Synthetic Peptides

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S Muller - One of the best experts on this subject based on the ideXlab platform.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    The reactivity of autoantibodies present in the sera of 489 patients with Sjogren's syndrome (SS), systemic lupus erythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinant 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, five were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2-11, 107-122, 107-126, 277-292 and 365-382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2-11 and 365-382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365-382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11, 107-122, 277-292 and 365-382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    SUMMARY The reactivity of autoantibodies present in the sera of 489 palicnts with Sjogren's syndrome (SS), systemic lupus crythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinani 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, live were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2 11, 107 122, 107 126, 277 292 and 365 382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2 11 and 365 382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365 382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11. 107 122, 277 292 and 365 382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

V Ricchiuti - One of the best experts on this subject based on the ideXlab platform.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    The reactivity of autoantibodies present in the sera of 489 patients with Sjogren's syndrome (SS), systemic lupus erythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinant 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, five were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2-11, 107-122, 107-126, 277-292 and 365-382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2-11 and 365-382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365-382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11, 107-122, 277-292 and 365-382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    SUMMARY The reactivity of autoantibodies present in the sera of 489 palicnts with Sjogren's syndrome (SS), systemic lupus crythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinani 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, live were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2 11, 107 122, 107 126, 277 292 and 365 382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2 11 and 365 382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365 382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11. 107 122, 277 292 and 365 382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

Amy P N Skubitz - One of the best experts on this subject based on the ideXlab platform.

  • abstract a06 Synthetic Peptides derived from the cell adhesion molecule nectin 4 inhibit the formation of ovarian cancer 3d spheroids
    Clinical Cancer Research, 2020
    Co-Authors: Kristin L M Boylan, Rory D Manion, Heena Shah, Amy P N Skubitz
    Abstract:

    A unique aspect of ovarian cancer progression is the collection of ascites fluid in the abdominal cavity, which contains free-floating tumor cells in the form of single cells and also multicellular aggregates or spheroids. Spheroids are more resistant to standard chemotherapy due in part to their slow proliferation rate and also to the protection afforded by the tight cell aggregation. Agents that prevent spheroid formation have the potential to improve chemotherapeutic response. Our previous work on the function of the cell surface adhesion molecule Nectin-4 in ovarian cancer demonstrates that it plays a key role in the formation of ovarian cancer spheroids. We also showed that Synthetic Peptides derived from the amino acid sequences of Nectin-4 and its binding partner Nectin-1 could inhibit cell adhesion in an in vitro assay. The purpose of this study was to further examine the role of Nectin-4 in the formation of ovarian cancer spheroids using live-cell digital microscopy to monitor spheroid formation over time. Synthetic Peptides derived from the amino acid sequences of Nectin-4 and Nectin-1 were tested for their ability to alter the spheroid formation of two ovarian cancer cell lines. Several Peptides disrupted ovarian cancer spheroid formation, warranting further investigation. For the peptide with the strongest inhibitory effect on spheroid formation, we tested scrambled versions of the peptide, which did not affect the formation of spheroids. This peptide also inhibited spheroid formation in a concentration-dependent manner and was not cytotoxic. These results suggest that Nectin-derived Peptides could augment the effect of chemotherapy, as they would maintain the cancer cells as single cells or small aggregates that are more sensitive to chemotherapy. Citation Format: Kristin L.M. Boylan, Rory D. Manion, Heena Shah, Amy P.N. Skubitz. Synthetic Peptides derived from the cell adhesion molecule Nectin-4 inhibit the formation of ovarian cancer 3D spheroids [abstract]. In: Proceedings of the AACR Special Conference on Advances in Ovarian Cancer Research; 2019 Sep 13-16, 2019; Atlanta, GA. Philadelphia (PA): AACR; Clin Cancer Res 2020;26(13_Suppl):Abstract nr A06.

