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Journal articles on the topic 'Anti-Saccharomyces cerevisiae antibody'

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Published: 25 May 2024

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1

Fedrigo, Aiessa, Thelma L. Skare, André Luiz Bortoluzzi, and Renato Nisihara. "ASCA (Anti-Saccharomyces cerevisiae Antibody) in Patients With Scleroderma." JCR: Journal of Clinical Rheumatology 25, no. 1 (January 2019): 24–27. http://dx.doi.org/10.1097/rhu.0000000000000759.

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2

Oshitani, Nobuhide. "Anti-Saccharomyces Cerevisiae Antibody and 5-aminosalicylic Acid Treatment." American Journal of Gastroenterology 99, no. 5 (May 2004): 955. http://dx.doi.org/10.1111/j.1572-0241.2004.40044.x.

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3

Teml, Alexander, and Walter Reinisch. "Anti-Saccharomyces Cerevisiae Antibody and 5-aminosalicylic Acid Treatment: Response." American Journal of Gastroenterology 99, no. 5 (May 2004): 956. http://dx.doi.org/10.1111/j.1572-0241.2004.40193.x.

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4

Oshitani, N., F. Hato, Y. Jinno, Y. Sawa, S. Nakamura, T. Matsumoto, S. Seki, S. Kitagawa, and T. Arakawa. "IgG subclasses of anti Saccharomyces cerevisiae antibody in inflammatory bowel disease." European Journal of Clinical Investigation 31, no. 3 (March 2001): 221–25. http://dx.doi.org/10.1046/j.1365-2362.2001.00798.x.

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5

Filik, Levent, and Ibrahim Biyikoglu. "Differentiation of Behcet’s disease from inflammatory bowel diseases: Anti-saccharomyces cerevisiae antibody and anti-neutrophilic cytoplasmic antibody." World Journal of Gastroenterology 14, no. 47 (2008): 7271. http://dx.doi.org/10.3748/wjg.14.7271.

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6

Tandio Saputro, Shania Safera, Khayu Wahyunita, Astutiati Nurhasanah, Yudhi Nugraha, Irvan Faizal, Sabar Pambudi, and Andri Pramesyanti Pramono. "Expression of modified enhanced green fluorescent polyarginine protein in Saccharomyces cerevisiae INVSc1." F1000Research 12 (January 3, 2023): 1. http://dx.doi.org/10.12688/f1000research.123181.1.

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Background: The enhanced green fluorescent protein (EGFP) gene is a reporter gene that can be used to optimize protein isolation procedures and the functional working of a transduction protein. EGFP, with the addition of eleven arginine residues, has been engineered to functionally improve the protein transduction process, which can later be used for cell reprogramming like induced pluripotent stem cells. The addition of six histidine amino acid residues at its C-terminal is intended for the protein isolation process using the His-tag antibody. Methods: The study aimed to investigate the optimization of the EGFP polyarginine protein expression in Saccharomyces cerevisiae in sufficient quantities for the protein isolation stage. This study also analyzed EGFP expression without polyarginine to analyze the polyarginine addition effect on expression processes. Protein expression was qualitatively measured by looking at expression fluorescence and protein levels of EGFP and EGFP - PolyR proteins. Results: Bands on Western Blots with 6×His-tag monoclonal antibody (primary antibody) and Goat anti-mouse IgG HRP (secondary antibody) showed the EGFP polyarginine and EGFP proteins were expressed in Saccharomyces cerevisiae INVSc1 at relatively low levels. The lyticase incubation time modification and administration of 3-5 kDa microfilter to concentrate increased the yield of isolated protein. Conclusions: The sufficient amount of protein isolation in S. cerevisiae can be achieved by using lyticase and sonicators combination for the lysis process.

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7

Vermeire, Severine, Sofie Joossens, Marc Peeters, Fred Monsuur, Godelieve Marien, Xavier Bossuyt, Peter Groenen, Robert Vlietinck, and Paul Rutgeerts. "Comparative study of ASCA (Anti–Saccharomyces cerevisiae antibody) assays in inflammatory bowel disease." Gastroenterology 120, no. 4 (March 2001): 827–33. http://dx.doi.org/10.1053/gast.2001.22546.

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8

Makharia, Govind K., Vikas Sachdev, Rajiva Gupta, Suman Lal, and R. M. Pandey. "Anti-Saccharomyces cerevisiae Antibody Does Not Differentiate Between Crohn's Disease and Intestinal Tuberculosis." Digestive Diseases and Sciences 52, no. 1 (December 8, 2006): 33–39. http://dx.doi.org/10.1007/s10620-006-9527-0.

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9

Choi, Chang Hwan, Tae Il Kim, Byung Chang Kim, Sung Jae Shin, Sang Kil Lee, Won Ho Kim, and Hyon Suk Kim. "Anti-Saccharomyces cerevisiae Antibody in Intestinal Behçetʼs Disease Patients: Relation to Clinical Course." Diseases of the Colon & Rectum 49, no. 12 (December 2006): 1849–59. http://dx.doi.org/10.1007/s10350-006-0706-z.

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10

Belazi, Maria, Alexandra Fleva, Drakoulis Drakoulakos, and Despina Panayiotidou. "Comparison of salivary IgA and systemic IgA and IgG antibodies to Saccharomyces cerevisiae in HIV-infected subjects." International Journal of STD & AIDS 14, no. 7 (July 1, 2003): 458–62. http://dx.doi.org/10.1258/095646203322025759.

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Our objective was to investigate the concentrations of IgA and IgG antibodies to Saccharomyces cerevisiae in whole saliva and serum samples from HIV-infected patients and to compare them with the corresponding antibody values of healthy controls. A cross-sectional design was used. The test group consisted of 23 HIV-infected male individuals, aged 20-41 years old, free of any other systemic disease. Twenty healthy subjects aged 27-43 years old served as controls. Whole unstimulated saliva and blood were collected from all subjects. IgA concentrations in saliva and IgA and IgG concentrations in serum were measured by solid-phase enzyme-linked immunosorbent assay. Salivary antibody concentrations were calculated by reference to a pooled standard saliva obtained from 10 healthy males with high levels of anti- S. cerevisiae antibody activity. Total IgA and IgG concentrations were measured by nephelometry/tholocymetry assay. No significant difference was observed in salivary specific IgA and serum specific IgG levels to S. cerevisiae, while serum specific IgA were significantly lower in HIV infected patients compared to control group. Opportunistic infections due to S. cerevisiae, although rare, cannot be dismissed. This yeast can show a potential virulence in debilitated patients, therefore, further extensive investigation should be considered.

