Anti-amyloidogenic property of human gastrokine (527 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 0300-9084linking), 2014 Nov; 106C: 91-100.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.963, 5-year impact factor: 3.124
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908005465&partnerID=40&md5=8f0ecc092b7da77c3db3ba71919b5454
Keywords: Amyloidogenesis, Aβ Peptide, Brichos Domain, Gastric Cancer, Gastrokine 1, Amyloid Beta Protein[1-40], Amyloid Precursor Protein, Chaperone, Cystatin, Nitrilotriacetate Nickel, Polypeptide, Recombinant Gastrokine 1, Recombinant Protein, Surfactant Protein C, Thioflavine, Unclassified Drug, Article, Binding Assay, Confocal Microscopy, Controlled Study, Drug Activity, Fiber, Human, Human Cell, Hydrolysis, Mass Spectrometry, Neuroblastoma Cell Line, Polyacrylamide Gel Electrophoresis, Polymerization, Protein Aggregation, Protein Binding, Protein Expression, Protein Protein Interaction, Protein Secondary Structure, Stomach Adenocarcinoma, Surface Plasmon Resonance, Z Peptide, Aß Peptide, A Peptide, Amyloid Beta Protein [1-40], Amino Acid Sequence , Amyloid Chemistry Metabolism , Amyloid Beta-Peptides Chemistry Metabolism , Amyloid Beta-Protein Precursor Metabolism , Tumor , Molecular Sequence Data , Peptide Fragments Chemistry Metabolism , Peptide Hormones Genetics Metabolism Pharmacology , Protein Aggregates Drug Effects , Recombinant Proteins Metabolism Pharmacology , Sequence Homology, Matrix-Assisted Laser Desorption-Ionization,
Affiliations:
*** IBB - CNR ***
Department of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Via S. Pansini 5Naples, Italy
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of NaplesCaserta, Italy
Institute of Biostructures and Bioimaging-IBB, CNRNaples, Italy
IRCCS MultimedicaMilan, Italy
Laboratory of Biotechnology, Department of Anesthesia, Surgical and Emergency Sciences, Second University of Naples, Via Costantinopoli 16Naples, Italy
Department of Motor Sciences and Wellness, University of ParthenopeNaples, Italy
CEINGE, Advanced Biotechnology Scarl, Via Gaetano Salvatore 486Naples, Italy
IRCCS Multimedica, Milan, Italy
References:
Martin, T.E., Powell, C.T., Wang, Z., Bhattacharyya, S., Walsh-Reitz, M.M., Agarwal, K., Toback, F.G., A novel mitogenic protein that is highly expressed in cells of the gastric antrum mucosa (2003) Am. J. Physiol. Gastrointest. Liver Physiol., 285 (2), pp. 332-G34
Nardone, G., Rippa, E., Martin, G., Rocco, A., Siciliano, R.A., Fiengo, A., Cacace, G., Arcari, P., Gastrokine 1 expression in patients with and without Helicobacter pylori infection (2007) Dig. Liver Dis., 39 (2), pp. 122-129
Nardone, G., Martin, G., Rocco, A., Rippa, E., La Monica, G., Caruso, F., Arcari, P., Molecular expression of gastrokine 1 in normal mucosa and in Helicobacter pylori-related preneoplastic and neoplastic lesions (2008) Cancer Biol. Ther., 7 (12), pp. 1890-1895
Moss, S.F., Lee, J.W., Sabo, E., Rubin, A.K., Rommel, J., Westley, B.R., May, F.E., Resnick, M.B., Decreased expression of gastrokine 1 and the trefoil factor interacting protein TFIZ1/GKN2 in gastric cancer: Influence of tumor histology and relationship to prognosis (2008) Clin. Cancer Res., 14 (13), pp. 4161-4167
Shiozaki, K., Nakamori, S., Tsujie, M., Okami, J., Yamamoto, H., Nagano, H., Dono, K., Monden, M., Human stomach-specific gene, CA11, is down-regulated in gastric cancer (2001) Int. J. Oncol., 19, pp. 701-707
Oien, K.A., McGregor, F., Butler, S., Ferrier, R.K., Downie, I., Bryce, S., Burns, S., Keith, W.N., Gastrokine 1 is abundantly and specifically expressed in superficial gastric epithelium, down-regulated in gastric carcinoma, and shows high evolutionary conservation (2004) J. Pathol., 203 (3), pp. 789-797
Sánchez-Pulido, L., Devos, D., Valencia, A., BRICHOS: A conserved domain in proteins associated with dementia, respiratory distress and cancer (2002) Trends Biochem. Sci., 27 (7), pp. 329-332
