scholarly journals Further Characterization of the Target of a Potential Aptamer Biomarker for Pancreatic Cancer: Cyclophilin B and Its Posttranslational Modifications

2013 ◽  
Vol 23 (6) ◽  
pp. 435-442 ◽  
Author(s):  
Partha Ray ◽  
Bruce A. Sullenger ◽  
Rebekah R. White
Keyword(s):  
Pancreatic Cancer ◽  
Posttranslational Modifications ◽  
Cyclophilin B

Molecular Alterations in Exocrine Neoplasms of the Pancreas

2009 ◽  
Vol 133 (3) ◽  
pp. 405-412 ◽  
Author(s):  
Prathibha Ranganathan ◽  
H. C. Harsha ◽  
Akhilesh Pandey
Keyword(s):  
Pancreatic Cancer ◽  
Posttranslational Modifications ◽  
Systems Approach ◽  
Germ Line ◽  
Expression Patterns ◽  
Molecular Alterations ◽  
The Past ◽  
Pancreatic Cancers ◽  
Expression Of Genes

Abstract Context.—Pancreatic cancer is one of the leading causes of cancer-related deaths. Most cases are diagnosed at an advanced stage when the disease is beyond surgical intervention. Molecular studies during the past decade have contributed greatly to our understanding of this disease. Various germ-line and somatic mutations associated with pancreatic cancers have been characterized, along with abnormal variations in the gene expression patterns. A thorough characterization of molecular alterations such as genetic and epigenetic changes, alterations in the expression of genes and changes in proteins, and posttranslational modifications in pancreatic cancer could lead to a better understanding of its pathogenesis. Objective.—To provide an overview of the various molecular alterations in pancreatic cancer and the methodologies used to catalog such alterations. Data Sources.—Published studies about various molecular alterations at the genomic, epigenetic, transcriptomic, and proteomic levels in pancreatic cancer. Conclusions.—The available data from pancreatic cancer suggests that there are a large number of molecular alterations at genomic, epigenetic, transcriptomic, and proteomic levels. It is now possible to initiate a systems approach to studying pancreatic cancer especially in light of newer initiatives to dissect the pancreatic cancer genome.

Galectin-3 is modulated in pancreatic cancer cells under hypoxia and nutrient deprivation

2020 ◽  
Vol 401 (10) ◽  
pp. 1153-1165 ◽  
Author(s):  
Antônio F. da Silva Filho ◽  
Lucas B. Tavares ◽  
Maira G. R. Pitta ◽  
Eduardo I. C. Beltrão ◽  
Moacyr J. B. M. Rêgo
Keyword(s):  
Pancreatic Cancer ◽  
Cell Death ◽  
Mrna Expression ◽  
Cancer Cells ◽  
Ductal Adenocarcinoma ◽  
Reverse Transcription Pcr ◽  
Pancreatic Cancer Cells ◽  
Through Flow ◽  
Galectin 3

AbstractPancreatic ductal adenocarcinoma is one of the most aggressive tumors with a microenvironment marked by hypoxia and starvation. Galectin-3 has been evaluated in solid tumors and seems to present both pro/anti-tumor effects. So, this study aims to characterize the expression of Galectin-3 from pancreatic tumor cells and analyze its influence for cell survive and motility in mimetic microenvironment. For this, cell cycle and cell death were accessed through flow cytometry. Characterization of inside and outside Galectin-3 was performed through Real-Time Quantitative Reverse Transcription PCR (qRT-PCR), immunofluorescence, Western blot, and ELISA. Consequences of Galectin-3 extracellular inhibition were investigated using cell death and scratch assays. PANC-1 showed increased Galectin-3 mRNA expression when cultivated in hypoxia for 24 and 48 h. After 24 h in simultaneously hypoxic/deprived incubation, PANC-1 shows increased Galectin-3 protein and secreted levels. For Mia PaCa-2, cultivation in deprivation was determinant for the increasing in Galectin-3 mRNA expression. When cultivated in simultaneously hypoxic/deprived condition, Mia PaCa-2 also presented increasing for the Galectin-3 secreted levels. Treatment of PANC-1 cells with lactose increased the death rate when cells were incubated simultaneously hypoxic/deprived condition. Therefore, it is possible to conclude that the microenvironmental conditions modulate the Galectin-3 expression on the transcriptional and translational levels for pancreatic cancer cells.

scholarly journals Insights into the Functionality of the Putative Residues Involved in Enterocin AS-48 Maturation

2010 ◽  
Vol 76 (21) ◽  
pp. 7268-7276 ◽  
Author(s):  
Rubén Cebrián ◽  
Mercedes Maqueda ◽  
José Luis Neira ◽  
Eva Valdivia ◽  
Manuel Martínez-Bueno ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
High Efficiency ◽  
Specific Protein ◽  
Culture Conditions ◽  
Site Directed Mutagenesis ◽  
Circular Structure ◽  
Cleavage Enzyme ◽  
Site Recognition ◽  
Biosynthetic Machinery

ABSTRACT AS-48 is a 70-residue, α-helical, cationic bacteriocin produced by Enterococcus faecalis and is very singular in its circular structure and its broad antibacterial spectrum. The AS-48 preprotein consists of an N-terminal signal peptide (SP) (35 residues) followed by a proprotein moiety that undergoes posttranslational modifications to yield the mature and active circular protein. For the study of the specificity of the region of AS-48 that is responsible for maturation, three single mutants have been generated by site-directed mutagenesis in the as-48A structural gene. The substitutions were made just in the residues that are thought to constitute a recognition site for the SP cleavage enzyme (His-1, Met1) and in those involved in circularization (Met1, Trp70). Each derivative was expressed in the enterococcal JH2-2 strain containing the necessary native biosynthetic machinery for enterocin production. The importance of these derivatives in AS-48 processing has been evaluated on the basis of the production and structural characterization of the corresponding derivatives. Notably, only two of them (Trp70Ala and Met1Ala derivatives) could be purified in different forms and amounts and are characterized for their bactericidal activity and secondary structure. We could not detect any production of AS-48 in JH2-2(pAM401-81 His-1Ile ) by using the conventional chromatographic techniques, despite the high efficiency of the culture conditions applied to produce this enterocin. Our results underline the different important roles of the mutated residues in (i) the elimination of the SP, (ii) the production levels and antibacterial activity of the mature proteins, and (iii) protein circularization. Moreover, our findings suggest that His-1 is critically involved in cleavage site recognition, its substitution being responsible for the blockage of processing, thereby hampering the production of the specific protein in the cellular culture supernatant.