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11

Griffiths, Anne M., and Mary Zachos. "Antineutrophil Cytoplasmic Antibodies and Anti-Saccharomyces cerevisiae Antibody: Clinical Tools or Clues for Research?" Journal of Pediatric Gastroenterology and Nutrition 30, no. 1 (January 2000): 1. http://dx.doi.org/10.1097/00005176-200001000-00006.

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12

Standaert–Vitse, Annie, Thierry Jouault, Peggy Vandewalle, Céline Mille, Mimouna Seddik, Boualem Sendid, Jean–Maurice Mallet, Jean–Frédéric Colombel, and Daniel Poulain. "Candida albicans Is an Immunogen for Anti–Saccharomyces cerevisiae Antibody Markers of Crohn’s Disease." Gastroenterology 130, no. 6 (May 2006): 1764–75. http://dx.doi.org/10.1053/j.gastro.2006.02.009.

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13

Vermeulen, N., S. Vermeire, P. Rutgeerts, and X. Bossuyt. "Likelihood ratio for Crohnʼs disease as a function of Anti-Saccharomyces cerevisiae antibody concentration." Inflammatory Bowel Diseases 16, no. 1 (January 2010): 5–6. http://dx.doi.org/10.1002/ibd.20905.

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14

Ashorn, Sara, Hanna Raukola, Tuuli Välineva, Merja Ashorn, Bo Wei, Jonathan Braun, Immo Rantala, et al. "Elevated Serum Anti-Saccharomyces cerevisiae, Anti-I2 and Anti-OmpW Antibody Levels in Patients with Suspicion of Celiac Disease." Journal of Clinical Immunology 28, no. 5 (May 22, 2008): 486–94. http://dx.doi.org/10.1007/s10875-008-9200-9.

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15

Gorgel, Ahmet, Cem Cankaya, and Mehmet Tecellioglu. "Anti-Saccharomyces Cerevisiae as Unusual Antibody in Autoimmune Polyglandular Syndrome Type III: A Case Report." Endocrine, Metabolic & Immune Disorders - Drug Targets 19, no. 1 (January 3, 2019): 90–94. http://dx.doi.org/10.2174/1871530318666180817143536.

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Backgraund and Objective: Anti-Saccharomyces Cerevisiae Antibodies (ASCA) that are considered to reflect immune response against increased intestinal permeability due to mucosal damage are among the serological markers of Crohn’s Disease. </p><p> Methods: This microbial seromarker was recently shown to be elevated in several autoimmune disorders such as celiac disease, autoimmune liver diseases, type 1 diabetes, and Graves’ disease. Despite that fact, ASCA seropositivity in Autoimmune Polyglandular Syndrome (APS) has never been reported before. </p><p> Results: Herein, we present a 46-year-old woman who has uveitis, autoimmune thyroiditis, and primary ovarian failure. </p><p> Conclusion: Based on the coexistence of these diseases, the patient was diagnosed with APS type III. Moreover, ASCA seropositivity was detected although she has no overt intestinal disease.

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16

Kansal, Shivani, Anthony G. Catto-Smith, Karen Boniface, Sarah Thomas, Donald J. Cameron, Mark Oliver, George Alex, Carl D. Kirkwood, and Josef Wagner. "Variation of Gut Mucosal Microbiome With Anti-Saccharomyces cerevisiae Antibody Status in Pediatric Crohn Disease." Journal of Pediatric Gastroenterology and Nutrition 69, no. 6 (December 2019): 696–703. http://dx.doi.org/10.1097/mpg.0000000000002461.

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17

Kirschner, Barbara S., Barbara S. Reid, Ranjana Gokhale, and John Hart. "Chronic granulomatous disease (CGD) — another cause of anti-saccharomyces cerevisiae antibody (ASCA) positivty in children." Gastroenterology 118, no. 4 (April 2000): A104. http://dx.doi.org/10.1016/s0016-5085(00)82495-6.

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18

Musleh, Mustafa, Drew Triplett, and Salma Akram. "Sa1186 Prognostic Significance of Anti-Saccharomyces Cerevisiae Antibody (ASCA) in Southwestern Ohio Veteran IBD Population." Gastroenterology 148, no. 4 (April 2015): S—251. http://dx.doi.org/10.1016/s0016-5085(15)30826-x.

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19

Neff, M. W., and D. J. Burke. "Random segregation of chromatids at mitosis in Saccharomyces cerevisiae." Genetics 127, no. 3 (March 1, 1991): 463–73. http://dx.doi.org/10.1093/genetics/127.3.463.

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Abstract Previous experiments suggest that mitotic chromosome segregation in some fungi is a nonrandom process in which chromatids of the same replicative age are destined for cosegregation. We have investigated the pattern of chromatid segregation in Saccharomyces cerevisiae by labeling the DNA of a strain auxotrophic for thymidine with 5-bromodeoxyuridine. The fate of DNA strands was followed qualitatively by immunofluorescence microscopy and quantitatively by microphotometry using an anti-5-bromodeoxyuridine monoclonal antibody. Chromatids of the same replicative age were distributed randomly to daughter cells at mitosis. Quantitative measurements showed that the amount of fluorescence in the daughter nuclei derived from parents with hemilabeled chromosomes diminished in intensity by one half. The concentration of 5-bromodeoxyuridine used in the experiments had little effect on the frequency of either homologous or sister chromatid exchanges. We infer that the 5-bromodeoxyuridine was distributed randomly due to mitotic segregation of chromatids and not via sister chromatid exchanges.