Pavone, L.M., Del Vecchio, P., Mallardo, P., Altieri, F., De Pasquale, V., Rea, S., Martucci, N.M., Rippa, E., Structural characterization and biological properties of human gastrokine 1 (2013) Mol. Biosyst., 9, pp. 412-421
Kallberg, Y., Gustaffson, M., Persson, B., Thyberg, J., Johansson, J., Prediction of amyloid fibril-forming proteins (2001) J. Biol. Chem., 276 (16), pp. 12945-12950
Warr, R.G., Hawgood, S., Buckley, D.I., Crisp, T.M., Schilling, J., Benson, B.J., Ballard, P.L., White, R.T., Low molecular weight human pulmonary surfactant protein (SP5): Isolation, characterization, and cDNA and amino acid sequences (1987) Proc. Natl. Acad. Sci. U S A, 84 (22), pp. 7915-7919
Willander, H., Askarieh, G., Landreh, M., Westermark, P., Nordling, K., Keränen, H., Hermansson, E., Johansson, J., High-resolution structure of a BRICHOS domain and ist implications for anti-amyloid chaperone activity on lung surfactant protein C (2012) Proc. Natl. Acad. Sci. U S A, 109 (7), pp. 2325-2329
Johansson, H., Nordling, K., Weaver, T.E., Johansson, J., The Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment (2006) J. Biol. Chem., 281, pp. 21032-21039
Nerelius, C., Martin, E., Peng, S., Gustafsson, M., Nordling, K., Weaver, T., Johansson, J., Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C (2008) Biochem. J., 416, pp. 201-209
Peng, S., Fitzen, M., Jörnvall, H., Johansson, J., The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-23) and amyloid β-peptide (Aβ1-40): Implications for Bri2 effects on processing of amyloid precursor protein and Aβ aggregation (2010) Biochem. Biophys. Res. Commun., 393, pp. 356-361
Willander, H., Hermansson, E., Johansson, J., Presto, J., BRICHOS domain associated with lung fibrosis, dementia and cancer - A chaperone that prevents amyloid fibril formation? (2011) FEBS J., 278 (20), pp. 3893-3904
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Nerelius, C., Gustafsson, M., Nordling, K., Larsson, A., Johansson, J., Anti-amyloid activity of the c-terminal domain of proSP-c against amyloid β-peptide and Medin (2009) Biochemistry, 48, pp. 3778-3786
Tamburino, R., Severino, V., Sandomenico, A., Ruvo, M., Parente, A., Chambery, A., De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. Seeds by electrospray mass spectrometry (2012) Mol. Biosyst., 8 (12), pp. 3232-3241
Farmer, T.B., Caprioli, R.M., Determination of protein-protein interactions by matrix-assisted laser desorption/ionization mass spectrometry (1998) J. Mass Spectrom., 33 (8), pp. 697-704
Johnsson, B., Lofas, S., Lindquist, G., Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors (1991) Anal. Biochem., 198, pp. 268-277
Hofmann, K., Stoffel, W., TMbase - A database of membrane spanning proteins segments (1993) Biol. Chem. Hoppe-Seyler, 374, p. 166
Selkoe, D., Kopan, R., Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration (2003) Annu. Rev. Neurosci., 26, pp. 565-597
Willander, H., Presto, J., Askarieh, G., Biverstål, H., Frohm, B., Knight, S.D., Johansson, J., Linse, S., BRICHOS domains efficiently delay fibrillation of amyloid β-peptide (2012) J. Biol. Chem., 287 (37), pp. 31608-31617
Wilhelmus, M.M., Boelens, W.C., Otte-Höller, I., Kamps, B., Kusters, B., Maat-Schieman, M.L., De Waal, R.M., Verbeek, M.M., Small heat shock protein HspB8: Its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity (2006) Acta Neuropathol., 111, pp. 139-149
Fitzen, M., Alvelius, G., Nordling, K., Jornvall, H., Bergman, T., Johansson, J., Peptide-binding specificity of the prosurfactant protein C Brichos domain analyzed by electrospray ionization mass spectrometry (2009) Rapid Commun. Mass Spectrom., 23, pp. 3591-3598
Knight, S.D., Presto, J., Linse, S., Johansson, J., The BRICHOS domain, amyloid fibril formation, and their relationship (2013) Biochemistry, 52, pp. 7523-7531
Porat, Y., Abramowitz, A., Gazit, E., Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism (2006) Chem. Biol. Drug. Des., 67, pp. 27-37