  • inhibition of ovarian cancer cell spheroid formation by Synthetic Peptides derived from nectin 4
    International Journal of Molecular Sciences, 2020
    Co-Authors: Kristin L M Boylan, Rory D Manion, Heena Shah, Keith M Skubitz, Amy P N Skubitz
    Abstract:

    The formation of 3D multicellular spheroids in the ascites fluid of ovarian cancer patients is an understudied component of the disease progression. Spheroids are less sensitive to chemotherapy, in part due to the protection afforded by their structure, but also due to their slower proliferation rate. Previous studies suggest that the cell adhesion molecule Nectin-4 plays a key role in the formation of ovarian cancer spheroids. In this study, we further examined the role of Nectin-4 at early time points in spheroid formation using real-time digital photography. Human NIH:OVCAR5 ovarian cancer cells formed aggregates within 8 h, which further contracted into compact spheroids over 24 h. In contrast, Nectin-4 knockdown cells did not form tightly compacted spheroids. Synthetic Peptides derived from Nectin-4 were tested for their ability to alter spheroid formation in two ovarian cancer cell lines. Nectin-4 peptide 10 (N4-P10) had an immediate effect on disrupting ovarian cancer spheroid formation, which continued for over 24 h, while a scrambled version of the peptide had no effect. N4-P10 inhibited spheroid formation in a concentration-dependent manner and was not cytotoxic; suggesting that N4-P10 treatment could maintain the cancer cells as single cells which may be more sensitive to chemotherapy.

Olivier Meyer - One of the best experts on this subject based on the ideXlab platform.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    The reactivity of autoantibodies present in the sera of 489 patients with Sjogren's syndrome (SS), systemic lupus erythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinant 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, five were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2-11, 107-122, 107-126, 277-292 and 365-382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2-11 and 365-382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365-382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11, 107-122, 277-292 and 365-382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    SUMMARY The reactivity of autoantibodies present in the sera of 489 palicnts with Sjogren's syndrome (SS), systemic lupus crythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinani 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, live were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2 11, 107 122, 107 126, 277 292 and 365 382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2 11 and 365 382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365 382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11. 107 122, 277 292 and 365 382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

D A Isenberg - One of the best experts on this subject based on the ideXlab platform.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    The reactivity of autoantibodies present in the sera of 489 patients with Sjogren's syndrome (SS), systemic lupus erythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinant 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, five were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2-11, 107-122, 107-126, 277-292 and 365-382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2-11 and 365-382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365-382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11, 107-122, 277-292 and 365-382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.

  • epitope mapping with Synthetic Peptides of 52 kd ssa ro protein reveals heterogeneous antibody profiles in human autoimmune sera
    Clinical and Experimental Immunology, 2008
    Co-Authors: V Ricchiuti, Jeanpaul Briand, Olivier Meyer, D A Isenberg, G Pruijnj, S Muller
    Abstract:

    SUMMARY The reactivity of autoantibodies present in the sera of 489 palicnts with Sjogren's syndrome (SS), systemic lupus crythematosus (SLE) and other autoimmune diseases was investigated by ELISA using recombinani 52-kD SSA/Ro protein (rRo52) and 39 overlapping Synthetic Peptides representing the entire sequence of Ro52. We report that IgG antibodies reacting with rRo52 were present in the sera of a large number of patients with SS (67% of patients with primary SS and 46% of patients with SS associated with SLE), whereas they were less frequent (10-25%) in SLE, rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and mixed connective tissue disease (MCTD), and absent in scleroderma. Among the 39 Peptides tested, live were recognized by sera from 30-65% of patients with SS, namely Peptides representing residues 2 11, 107 122, 107 126, 277 292 and 365 382. Patients with JCA had raised levels of IgG antibodies reacting with Peptides 2 11 and 365 382, and 51% of patients with MCTD had raised levels of IgG antibodies reacting with peptide 365 382. None of the five Peptides was recognized by more than 20% of sera from patients with SLE and RA. Interestingly, and of importance in the field of diagnostic tests based on Peptides, the reactivity of antibodies to the Ro52 Synthetic Peptides varied greatly according to the origin of sera. Inhibition experiments using either patients' sera or antibodies induced in rabbits against Ro52 Peptides showed that the four domains 2-11. 107 122, 277 292 and 365 382 are accessible on the surface of the Ro52 protein. These regions may thus be involved in the induction of specific antibodies in autoimmune patients.