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20

Hu, Chaojun, Chuiwen Deng, Shulan Zhang, Guang Song, Lijun Li, Xi Li, Li Wang, Fengchun Zhang, and Yongzhe Li. "Clinical significance and prevalence of anti-Saccharomyces cerevisiae antibody in Chinese patients with primary biliary cirrhosis." Clinical and Experimental Medicine 13, no. 4 (September 15, 2012): 245–50. http://dx.doi.org/10.1007/s10238-012-0207-4.

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21

Griffiths, Anne M., Mary Zachos, Philip M. Sherman, and Hans Büller. "Antineutrophil Cytoplasmic Antibodies and Anti‐Saccharomyces cerevisiae Antibody: Clinical Tools or Clues for Research?" Journal of Pediatric Gastroenterology and Nutrition 30, no. 1 (January 2000): 1. http://dx.doi.org/10.1002/j.1536-4801.2000.tb02648.x.

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22

Forcione, D. G. "Anti-Saccharomyces cerevisiae antibody (ASCA) positivity is associated with increased risk for early surgery in Crohn's disease." Gut 53, no. 8 (August 1, 2004): 1117–22. http://dx.doi.org/10.1136/gut.2003.030734.

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23

Kim, You Sun, Young-Ho Kim, Byong Duk Ye, Dong Won Park, Ji Won Kim, and Dong Soo Han. "Mannose-binding lectin deficiency is not associated with Anti-Saccharomyces cerevisiae antibody in Korean Crohn's disease patients." Clinica Chimica Acta 429 (February 2014): 206–11. http://dx.doi.org/10.1016/j.cca.2013.12.019.

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24

Brockerhoff, S. E., and T. N. Davis. "Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae." Journal of Cell Biology 118, no. 3 (August 1, 1992): 619–29. http://dx.doi.org/10.1083/jcb.118.3.619.

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Calmodulin was localized in Saccharomyces cerevisiae by indirect immunofluorescence using affinity-purified polyclonal antibodies. Calmodulin displays an asymmetric distribution that changes during the cell cycle. In unbudded cells, calmodulin concentrates at the presumptive site of bud formation approximately 10 min before bud emergence. In small budded cells, calmodulin accumulates throughout the bud. As the bud grows, calmodulin concentrates at the tip, then disperses, and finally concentrates in the neck region before cytokinesis. An identical staining pattern is observed when wild-type calmodulin is replaced with mutant forms of calmodulin impaired in binding Ca2+. Thus, the localization of calmodulin does not depend on its ability to bind Ca2+ with a high affinity. Double labeling of yeast cells with affinity-purified anti-calmodulin antibody and rhodamine-conjugated phalloidin indicates that calmodulin and actin concentrate in overlapping regions during the cell cycle. Furthermore, disrupting calmodulin function using a temperature-sensitive calmodulin mutant delocalizes actin, and act1-4 mutants contain a random calmodulin distribution. Thus, calmodulin and actin distributions are interdependent. Finally, calmodulin localizes to the shmoo tip in cells treated with alpha-factor. This distribution, at sites of cell growth, implicates calmodulin in polarized cell growth in yeast.

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25

Todorov, I. T., R. Pepperkok, R. N. Philipova, S. E. Kearsey, W. Ansorge, and D. Werner. "A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division." Journal of Cell Science 107, no. 1 (January 1, 1994): 253–65. http://dx.doi.org/10.1242/jcs.107.1.253.

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Molecular cloning and characterisation of a human nuclear protein designated BM28 is reported. On the amino acid level this 892 amino acid protein, migrating on SDS-gels as a 125 kDa polypeptide, shares areas of significant similarity with a recently defined family of early S phase proteins. The members of this family, the Saccharomyces cerevisiae Mcm2p, Mcm3p, Cdc46p/Mcm5p, the Schizosaccharomyces pombe Cdc21p and the mouse protein P1 are considered to be involved in the onset of DNA replication. The highest similarity was found with Mcm2p (42% identity over the whole length and higher than 75% over a conservative region of 215 amino acid residues), suggesting that BM28 could represent the human homologue of the S. cerevisiae MCM2. Using antibodies raised against the recombinant BM28 the corresponding antigen was found to be localised in the nuclei of various mammalian cells. Microinjection of anti-BM28 antibody into synchronised mouse NIH3T3 or human HeLa cells presents evidence for the involvement of the protein in cell cycle progression. When injected in G1 phase the anti-BM28 antibody inhibits the onset of subsequent DNA synthesis as tested by the incorporation of bromodeoxyuridine. Microinjection during the S phase had no effect on DNA synthesis, but inhibits cell division. The data suggest that the nuclear protein BM28 is required for two events of the cell cycle, for the onset of DNA replication and for cell division.

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26

Ferreira, Sofia, Ana F. Raimundo, Inês Farrim, and Regina Menezes. "Ablation of Kex2 activity enhances proIAPP proteotoxicity in yeast." Journal Biomedical and Biopharmaceutical Research 19, no. 2 (2022): 337–54. http://dx.doi.org/10.19277/bbr.19.2.301.

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Pancreatic deposition of Islet Amyloid PolyPeptide (IAPP) is a histopathological hallmark of type 2 diabetes. Inadequate processing of immature IAPP by proprotein convertases (PCs) leads to the accumulation of unprocessed forms, which in turn favors increased aggregate formation in pancreatic β-cells. Kexin 2 (Kex2) of Saccharomyces cerevisiae is the prototype of eukaryotic PCs family, but to date no direct correlations between Kex2 activity and preproIAPP processing in yeast have been reported. In this study we aimed to address the possible role of Kex2 on IAPP maturation as a tool to investigate the contribution of impaired processing towards IAPP proteototoxicity. Genetically modified S. cerevisiae models lacking the KEX2 gene and carrying different chimeric fusions of human IAPP linked to GFP were used. The cytotoxic effects of Kex2 ablation were assessed by means of growth curve analysis and cell viability assays using flow cytometry. IAPP protein profile was evaluated by immunoblotting assays using an anti-IAPP antibody. Intracellular IAPP aggregates were monitored by confocal fluorescence microscopy. Data showed that kex2 mutants exhibit growth defects, potentiated by preproIAPP-GFP, proIAPP-GFP and mature IAPP-GFP expression with an increased cytotoxicity for proIAPP-GFP. Notwithstanding, Kex2 absence does not seem to affect IAPP protein pattern nor the frequency/distribution of intracellular IAPP aggregates in yeast. Our findings suggest that Kex2 is not essential for IAPP processing in yeast, at least under the conditions tested. Keywords: Amylin, Islet Amyloid Polypeptide (IAPP), Kexin 2, Prohormone processing, Saccharomyces cerevisiae