Fotinopoulou, A., Tsachaki, M., Vlavaki, M., Poulopoulos, A., Rostagno, A., Frangione, B., Ghiso, J., Efthimiopoulos, S., BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid β (Aβ) production (2005) J. Biol. Chem., 280 (35), pp. 30768-30772
Tsachaki, M., Fotinopoulou, A., Slavi, N., Zarkou, V., Ghiso, J., Efthimiopoulos, S., BRI2 interacts with BACE1 and regulates its cellular levels by promoting its degradation and reducing its mRNA levels (2013) Curr. Alzheimer Res., 10 (5), pp. 532-541
Matsuda, S., Matsuda, Y., D'Adamio, L., BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2 (2009) J. Biol. Chem., 284 (23), pp. 15815-15825
Eder, J., Fersht, A.R., Pro-sequence-assisted protein folding (1995) Mol. Microbiol., 16 (4), pp. 609-614
Biochimie (ISSN: 0300-9084, 1638-6183, 0300-9084linking), 2014 Nov; 106C: 91-100.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.963, 5-year impact factor: 3.124
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908005465&partnerID=40&md5=8f0ecc092b7da77c3db3ba71919b5454
Keywords: Amyloidogenesis, Aβ Peptide, Brichos Domain, Gastric Cancer, Gastrokine 1, Amyloid Beta Protein[1-40], Amyloid Precursor Protein, Chaperone, Cystatin, Nitrilotriacetate Nickel, Polypeptide, Recombinant Gastrokine 1, Recombinant Protein, Surfactant Protein C, Thioflavine, Unclassified Drug, Article, Binding Assay, Confocal Microscopy, Controlled Study, Drug Activity, Fiber, Human, Human Cell, Hydrolysis, Mass Spectrometry, Neuroblastoma Cell Line, Polyacrylamide Gel Electrophoresis, Polymerization, Protein Aggregation, Protein Binding, Protein Expression, Protein Protein Interaction, Protein Secondary Structure, Stomach Adenocarcinoma, Surface Plasmon Resonance, Z Peptide, Aß Peptide, A Peptide, Amyloid Beta Protein [1-40], Amino Acid Sequence , Amyloid Chemistry Metabolism , Amyloid Beta-Peptides Chemistry Metabolism , Amyloid Beta-Protein Precursor Metabolism , Tumor , Molecular Sequence Data , Peptide Fragments Chemistry Metabolism , Peptide Hormones Genetics Metabolism Pharmacology , Protein Aggregates Drug Effects , Recombinant Proteins Metabolism Pharmacology , Sequence Homology, Matrix-Assisted Laser Desorption-Ionization,
Affiliations:
*** IBB - CNR ***
Department of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Via S. Pansini 5Naples, Italy
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of NaplesCaserta, Italy
Institute of Biostructures and Bioimaging-IBB, CNRNaples, Italy
IRCCS MultimedicaMilan, Italy
Laboratory of Biotechnology, Department of Anesthesia, Surgical and Emergency Sciences, Second University of Naples, Via Costantinopoli 16Naples, Italy
Department of Motor Sciences and Wellness, University of ParthenopeNaples, Italy
CEINGE, Advanced Biotechnology Scarl, Via Gaetano Salvatore 486Naples, Italy
IRCCS Multimedica, Milan, Italy
References:
Martin, T.E., Powell, C.T., Wang, Z., Bhattacharyya, S., Walsh-Reitz, M.M., Agarwal, K., Toback, F.G., A novel mitogenic protein that is highly expressed in cells of the gastric antrum mucosa (2003) Am. J. Physiol. Gastrointest. Liver Physiol., 285 (2), pp. 332-G34
Nardone, G., Rippa, E., Martin, G., Rocco, A., Siciliano, R.A., Fiengo, A., Cacace, G., Arcari, P., Gastrokine 1 expression in patients with and without Helicobacter pylori infection (2007) Dig. Liver Dis., 39 (2), pp. 122-129
Nardone, G., Martin, G., Rocco, A., Rippa, E., La Monica, G., Caruso, F., Arcari, P., Molecular expression of gastrokine 1 in normal mucosa and in Helicobacter pylori-related preneoplastic and neoplastic lesions (2008) Cancer Biol. Ther., 7 (12), pp. 1890-1895
Moss, S.F., Lee, J.W., Sabo, E., Rubin, A.K., Rommel, J., Westley, B.R., May, F.E., Resnick, M.B., Decreased expression of gastrokine 1 and the trefoil factor interacting protein TFIZ1/GKN2 in gastric cancer: Influence of tumor histology and relationship to prognosis (2008) Clin. Cancer Res., 14 (13), pp. 4161-4167
