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Qingyu Wu - One of the best experts on this subject based on the ideXlab platform.

  • effect of sialylated o glycans in pro brain natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

  • Effect of Sialylated O-Glycans in Pro–Brain Natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

Jingjing Jiang - One of the best experts on this subject based on the ideXlab platform.

  • effect of sialylated o glycans in pro brain natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

  • Effect of Sialylated O-Glycans in Pro–Brain Natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

Nicole Pristera - One of the best experts on this subject based on the ideXlab platform.

  • effect of sialylated o glycans in pro brain natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

  • Effect of Sialylated O-Glycans in Pro–Brain Natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

Xiumei Zhang - One of the best experts on this subject based on the ideXlab platform.

  • effect of sialylated o glycans in pro brain natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

  • Effect of Sialylated O-Glycans in Pro–Brain Natriuretic Peptide Stability
    Clinical Chemistry, 2010
    Co-Authors: Jingjing Jiang, Nicole Pristera, Wei Wang, Xiumei Zhang, Qingyu Wu
    Abstract:

    Background: Atrial, brain, and C-type natriuretic Peptides (ANP, BNP, and CNP) are important in regulating a variety of cardiovascular and cellular functions. In cells, these Peptides are made as proforms that are converted to mature forms. BNP and its related Peptides are biomarkers for the diagnosis of heart failure. In this study, we examined glycosylation in pro-ANP, pro-BNP, and pro-CNP, which may alter their biochemical and metabolic properties. Methods: Human pro-ANP, pro-BNP, and pro-CNP were expressed in HEK 293 cells and murine HL-1 cardiomyocytes and analyzed by immunoprecipitation and Western blotting. We used deglycosylation enzymes to determine the carbohydrate content on these Peptides and examined the effects of inhibiting O -glycosylation on cellular expression and Stability of the Peptides. Results: In HEK 293 and HL-1 cells, pro-BNP, but not pro-ANP and pro-CNP, from the culture medium had a greater molecular mass than that from cell lysate. Digestion with PNGase F, O -glycosidase, and sialidase A indicated that pro-BNP contained O -glycans but not N -glycans. The O -glycans on pro-BNP had sialic acids at their termini, protecting it from O -glycosidase digestion. In contrast, pro-ANP and pro-CNP contained no detectable amounts of N - or O -glycans. Inhibition of O -glycosylation on pro-BNP did not prevent its expression in the cells. However, partially O -glycosylated pro-BNP was much less stable than fully O - glycosylated pro-BNP. Conclusions: O -glycosylation is not necessary for pro-BNP expression but important for its Stability.

Eric G Pamer - One of the best experts on this subject based on the ideXlab platform.

  • mhc class i Peptide Stability implications for immunodominance in vitro proliferation and diversity of responding ctl
    Journal of Immunology, 1998
    Co-Authors: Dirk H Busch, Eric G Pamer
    Abstract:

    Infection of BALB/c mice with Listeria monocytogenes primes CD8 + cytotoxic T cells specific for four different H2-K d -restricted Peptides. In vitro restimulation of L. monocytogenes immune splenocytes with each of these Peptides resulted in larger T cell responses to p60 217–225 and mpl 84–92 than to LLO 91–99 and p60 449–457. Direct frequency analyses of immune splenocytes, however, revealed that LLO 91–99 and p60 217–225 elicit dominant T cell responses, while p60 449–457 and mpl 84–92 elicit minor, subdominant responses. Restimulation of immune splenocytes with a range of Peptide concentrations revealed that T cells with dominant specificities respond optimally to low Peptide concentrations, while T cells specific for subdominant epitopes expand maximally to high Peptide concentrations. This disparity correlates with the Stability of H2-K d /epitope complexes: the two dominant epitopes form stable complexes, while the subdominant epitopes form less stable complexes with H2-K d . Interestingly, T cells specific for LLO 91–99 and p60 217–225 express more complex TCR-Vβ repertoires than p60 449–457- and mpl 84–92-specific T cells. Thus, in our system, dominant T cell responses have relatively diverse TCR repertoires and are specific for Peptides that form stable complexes with MHC class I molecules. Determining the precise roles of epitope/MHC class I Stability and TCR repertoire in the generation of dominant T cell responses will require further investigation.