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27

Kim, You Sun, Beom Jin Kim, Young-Ho Kim, Won Ho Kim, Joo Sung Kim, Young-Sook Park, Suk-Kyun Yang, et al. "T1284 Anti-Saccharomyces Cerevisiae Antibody (ASCA) is a Useful Diagnostic Tool to Differentiate Crohn's Disease From Intestinal Tuberculosis." Gastroenterology 138, no. 5 (May 2010): S—528. http://dx.doi.org/10.1016/s0016-5085(10)62438-9.

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28

Kim, Y. S., Y. H. Kim, B. D. Ye, J. W. Kim, and D. S. Han. "P195 Mannose-binding lectin deficiency is not associated with anti-Saccharomyces cerevisiae antibody in Korean Crohn's disease patients." Journal of Crohn's and Colitis 7 (February 2013): S87. http://dx.doi.org/10.1016/s1873-9946(13)60217-2.

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29

Zhou, Guangxi, Yang Song, Wenjing Yang, Yanmin Guo, Leilei Fang, Yamei Chen, and Zhanju Liu. "ASCA, ANCA, ALCA and Many More: Are They Useful in the Diagnosis of Inflammatory Bowel Disease?" Digestive Diseases 34, no. 1-2 (2016): 90–97. http://dx.doi.org/10.1159/000442934.

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Background: Inflammatory bowel disease (IBD) is characterized by excessive immune responses to altered intestinal microbiota in genetically susceptible individuals. The diagnosis of IBD depends on clinical, endoscopic, histological, radiological and biochemical criteria, which may be invasive, time consuming and usually not accepted by patients with IBD. Key Messages: Serological biomarkers have been demonstrated to be a series of rapid, non-invasive approaches for assessments of early diagnosis, disease activity and prognosis for IBD. Importantly, serum antibodies against microbial antigens or auto-antigens have been used as biomarkers in predicting disease course, complications and responses to medications and surgery. Moreover, they have been demonstrated to be useful in distinguishing patients with Crohn's disease (CD) from those with ulcerative colitis (UC). Recently, a great number of new serum biomarkers (e.g., anti-glycoprotein 2, anti-granulocyte macrophage colony-stimulating factor, anti-neutrophil cytoplasmic antibody, anti-Saccharomyces cerevisiae antibody, anti-laminaribioside carbohydrate IgG antibody, anti-mannobioside carbohydrate IgG antibody, antibody to the outer membrane protein of Escherichia coli, anti-CBir1) have been found to be present in patients with IBD and are potentially used in the diagnosis and prediction. The presence of these antibodies in the sera is due to the disruption of intestinal mucosa barrier and they may reflect a possibly genetic loss of immunological tolerance toward microbiota-derived antigens. Due to their non-invasive, easily accessible, repetitive and economical characteristics, these biomarkers have been found to serve as precious supplementary means in the diagnosis and disease evaluation of IBD. Conclusions: Currently, the most important utility of serological biomarkers is to evaluate the aggressive risks of disease phenotype, complications or surgery requirement, predict prognosis of the disease and distinguish CD from UC. However, they have limited values in making initially definite diagnosis for IBD. Therefore, more effective biomarkers with high sensitivity and specificity need to be further explored in the future.

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30

Benmerah, A., J. Gagnon, B. Bègue, B. Mégarbané, A. Dautry-Varsat, and N. Cerf-Bensussan. "The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2." Journal of Cell Biology 131, no. 6 (December 15, 1995): 1831–38. http://dx.doi.org/10.1083/jcb.131.6.1831.

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The ubiquitous eps15 protein was initially described as a substrate of the EGF receptor kinase. Its functions are not yet delineated and this work provides evidence for its possible role in endocytosis. A novel anti-eps15 antibody, 6G4, coimmunoprecipitated proteins of molecular mass 102 kD. In human cells, these proteins were identified as the alpha- and beta-adaptins of the AP-2 complex on the basis of their NH2-terminal sequence and their immunoreactivity with anti-alpha- and anti-beta-adaptin antibodies but not with anti-gamma-adaptin antibody. In addition, the anti-eps15 antibody coimmunoprecipitated metabolically labeled polypeptides with molecular mass of 50 and 17 kD, comparable to those of the two other components of the AP-2 complex, mu2 and sigma 2. Constitutive association of eps15 with AP-2 was confirmed by two sets of experiments. First, eps15 was detected in immunoprecipitates of anti-alpha- and anti-beta-adaptin antibodies. Second, alpha- and beta- but not gamma-adaptins were precipitated by a glutathione-S-transferase eps15 fusion protein. The association of eps15 with AP-2 was ubiquitous and conserved between species, since it was observed in human lymphocytes and epithelial cells and in murine NIH3T3 fibroblasts. Our results are in keeping with a recent study showing homology between the NH2-terminal domains of eps15 and the product of the gene END3, involved in clathrin-mediated endocytosis of the pheromone alpha factor in Saccharomyces cerevisiae, and suggest a possible role for eps15 in clathrin-mediated endocytosis in mammals.

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31

Sherwood, Roy A. "Faecal markers of gastrointestinal inflammation." Journal of Clinical Pathology 65, no. 11 (July 19, 2012): 981–85. http://dx.doi.org/10.1136/jclinpath-2012-200901.