Shiozaki, K., Nakamori, S., Tsujie, M., Okami, J., Yamamoto, H., Nagano, H., Dono, K., Monden, M., Human stomach-specific gene, CA11, is down-regulated in gastric cancer (2001) Int. J. Oncol., 19, pp. 701-707
Oien, K.A., McGregor, F., Butler, S., Ferrier, R.K., Downie, I., Bryce, S., Burns, S., Keith, W.N., Gastrokine 1 is abundantly and specifically expressed in superficial gastric epithelium, down-regulated in gastric carcinoma, and shows high evolutionary conservation (2004) J. Pathol., 203 (3), pp. 789-797
Sánchez-Pulido, L., Devos, D., Valencia, A., BRICHOS: A conserved domain in proteins associated with dementia, respiratory distress and cancer (2002) Trends Biochem. Sci., 27 (7), pp. 329-332
Pavone, L.M., Del Vecchio, P., Mallardo, P., Altieri, F., De Pasquale, V., Rea, S., Martucci, N.M., Rippa, E., Structural characterization and biological properties of human gastrokine 1 (2013) Mol. Biosyst., 9, pp. 412-421
Kallberg, Y., Gustaffson, M., Persson, B., Thyberg, J., Johansson, J., Prediction of amyloid fibril-forming proteins (2001) J. Biol. Chem., 276 (16), pp. 12945-12950
Warr, R.G., Hawgood, S., Buckley, D.I., Crisp, T.M., Schilling, J., Benson, B.J., Ballard, P.L., White, R.T., Low molecular weight human pulmonary surfactant protein (SP5): Isolation, characterization, and cDNA and amino acid sequences (1987) Proc. Natl. Acad. Sci. U S A, 84 (22), pp. 7915-7919
Willander, H., Askarieh, G., Landreh, M., Westermark, P., Nordling, K., Keränen, H., Hermansson, E., Johansson, J., High-resolution structure of a BRICHOS domain and ist implications for anti-amyloid chaperone activity on lung surfactant protein C (2012) Proc. Natl. Acad. Sci. U S A, 109 (7), pp. 2325-2329
Johansson, H., Nordling, K., Weaver, T.E., Johansson, J., The Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment (2006) J. Biol. Chem., 281, pp. 21032-21039
Nerelius, C., Martin, E., Peng, S., Gustafsson, M., Nordling, K., Weaver, T., Johansson, J., Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C (2008) Biochem. J., 416, pp. 201-209
Peng, S., Fitzen, M., Jörnvall, H., Johansson, J., The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-23) and amyloid β-peptide (Aβ1-40): Implications for Bri2 effects on processing of amyloid precursor protein and Aβ aggregation (2010) Biochem. Biophys. Res. Commun., 393, pp. 356-361
Willander, H., Hermansson, E., Johansson, J., Presto, J., BRICHOS domain associated with lung fibrosis, dementia and cancer - A chaperone that prevents amyloid fibril formation? (2011) FEBS J., 278 (20), pp. 3893-3904
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Nerelius, C., Gustafsson, M., Nordling, K., Larsson, A., Johansson, J., Anti-amyloid activity of the c-terminal domain of proSP-c against amyloid β-peptide and Medin (2009) Biochemistry, 48, pp. 3778-3786
Tamburino, R., Severino, V., Sandomenico, A., Ruvo, M., Parente, A., Chambery, A., De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. Seeds by electrospray mass spectrometry (2012) Mol. Biosyst., 8 (12), pp. 3232-3241
Farmer, T.B., Caprioli, R.M., Determination of protein-protein interactions by matrix-assisted laser desorption/ionization mass spectrometry (1998) J. Mass Spectrom., 33 (8), pp. 697-704
Johnsson, B., Lofas, S., Lindquist, G., Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors (1991) Anal. Biochem., 198, pp. 268-277
Hofmann, K., Stoffel, W., TMbase - A database of membrane spanning proteins segments (1993) Biol. Chem. Hoppe-Seyler, 374, p. 166
Selkoe, D., Kopan, R., Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration (2003) Annu. Rev. Neurosci., 26, pp. 565-597
Willander, H., Presto, J., Askarieh, G., Biverstål, H., Frohm, B., Knight, S.D., Johansson, J., Linse, S., BRICHOS domains efficiently delay fibrillation of amyloid β-peptide (2012) J. Biol. Chem., 287 (37), pp. 31608-31617
