a carbohydrate-digesting enzyme, elicited this type of immune response, probably as a result of the presence of natural antibodies recognizing GlcNAc residues in host animals. Treatment of a cell with endo-β-N-acetylglucosaminidase (ENGase), an enzyme that cleaves the amide bond between the proximal GlcNAc residues at the side chain of an asparagine residue on N-glycans, also causes exposure of GlcNAc residues on the cell surface. In this study, we examined whether mouse melanoma B16 cells transfected with a human ENGase (hENGase) cDNA expression construct, are susceptible to an immune attack after subcutaneous grafting to the syngenic host. The recombinant B16 cells overexpressing hENGase had approximately 3-fold more cell-surface GlcNAc residues than their parental cells. The grafting experiment revealed that the tumor size was approximately one-tenth of that derived from wild-type grafted cells. Direct injection and subsequent in vivo electroporation of a hENGase expression vector into B16 solid tumors resulted in regression of the tumors. Our present results strongly suggest that the ENGase is a useful tool for novel cancer vaccination.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"3 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70858651","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}

引用次数: 6

Anti-Tumour and Chemosensitising Effect of a Combination of Bromelain + N-Acetyl Cysteine with Cisplatin or 5-Fu on Malignant Peritoneal Mesothelioma Cells 菠萝蛋白酶+ n -乙酰半胱氨酸联合顺铂或5-Fu对恶性腹膜间皮瘤细胞的抗肿瘤和化学增敏作用

Journal of glycobiology Pub Date : 2013-06-29 DOI: 10.4172/2168-958X.S1-005

K. Pillai, J. Akhter, A. Ehteda, S. Badar, T. Chua, D. Morris

{"title":"Anti-Tumour and Chemosensitising Effect of a Combination of Bromelain + N-Acetyl Cysteine with Cisplatin or 5-Fu on Malignant Peritoneal Mesothelioma Cells","authors":"K. Pillai, J. Akhter, A. Ehteda, S. Badar, T. Chua, D. Morris","doi":"10.4172/2168-958X.S1-005","DOIUrl":"https://doi.org/10.4172/2168-958X.S1-005","url":null,"abstract":"normally poor however, cytoreductive surgery and hyperthermic intraperitoneal chemotherapy has increased survival in some patients. Hence, new therapies are needed. MUC1 is a glycosylation dependant protein associated with tumour invasiveness, metastasis and chemo resistance. Bromelain, a cysteine proteinase, hydrolyses glycosidic bonds, whilst N-Acetyl cysteine reduces disulphide bonds in glycoprotein. Hence, we investigated the anti-tumour effect of these agents in MUC 1 expressing MPM cell lines. Materials and Methods: The cell lines were treated to various concentrations of bromelain, NAC and combinations of NAC + bromelain, NAC + bromelain + cisplatin or 5-FU. Their cell viabilities were assessed at 48 hours with sulfhordamine B assay. Finally, with western blotting, the effect of NAC and the combination of NAC + bromelain on cellular survival proteins were investigated. Results: Combination of NAC (10 mM) with bromelain (75 ug/ml) showed 97% and 88% cell proliferation inhibition in YOU and PET cells, respectively. In triple combination, the addition of cisplatin to only 5.0 mM NAC and bromelain increased cytotoxicity in YOU cells but absent at 10.0 mM NAC concentration. However, in PET cells, triple combinations with cisplatin had no effect. The addition of 5-FU in triple combinations showed an increase in cytotoxicity with 5.0 mM NAC and bromelain in YOU cells. No increase in cytotoxicity was seen with addition of 10 mM NAC. In PET cells, the addition 5-FU to 5.0 mM NAC + 50 ug/ml bromelain, enhanced cytotoxicity significantly but was absent at all other combinations. Conclusion: The combination of bromelain and NAC may be developed as anti-tumour agents for treating MPM, with a possible role in combined therapy with current chemotherapeutic agents.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"2013 1","pages":"1-11"},"PeriodicalIF":0.0,"publicationDate":"2013-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.S1-005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862827","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}

引用次数: 9

Towards Integrative Glycoinformatics for Glycan Based Biomarker Cancer Research and Discovery 基于糖聚糖的生物标志物癌症研究与发现的整合糖信息学研究

Journal of glycobiology Pub Date : 2013-06-24 DOI: 10.4172/2168-958X.S1-004

Sandra V. Bennun, Deniz Bayçın Hızal, R. Ranzinger, M. Betenbaugh

{"title":"Towards Integrative Glycoinformatics for Glycan Based Biomarker Cancer Research and Discovery","authors":"Sandra V. Bennun, Deniz Bayçın Hızal, R. Ranzinger, M. Betenbaugh","doi":"10.4172/2168-958X.S1-004","DOIUrl":"https://doi.org/10.4172/2168-958X.S1-004","url":null,"abstract":"Despite some recent successes in deciphering new cancer molecular makers, there is still a clear and continual need to develop new technologies that help characterizing existing biomarkers or facilitate discovery of new biomarkers. An important systems biology opportunity on this respect is provided by understanding the glycosylation changes associated with cancer. Indeed, interest in cancer glycosylation has expanded over the past decade and large amount of data relevant to cancer glycosylation has been accumulating rapidly. Furthermore, new and improved sophisticated glycoinformatics tools, methods and databases for glycan analysis now offer the opportunity to investigate this data for understanding the role that glycans play in cancer glycosylation. Here we summarize developments of glycoinformatics tools to support analysis of cancer glycosylation and experimental glycoproteomics approaches. In addition, we discuss challenges faced by glycoinformatics for the integration and interrogation of disparate high-throughput glycan data sets in order to assimilate technologies and better address cancer glycosylation. We also provide examples of integrative glycoinformatics approaches that lead to a better understanding of cancer glycosylation as a complex cellular process.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"39 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2013-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.S1-004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862946","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}

引用次数: 2