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Gastrointestinal (GI) symptoms including abdominal pain, bloating and diarrhoea are a relatively common reason for consulting a physician. They may be due to inflammatory bowel disease (inflammatory bowel disease; Crohn's disease, ulcerative colitis and indeterminate colitis), malignancy (colorectal cancer), infectious colitis or irritable bowel syndrome (IBS). Differentiation between these involves the use of clinical, radiological, endoscopic and serological techniques, which are invasive or involve exposure to radiation. Serological markers include C-reactive protein, erythrocyte sedimentation rate and antibodies (perinuclear antineutrophil cytoplasm antibody and anti-Saccharomyces cerevisiae antibody). Faecal markers that can aid in distinguishing inflammatory disorders from non-inflammatory conditions are non-invasive and generally acceptable to the patient. As IBS accounts for up to 50% of cases presenting to the GI clinic and is a diagnosis of exclusion (Rome III criteria), any test that can reliably distinguish IBS from organic disease could speed diagnosis and reduce endoscopy waiting times. Faecal calprotectin, lactoferrin, M2-PK and S100A12 will be reviewed.

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32

Smith, Ben R. K., Ian D. R. Arnott, Hazel E. Drummond, Elaine R. Nimmo, and Jack Satsangi. "Disease Location, Anti-Saccharomyces cerevisiae Antibody, and NOD2/CARD15 Genotype Influence the Progression of Disease Behavior in Crohn’s Disease." Inflammatory Bowel Diseases 10, no. 5 (September 2004): 521–28. http://dx.doi.org/10.1097/00054725-200409000-00005.

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33

Cao, Liang, Che-man Chan, Cindy Lee, Samson Sai-yin Wong, and Kwok-yung Yuen. "MP1 Encodes an Abundant and Highly Antigenic Cell Wall Mannoprotein in the Pathogenic Fungus Penicillium marneffei." Infection and Immunity 66, no. 3 (March 1, 1998): 966–73. http://dx.doi.org/10.1128/iai.66.3.966-973.1998.

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ABSTRACT We cloned the MP1 gene, which encodes an abundant antigenic cell wall mannoprotein from the dimorphic pathogenic fungusPenicillium marneffei. MP1 is a unique gene without homologs in sequence databases. It codes for a protein, Mp1p, of 462 amino acid residues, with a few sequence features that are present in several cell wall proteins of Saccharomyces cerevisiae andCandida albicans. It contains two putative N glycosylation sites, a serine- and threonine-rich region for O glycosylation, a signal peptide, and a putative glycosylphosphatidylinositol attachment signal sequence. Specific anti-Mp1p antibody was generated with recombinant Mp1p protein purified from Escherichia coli to allow further characterization of Mp1p. Western blot analysis with anti-Mp1p antibody revealed that Mp1p has predominant bands with molecular masses of 58 and 90 kDa and that it belongs to a group of cell wall proteins that can be readily removed from yeast cell surfaces by glucanase digestion. In addition, Mp1p is an abundant yeast glycoprotein and has high affinity for concanavalin A, a characteristic indicative of a mannoprotein. Furthermore, ultrastructural analysis with immunogold staining indicated that Mp1p is present in the cell walls of the yeast, hyphae, and conidia of P. marneffei. Finally, it was observed that infected patients develop a specific antibody response against Mp1p, suggesting that this protein represents a good cell surface target for host humoral immunity.

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34

Yorulmaz, Elif, Gupse Adalı, Hatice Yorulmaz, Güralp Taşan, Seval Gürses, Mehmet Ramazan Ayaş, and İlyas Tuncer. "The Correlation between New Serological Markers and Disease Phenotype and Activation in Inflammatory Bowel Disease." Middle East Journal of Digestive Diseases 14, no. 3 (July 30, 2022): 294–303. http://dx.doi.org/10.34172/mejdd.2022.286.

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Background: The aim of the study is to assess the correlation between a new antibody panel that is developed against glycans on Crohn’s disease (CD) and ulcerative colitis (UC) differentiative diagnosis and disease properties. Methods: In the study, 137 CD and 122 UC patients and 90 controls were included. Anti-saccharomyces cerevisiae IgG (ASCA), anti-laminaribioside IgG (ALCA), anti-chitobioside IgA (ACCA), and anti-mannobioside IgG (AMCA) were tested in serum. Results: While at least 1 of the other 3 serological markers was positive in 89% of ASCA-positive patients, at least 1 of the other 3 serological markers was positive in 77% of ASCA-negative patients. Positivity ratio for a single anticarbohydrate was ALCA 18 (22%), ACCA 5 (12%), and AMCA 16 (23%). A significant correlation was found between ASCA positivity (P<0.001) in operated patients and between ASCA, ALCA, and ACCA positivity (P<0.05) in patients with stricturing and fistulizing CD. According to the ROC analysis, ASCA was found to have the highest area under the curve (0.70-0.82) (correlation coefficient interval 95%). A significant correlation was found between ASCA, ALCA, and ACCA positivity and high serum antibody levels and disease activation (P<0.05). Conclusion: ASCA, ALCA, and ACCA were found to be correlated with the disease complication and activation in CD. ASCA and ALCA were determined as the best markers in the differentiation between CD and UC.

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35

Lu, C. F., R. C. Montijn, J. L. Brown, F. Klis, J. Kurjan, H. Bussey, and P. N. Lipke. "Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall." Journal of Cell Biology 128, no. 3 (February 1, 1995): 333–40. http://dx.doi.org/10.1083/jcb.128.3.333.

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The cell adhesion protein alpha-agglutinin is bound to the outer surface of the Saccharomyces cerevisiae cell wall and mediates cell-cell contact in mating. alpha-Agglutinin is modified by addition of a glycosyl phosphatidylinositol (GPI) anchor as it traverses the secretory pathway. The presence of a GPI anchor is essential for cross-linking into the wall, but the fatty acid and inositol components of the anchor are lost before cell wall association (Lu, C.-F., J. Kurjan, and P. N. Lipke, 1994. A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin. Mol. Cell. Biol. 14:4825-4833). Cell wall association of alpha-agglutinin was accompanied by an increase in size and a gain in reactivity to antibodies directed against beta 1,6-glucan. Several kre mutants, which have defects in synthesis of cell wall beta 1,6-glucan, had reduced molecular size of cell wall alpha-agglutinin. These findings demonstrate that the cell wall form of alpha-agglutinin is covalently associated with beta 1,6-glucan. The alpha-agglutinin biosynthetic precursors did not react with antibody to beta 1,6-glucan, and the sizes of these forms were unaffected in kre mutants. A COOH-terminal truncated form of alpha-agglutinin, which is not GPI anchored and is secreted into the medium, did not react with the anti-beta 1,6-glucan. We propose that extracellular cross-linkage to beta 1,6-glucan mediates covalent association of alpha-agglutinin with the cell wall in a manner that is dependent on prior addition of a GPI anchor to alpha-agglutinin.