Wilhelmus, M.M., Boelens, W.C., Otte-Höller, I., Kamps, B., Kusters, B., Maat-Schieman, M.L., De Waal, R.M., Verbeek, M.M., Small heat shock protein HspB8: Its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity (2006) Acta Neuropathol., 111, pp. 139-149
Fitzen, M., Alvelius, G., Nordling, K., Jornvall, H., Bergman, T., Johansson, J., Peptide-binding specificity of the prosurfactant protein C Brichos domain analyzed by electrospray ionization mass spectrometry (2009) Rapid Commun. Mass Spectrom., 23, pp. 3591-3598
Knight, S.D., Presto, J., Linse, S., Johansson, J., The BRICHOS domain, amyloid fibril formation, and their relationship (2013) Biochemistry, 52, pp. 7523-7531
Porat, Y., Abramowitz, A., Gazit, E., Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism (2006) Chem. Biol. Drug. Des., 67, pp. 27-37
Fotinopoulou, A., Tsachaki, M., Vlavaki, M., Poulopoulos, A., Rostagno, A., Frangione, B., Ghiso, J., Efthimiopoulos, S., BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid β (Aβ) production (2005) J. Biol. Chem., 280 (35), pp. 30768-30772
Tsachaki, M., Fotinopoulou, A., Slavi, N., Zarkou, V., Ghiso, J., Efthimiopoulos, S., BRI2 interacts with BACE1 and regulates its cellular levels by promoting its degradation and reducing its mRNA levels (2013) Curr. Alzheimer Res., 10 (5), pp. 532-541
Matsuda, S., Matsuda, Y., D'Adamio, L., BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2 (2009) J. Biol. Chem., 284 (23), pp. 15815-15825
Eder, J., Fersht, A.R., Pro-sequence-assisted protein folding (1995) Mol. Microbiol., 16 (4), pp. 609-614
Anti-amyloidogenic property of human gastrokine
Gastrokine 1 (GKN1) is a stomach-specific protein expressed in normal gastric tissue but absent in gastric cancer. GKN1 plays a major role in maintaining gastric mucosa integrity and is characterized by the presence of a BRICHOS domain consisting of about 100 amino acids also found in several unrelated proteins associated with major human diseases like BRI2, related to familial British and Danish dementia and surfactant protein C (SP-C), associated with respiratory distress syndrome. It was reported that recombinant BRICHOS domains from BRI2 and SP-C precursor (proSP-C) prevent fibrils formation of amyloid-beta peptide (A beta), that is the major component of extracellular amyloid deposits in Alzheimer's disease. Here we investigated on the interaction between human recombinant GKN1 (rGKN1) and A beta peptide (1-40) that derives from the partial hydrolysis of the amyloid precursor protein (APP). GKN1 prevented amyloid aggregation and fibrils formation by inhibiting A beta (1-40) polymerization, as evaluated by SDS-PAGE, thioflavin-T binding assay and gel filtration experiments. Mass spectrometry showed the formation of a prevailing 1: 1 complex between GKN1 and A beta (1-40). SPR analysis of GKN1/A beta interaction led to calculate a dissociation constant (K-D) of 34 mu M. Besides its interaction with A beta (1-40), GKN1 showed also to interact with APP as evaluated by confocal microscopy and Ni-NTA pull-down. Data strongly suggest that GKN1 has anti-amyloidogenic properties thus functioning as a chaperone directed against unfolded segments and with the ability to recognize amyloidogenic polypeptides and prevent their aggregation. (C) 2014 Elsevier B. V. and Societe francaise de biochimie et biologie Moleculaire (SFBBM). All rights reserved