206 Identification and Whole Transcriptome Characterization of Pancreatic Cancer Stem Cells

2012 ◽  
Vol 142 (5) ◽  
pp. S-50-S-51
Author(s):  
Christina Vorvis ◽  
George A. Poultsides ◽  
Jeffrey A. Norton ◽  
Maria Hatziapostolou ◽  
Dimitrios Iliopoulos
Keyword(s):  
Pancreatic Cancer ◽  
Stem Cells ◽  
Cancer Stem Cells ◽  
Whole Transcriptome ◽  
Pancreatic Cancer Stem Cells

Protein pIShifts due to Posttranslational Modifications in the Separation and Characterization of Proteins

2005 ◽  
Vol 77 (9) ◽  
pp. 2745-2755 ◽  
Author(s):  
Kan Zhu ◽  
Jia Zhao ◽  
David M. Lubman ◽  
Fred R. Miller ◽  
Timothy J. Barder
Keyword(s):  
Posttranslational Modifications

scholarly journals Biochemical and molecular characterization of N66 from the shell ofPinctada mazatlanica

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7212
Author(s):  
Crisalejandra Rivera-Perez ◽  
Catalina Magallanes-Dominguez ◽  
Rosa Virginia Dominguez-Beltran ◽  
Josafat Jehu Ojeda-Ramirez de Areyano ◽  
Norma Y. Hernandez-Saavedra
Keyword(s):  
Posttranslational Modifications ◽  
Protein A ◽  
Pearl Oyster ◽  
Peptide Sequence ◽  
Calcium Carbonate Precipitation ◽  
Base Pairs ◽  
Shell Matrix ◽  
Glycosylation Sites ◽  
Shell Matrix Proteins

Mollusk shell mineralization is a tightly controlled process made by shell matrix proteins (SMPs). However, the study of SMPs has been limited to a few model species. In this study, the N66 mRNA of the pearl oysterPinctada mazatlanicawas cloned and functionally characterized. The full sequence of the N66 mRNA comprises 1,766 base pairs, and encodes one N66 protein. A sequence analysis revealed that N66 contained two carbonic anhydrase (CA) domains, a NG domain and several glycosylation sites. The sequence showed similarity to the CA VII but also with its homolog protein nacrein. The native N66 protein was isolated from the shell and identified by mass spectrometry, the peptide sequence matched to the nucleotide sequence obtained. Native N66 is a glycoprotein with a molecular mass of 60–66 kDa which displays CA activity and calcium carbonate precipitation ability in presence of different salts. Also, a recombinant form of N66 was produced inEscherichia coli, and functionally characterized. The recombinant N66 displayed higher CA activity and crystallization capability than the native N66, suggesting that the lack of posttranslational modifications in the recombinant N66 might modulate its activity.

scholarly journals N-glycan chitobiose core biosynthesis by Agl24 strengthens the hypothesis of an archaeal origin of the eukaryal N-glycosylation

2021 ◽  
Author(s):  
Benjamin H. Meyer ◽  
Ben A. Wagstaff ◽  
Panagiotis S. Adam ◽  
Sonja-Verena Albers ◽  
Helge C. Dorfmueller
Keyword(s):  
Posttranslational Modifications ◽  
Biochemical Characterization ◽  
Similar Process ◽  
List Type ◽  
Histidine Residue ◽  
Functional Importance ◽  
Domains Of Life ◽  
Distant Relation ◽  
Identification And Characterization

AbstractProtein N-glycosylation is the most common posttranslational modifications found in all three domains of life. The crenarchaeal N-glycosylation begins with the synthesis of a lipid-linked chitobiose core structure, identical to that in eukaryotes. Here, we report the identification of a thermostable archaeal beta-1,4-N-acetylglucosaminyltransferase, named archaeal glycosylation enzyme 24 (Agl24), responsible for the synthesis of the N-glycan chitobiose core. Biochemical characterization confirmed the function as an inverting β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol glycosyltransferase. Substitution of a conserved histidine residue, found also in the eukaryotic and bacterial homologs, demonstrated its functional importance for Agl24. Furthermore, bioinformatics and structural modeling revealed strong similarities between Agl24 and both the eukaryotic Alg14/13 and a distant relation to the bacterial MurG, which catalyze the identical or a similar process, respectively. Our data, complemented by phylogenetic analysis of Alg13 and Alg14, revealed similar sequences in Asgardarchaeota, further supporting the hypothesis that the Alg13/14 homologs in eukaryotes have been acquired during eukaryogenesis.HighlightsFirst identification and characterization of a thermostable β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol glycosyltransferase (GT family 28) in Archaea.A highly conserved histidine, within a GGH motif in Agl24, Alg14, and MurG, is essential for function of Agl24.Agl24-like homologs are broadly distributed among Archaea.The eukaryotic Alg13 and Alg14 are closely related to the Asgard homologs, suggesting their acquisition during eukaryogenesis.

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