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Grabińska, Kariona A., Paula Magnelli, and Phillips W. Robbins. "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length." Eukaryotic Cell 6, no. 2 (December 1, 2006): 328–36. http://dx.doi.org/10.1128/ec.00203-06.

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ABSTRACT Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is recognized by anti-farnesyl antibody and is a substrate for farnesyl transferase (FTase) in vitro and that inactivation of FTase increases the amount of unmodified Chs4p in yeast cells. We demonstrate that abolition of Chs4p prenylation causes a ∼60% decrease in CSIII activity, which is correlated with a ∼30% decrease in chitin content and with increased resistance to the chitin binding compound calcofluor white. Furthermore, we show that lack of Chs4p prenylation decreases the average chain length of the chitin polymer. Prenylation of Chs4p, however, is not a factor that mediates plasma membrane association of the protein. Our results provide evidence that the prenyl moiety attached to Chs4p is a factor modulating the activity of CSIII both in vivo and in vitro.

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Gross, Sascha, Sjoerd F. Bakker, Adriaan A. Van Bodegraven, Ingrid M. W. Van Hoogstraten, Kyra A. Gelderman, Gerd Bouma, Chris J. Mulder, B. Mary E. Von Blomberg, and Hetty J. Bontkes. "Increased IgA Glycoprotein-2 Specic Antibody Titres in Refractory Celiac Disease." Journal of Gastrointestinal and Liver Diseases 23, no. 2 (June 1, 2014): 127–33. http://dx.doi.org/10.15403/jgld.2014.1121.232.sg1.

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Background & Aims: In most cases celiac disease (CD) is successfully treated with a gluten-free diet (GFD). However, some patients become refractory to the GFD. Refractory CD (RCD) patients have an increased risk for developing enteropathy associated T-cell lymphoma and early diagnosis is therefore of importance. Currently, RCD diagnosis relies on endoscopy and adequate serological markers are lacking. Antibodies against glycoprotein-2 (GP2A) were described in Crohn's disease (CrD) and active CD but not in ulcerative colitis (UC), suggesting this is a specific marker for small intestinal lesions.Methods: Sera obtained from patients visiting our outpatient clinic for routine serological tests for diagnosis and/or follow-up of inflammatory bowel disease (n=78), active CD (n=45), GFD (n=34) and RCD (n=15) were analysed for GP2A titres.Results: Increased GP2A-IgA levels in CrD and active CD as compared to controls (p<0.001) and lack thereof in UC was confirmed. However, we could not confirm the association with small bowel localization within the CrD patient group. Within CD patients, we demonstrated a significant decrease of GP2A-IgA titres upon a GFD and increased levels in RCD patients as compared to patients on a GFD. Although GP2A-IgA was not associated with the degree of villous atrophy, GP2A-IgA levels were able to distinguish RCD patients from GFD patients (ROC AUC=0.79, p=0.002).Conclusion: Follow-up of GP2A-IgA titres in CD patients on a GFD may help to identify patients at risk for developing RCD.Abbreviations: ABSA: anti-bovine serum albumine; ASCA: anti- Saccharomyces cerevisiae antigen; AU:artificial units; AUC: area under the curve; CD: celiac disease; CrD: Crohn's disease; EATL: enteropathyassociated T-cell lymphoma; EmA: anti-endomysium antibodies; GFD: gluten free diet; GP2A: glycoprotein 2 antibodies; IEL: intraepithelial lymphocytes; RCD: refractory celiac disease; ROC: receiver operator curve; TG2A: transglutaminase-2 antibodies; UC: ulcerative colitis.

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Kurokawa, Tomoyo, Chunyeon Lee, Naofumi Shiomi, Atsushi Nakano, and Shigeo Katoh. "Secretion of α-Amylase from Saccharomyces cerevisiae and Pichia pastoris and Characterization of Its C-Terminus with an Anti-Peptide Antibody." JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 35, no. 12 (2002): 1277–81. http://dx.doi.org/10.1252/jcej.35.1277.

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Yang, Huiying, Kent D. Taylor, Ying-Chao Lin, Stephan R. Targan, and Jerome I. Rotter. "Magnitude of anti-saccharomyces cerevisiae antibody (ASCA) expression is linked, in crohn's disease, families to the major histocompatibility complex (MHC) region." Gastroenterology 118, no. 4 (April 2000): A339. http://dx.doi.org/10.1016/s0016-5085(00)83453-8.

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Taylor, KD, Z. Li, M. Barry, N. Fischel-Ghodsian, SE Plevy, JI Rotter, SR Targan, and H. Yang. "Tumor necrosis factor microsatellite haplotype A11B4C1D3E3 is associated with anti-Saccharomyces cerevisiae antibody (ASCA) across clinical forms of inflammatory bowel disease." Gastroenterology 114 (April 1998): A1098. http://dx.doi.org/10.1016/s0016-5085(98)84463-6.

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Vasseur, Francis, Boualem Sendid, Thierry Jouault, Annie Standaert-Vitse, Laurent Dubuquoy, Nadine Francois, Corinne Gower-Rousseau, et al. "Variants of NOD1 and NOD2 genes display opposite associations with familial risk of crohnʼs disease and anti-saccharomyces cerevisiae antibody levels." Inflammatory Bowel Diseases 18, no. 3 (March 2012): 430–38. http://dx.doi.org/10.1002/ibd.21817.