Gastrokine 1 (GKN1) is a stomach-specific protein expressed in normal gastric tissue but absent in gastric cancer. GKN1 plays a major role in maintaining gastric mucosa integrity and is characterized by the presence of a BRICHOS domain consisting of about 100 amino acids also found in several unrelated proteins associated with major human diseases like BRI2, related to familial British and Danish dementia and surfactant protein C (SP-C), associated with respiratory distress syndrome. It was reported that recombinant BRICHOS domains from BRI2 and SP-C precursor (proSP-C) prevent fibrils formation of amyloid-beta peptide (A beta), that is the major component of extracellular amyloid deposits in Alzheimer's disease. Here we investigated on the interaction between human recombinant GKN1 (rGKN1) and A beta peptide (1-40) that derives from the partial hydrolysis of the amyloid precursor protein (APP). GKN1 prevented amyloid aggregation and fibrils formation by inhibiting A beta (1-40) polymerization, as evaluated by SDS-PAGE, thioflavin-T binding assay and gel filtration experiments. Mass spectrometry showed the formation of a prevailing 1: 1 complex between GKN1 and A beta (1-40). SPR analysis of GKN1/A beta interaction led to calculate a dissociation constant (K-D) of 34 mu M. Besides its interaction with A beta (1-40), GKN1 showed also to interact with APP as evaluated by confocal microscopy and Ni-NTA pull-down. Data strongly suggest that GKN1 has anti-amyloidogenic properties thus functioning as a chaperone directed against unfolded segments and with the ability to recognize amyloidogenic polypeptides and prevent their aggregation. (C) 2014 Elsevier B. V. and Societe francaise de biochimie et biologie Moleculaire (SFBBM). All rights reserved
Anti-amyloidogenic property of human gastrokine
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Anti-amyloidogenic property of human gastrokine
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Impact Factor: 4.183
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Ribaldone DG, Fagoonee S, Astegiano M, Durazzo M, Morgando A, Sprujevnik T, Giordanino C, Baronio M, De Angelis C, Saracco GM, Pellicano R
* Rifabutin-Based Rescue Therapy for Helicobacter pylori Eradication: A Long-Term Prospective Study in a Large Cohort of Difficult-to-Treat Patients (259 views)
J Clin Med (ISSN: 2077-0383linking, 2077-0383electronic), 2019 Feb 6; 8(2): N/D-N/D.
Impact Factor: 5.583
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Pellicano R, Fagoonee S
* Helicobacter pylori and Prevention of Gastric Cancer (231 views)
N Engl J Med (ISSN: 0028-4793linking, 1533-4406electronic), 2018 Jun 7; 378(23): 2244-2244.
Impact Factor: 72.406
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Fagoonee S, Durazzo M
* HOTAIR and gastric cancer: a lesson from two meta-analyses (155 views)
Panminerva Med (ISSN: 0031-0808, 1827-1898electronic, 0031-0808linking), 2017 Sep; 59(3): 201-202.
Impact Factor: 2.102
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Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ
* Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer (297 views)
N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756.
Impact Factor: 59.558
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Pannuzzo M, Milardi D, Raudino A, Karttunen M, La Rosa C
* Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: Towards a unifying description of conformational transitions, oligomerization and membrane damage (728 views)
Phys Chem Chem Phys (ISSN: 1463-9076, 1463-3907, 1463-9084electronic), 2013; 15(23): 8940-8951.
Impact Factor: 4.198
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Esposito G, Tempesta A, Galati MG, De Bellis M, Rossi GB, Potena MI, Marone P, Daniele B, Del Vecchio S
Mucosal expression of carcinoembryonic antigen and carbohydrate antigen 19-9 in patients with gastritis and gastric cancer (320 views)
Cancer Detect Prev (ISSN: 0361-090x, 0361-090xlinking), 1999; 23(2): 116-122.
Impact Factor: 0.927
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7 Records (7 excluding Abstracts).
Total impact factor: 148.957 (148.957 excluding Abstracts).
Total 5 year impact factor: 122.327 (122.327 excluding Abstracts).
Total impact factor: 148.957 (148.957 excluding Abstracts).
Total 5 year impact factor: 122.327 (122.327 excluding Abstracts).
527 views. Last view on Saturday 28 January 2023, 4:17:21
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