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Chen, Qingquan, Shirong Huang, Yue Wu, Shuyu Zhang, Qicai Liu, and Min Chen. "Age and Gender: Affecting the Positive Rates of Serum PAB and ANCA in Patients with Inflammatory Bowel Disease." Gastroenterology Research and Practice 2021 (August 4, 2021): 1–6. http://dx.doi.org/10.1155/2021/4963641.

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Inflammatory bowel disease (IBD) is a group of immune-mediated conditions. Immune activity is varied by age and gender. The present study is aimed at investigating the effect of age and gender on the positive rates of anti-Saccharomyces cerevisiae antibodies (ASCA), anti-neutrophil cytoplasmic antibodies (ANCA), anti-intestinal goblet cell antibodies (GAB), and antibodies to exocrine pancreas (PAB) in IBD patients. A total of 1871 hospitalized patients with confirmed IBD were included in this study. Sera were obtained from each subject for antibody measurement by indirect immunofluorescence assay. The positive rates of ANCA IgG and IgA were higher in female patients than those in male patients ( P < 0.001 ) while the positive rate of PAB IgG was just reversed ( P < 0.001 ). Moreover, the median ages of patients with positive ANCA IgG and IgA were higher than patients with negative antibodies ( P = 0.0019 and P = 0.0110 , respectively), while the median ages of patients with positive PAB IgG and IgA were significantly lower than patients with negative PAB ( P < 0.0001 ). The serum levels of ANCA IgG and IgA were potentiated in old female patients, while serum PAB IgG was easy to be detected in the young male patients with IBD.

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Kaila, Brinderjit, Kenneth Orr, and Charles N. Bernstein. "The Anti-Saccharomyces Cerevisiae Antibody Assay in a Province-Wide Practice: Accurate in Identifying Cases of Crohn’s Disease and Predicting Inflammatory Disease." Canadian Journal of Gastroenterology 19, no. 12 (2005): 717–21. http://dx.doi.org/10.1155/2005/147681.

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OBJECTIVE: To determine the utility of the anti-Saccharomyces cerevisiae antibody (ASCA) ELISA test developed in Manitoba in 2001 in a population-wide sample referred from physicians across Manitoba in their investigation of patients with gastrointestinal symptoms.METHODS: Patients whose serum was referred for ASCA testing in 2001 and 2002 were eligible for the present study. ELISA was performed by a technologist, blind to patient diagnoses. A single investigator contacted physicians to facilitate chart review. Data collected included demographics, final diagnoses and tests used to substantiate the final diagnosis.RESULTS: Of 482 subjects identified, 410 charts were available for review and 29 of those were unavailable for follow-up or had incomplete charts. The present study population included Crohn's disease (CD, n=114), ulcerative colitis (n=74), indeterminate colitis (n=31), celiac disease (n=9), irritable bowel syndrome (n=75), other diagnoses (n=33) and no disease (n=45). ASCA had a sensitivity of 37% (95% CI 27.8 to 46.8) and specificity of 97% (95% CI 93.8 to 98.6) for diagnosing CD and an odds ratio for a diagnosis of CD of 18.4 (95% CI 8.2 to 41.3). The 47 ASCA-positive patients included the following diagnoses: CD=39, ulcerative colitis=3, indeterminate colitis=1, celiac disease=3 and no disease=1. The likelihood of having an inflammatory disease if ASCA is positive was nearly 40-fold.CONCLUSION: A positive ASCA test using this assay nearly clinches a diagnosis of some form of inflammatory intestinal disease, which is highly likely to be CD. In symptomatic patients, a positive ASCA test should encourage the clinician to pursue further investigations

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Kim, B. C., S. Park, J. Han, J. H. Kim, T. I. Kim, and W. H. Kim. "Clinical significance of anti-Saccharomyces cerevisiae antibody (ASCA) in Korean patients with Crohn's disease and its relationship to the disease clinical course." Digestive and Liver Disease 39, no. 7 (July 2007): 610–16. http://dx.doi.org/10.1016/j.dld.2007.03.006.

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Levendoglu, Hulya. "Idiopathic Ulcerations of the Esophagus (IUE) in HIV Infection with Positive Anti-Saccharomyces Cerevisiae Antibody (ASCA); Coincidence or Causation, a Case Report." American Journal of Gastroenterology 101 (September 2006): S325. http://dx.doi.org/10.14309/00000434-200609001-00807.

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Kim, You Sun, Young-Ho Kim, Won Ho Kim, Joo Sung Kim, Young Sook Park, Suk-Kyun Yang, Byong Duk Ye, et al. "Diagnostic utility of anti-Saccharomyces cerevisiae antibody (ASCA) and Interferon-γ assay in the differential diagnosis of Crohn's disease and intestinal tuberculosis." Clinica Chimica Acta 412, no. 17-18 (August 2011): 1527–32. http://dx.doi.org/10.1016/j.cca.2011.04.029.

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Vojdani, Aristo. "Elevated IgG Antibody to Aluminum Bound to Human Serum Albumin in Patients with Crohn’s, Celiac and Alzheimer’s Disease." Toxics 9, no. 9 (September 4, 2021): 212. http://dx.doi.org/10.3390/toxics9090212.

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Aluminum is in our water and food, and is used as an adjuvant in vaccines. About 40% of the ingested dose accumulates within the intestinal mucosa, making the gut the main target of inflammation and autoimmunity; about 1% accumulates in the skeletal system and brain, inducing the cross-linking of amyloid-β-42 peptide and the formation of amyloid aggregates associated with Alzheimer’s disease. To examine whether the accumulation of aluminum in the gut and brain tissues results in neoantigen formation, we bound aluminum compounds to human serum albumin. We used ELISA to measure IgG antibody in 94 different sera from healthy controls and 47 sera from each group of patients: anti-Saccharomyces cerevisiae antibody-positive (Crohn’s), and positive for deamidated α-gliadin and transglutaminase-2 IgA antibodies (celiac disease), autoimmune disorders associated with intestinal tissue antigens. Because earlier studies have shown that aluminum exposure is linked to Alzheimer’s disease etiology, and high aluminum content is detected in Alzheimer’s patients’ brain tissue, we also measured aluminum antibody in the blood of these patients. Additionally, we measured aluminum antibody in the sera of mixed connective tissue disease patients who were positive for antinuclear antibodies, and used them as disease controls. We found significant IgG antibody elevation against all three aluminum compounds in the sera of patients with Crohn’s, celiac and Alzheimer’s disease, but not in patients with mixed connective tissue disease. We concluded that aluminum ingestion and absorption from the GI tract and brain may contribute to Crohn’s, celiac and Alzheimer’s disease, but not to mixed connective tissue disease.

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Gencheva, Marieta, Mitsuo Kato, Alain N. S. Newo, and Ren-Jang Lin. "Contribution of DEAH-box protein DHX16 in human pre-mRNA splicing." Biochemical Journal 429, no. 1 (June 14, 2010): 25–32. http://dx.doi.org/10.1042/bj20100266.

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Studies of mammalian splicing factors are often focused on small nuclear ribonucleoproteins or regulatory RNA-binding proteins, such as hnRNP (heterogeneous nuclear ribonucleoprotein) and SR proteins (serine/arginine-rich proteins); however, much less is known about the contribution of DExD/H-box proteins or RNA helicases in mammalian pre-mRNA splicing. The human DEAH-box protein DHX16 [also known as DBP2 (DEAD-box protein 2)], is homologous with Caenorhabditis elegans Mog-4, Schizosaccharomyces pombe Prp8 and Saccharomyces cerevisiae Prp2. In the present study, we show that DHX16 is required for pre-mRNA splicing after the formation of a pre-catalytic spliceosome. We found that anti-DHX16 antiserum inhibited the splicing reaction in vitro and the antibody immunoprecipitated pre-mRNA, splicing intermediates and spliceosomal small nuclear RNAs. Cells that expressed DHX16 that had a mutation in the helicase domain accumulated unspliced intron-containing minigene transcripts. Nuclear extracts isolated from the dominant-negative DHX16-G724N-expressing cells formed splicing complex B, but were impaired in splicing. Adding extracts containing DHX16-G724N or DHX16-S552L mutant proteins to HeLa cell nuclear extracts resulted in reduced splicing, indicating that the mutant protein directly inhibited splicing in vitro. Therefore our results show that DHX16 is needed for human pre-mRNA splicing at a step analogous to that mediated by the S. cerevisiae spliceosomal ATPase Prp2.

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Dowhanick, T. M., S. W. Scherer, G. Willick, I. Russell, G. G. Stewart, and V. L. Seligy. "Differential glucoamylase expression in Schwanniomyces castellii induced by maltose." Canadian Journal of Microbiology 34, no. 3 (March 1, 1988): 262–70. http://dx.doi.org/10.1139/m88-048.

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Different levels of glucoamylase expression occurred when Schwanniomyces castellii strain 1402 was shifted during growth on glucose to either glucose, maltose, or soluble starch medium. Extracellular glucoamylase activity was greatest from cells grown on maltose (~22×), slightly less on soluble starch (~16×), and least on glucose (1×). Glucoamylase biosynthesis was further studied by labelling of total proteins in vivo with [35S]methionine and immunoprobing with a polyclonal anti-glucoamylase antibody. Mature active glucoamylase is 146 kDa. Maltose cultures expressed four cellular (75, 78,138, and 146 kDa) and two extracellular (78 and 146 kDa) polypeptides. Neither the 138- nor the 146-kDa products were detected in cells in the presence of glucose; the 78-kDa product is expressed at approximately 5% the level obtained from cells in maltose. The 146-kDa glucoamylase is expressed within 30 min after transfer of cells from glucose- to maltose-containing medium. This expression appears to be cell growth and concentration independent and is therefore similar to galactose-inducible enzyme expression in Saccharomyces cerevisiae.

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Sendid, Boualem, Nicolas Salvetat, Helène Sarter, Severine Loridant, Catherine Cunisse, Nadine François, Rachid Aijjou, et al. "A Pilot Clinical Study on Post-Operative Recurrence Provides Biological Clues for a Role of Candida Yeasts and Fluconazole in Crohn’s Disease." Journal of Fungi 7, no. 5 (April 22, 2021): 324. http://dx.doi.org/10.3390/jof7050324.

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Background and aims: This study prompted by growing evidence of the relationship between the yeast Candida albicans and Crohn’s disease (CD) was intended to assess the effect of a 6-month course of the antifungal fluconazole (FCZ) on post-operative recurrence of CD. Methods: Mycological samples (mouth swabs and stools) and serum samples were collected from 28 CD patients randomized to receive either FCZ (n = 14) or placebo (n = 14) before surgical resection. Serological analysis focused on levels of calprotectin, anti-glycan antibodies, and antibody markers of C. albicans pathogenic transition. Levels of galectin-3 and mannose binding lectin (MBL) involved in C. albicans sensing and inflammation were also measured. Results: 1, 2, 3, and 6 months after surgery, endoscopy revealed recurrence in 5/12 (41.7%) patients in the FCZ group and 5/9 (55.6%) in the placebo group, the small cohort preventing any clinical conclusions. In both groups, surgery was followed by a marked decrease in C. albicans colonization and biomarkers of C. albicans pathogenic transition decreased to non-significant levels. Anti-glycan antibodies also decreased but remained significant for CD. Galectin-3 and calprotectin also decreased. Conversely, MBL levels, which inversely correlated with anti-C. albicans antibodies before surgery, remained stable. Building biostatistical multivariate models to analyze he changes in antibody and lectin levels revealed a significant relationship between C. albicans and CD. Conclusion: Several combinations of biomarkers of adaptive and innate immunity targeting C. albicans were predictive of CD recurrence after surgery, with area under the curves (AUCs) as high as 0.86. FCZ had a positive effect on biomarkers evolution. ClinicalTrials.gov ID: NCT02997059, 19 December 2016. University Hospital Lille, Ministry of Health, France. Effect of Fluconazole on the Levels of Anti-Saccharomyces cerevisiae Antibodies (ASCA) After Surgical Resection for Crohn’s Disease. Multicenter, Randomized, and Controlled in Two Parallel Groups Versus Placebo.

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