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Kenneth J Soprano - One of the best experts on this subject based on the ideXlab platform.

  • overexpression of mxi1 inhibits the induction of the human ornithine decarboxylase gene by the myc Max Protein complex
    Oncogene, 1996
    Co-Authors: A Pena, A Korcz, Dianne Robert Soprano, Kenneth J Soprano
    Abstract:

    We have previously shown that the Myc/Max Protein complex plays a role in the growth-associated expression of the human ornithine decarboxylase gene. Mxi1 and Mad, novel Max-associated Proteins have been identified and shown to form heterodimers with Max which bind efficiently to the Myc/Max consensus recognition sequence, CACGTG, in vitro. However, formation of Max/Mxi1 or Max/Mad heterodimers results in a reduction in Myc/Max dependent transcriptional activation of reporter plasmid constructs containing the consensus element. In light of the evidence that ODC is transcriptionally regulated in vitro and in vivo by the Myc/Max Protein complex and the potential role of Mxi1 and Mad as antagonists of Myc transactivation activity, we set out to determine if one of these Max associated Proteins, Mxi1, could affect the regulation of ODC expression by Myc/Max and if this regulation was correlated to growth status. Our results show that overexpression of Mxi1 does in fact inhibit ODC gene expression in a dose-dependent manner both in vivo and in vitro. In addition, evidence is presented which shows that levels of Mxi1 are up-regulated during long term quiescence and down-regulated following growth stimulation by serum. These results suggest that alterations in the levels of Max-associated Proteins such as Mxi1 can modulate critical levels of functional Myc/Max Protein complexes. This can alter transcriptional transactivation of Myc-regulated targets and as a consequence affect levels of genes essential for initiation and/or maintenance of growth.

  • regulation of human ornithine decarboxylase expression by the c myc Max Protein complex
    Journal of Biological Chemistry, 1993
    Co-Authors: A Pena, Dianne Robert Soprano, C D Reddy, N J Hickok, E P Reddy, Gladys Yumet, Kenneth J Soprano
    Abstract:

    The presence of a CACGTG element within a region of the human ornithine decarboxylase (ODC) promoter located at -491 to -474 base pairs 5' to the start site of transcription suggested that the c-Myc.Max Protein complex may play a role in the regulation of ODC expression during growth. Electrophoretic mobility shift assays and methylation interference analysis showed that the nuclei of WI-38 cells expressing ODC contained Proteins that bound to this region of the ODC gene in a manner that correlated with growth-associated ODC expression. Also, use of antibodies against c-Myc and Max and purified recombinant c-Myc and Max Protein in the electrophoretic mobility shift assay confirmed that these Proteins can specifically bind this portion of the human ODC promoter. Transient transfection studies showed that increase in the level of c-Myc and/or Max led to a significant enhancement of expression of a human ODC promoter-CAT reporter construct. Moreover, treatment of actively growing WI-38 cells with an antisense oligomer to c-Myc reduced the amount of endogenous Protein complex formed and the amount of endogenous ODC mRNA expressed. These studies show that the c-Myc.Max Protein complex plays a role in the transcriptional regulation of human ODC in vivo.

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

  • overexpression of mxi1 inhibits the induction of the human ornithine decarboxylase gene by the myc Max Protein complex
    Oncogene, 1996
    Co-Authors: A Pena, A Korcz, Dianne Robert Soprano, Kenneth J Soprano
    Abstract:

    We have previously shown that the Myc/Max Protein complex plays a role in the growth-associated expression of the human ornithine decarboxylase gene. Mxi1 and Mad, novel Max-associated Proteins have been identified and shown to form heterodimers with Max which bind efficiently to the Myc/Max consensus recognition sequence, CACGTG, in vitro. However, formation of Max/Mxi1 or Max/Mad heterodimers results in a reduction in Myc/Max dependent transcriptional activation of reporter plasmid constructs containing the consensus element. In light of the evidence that ODC is transcriptionally regulated in vitro and in vivo by the Myc/Max Protein complex and the potential role of Mxi1 and Mad as antagonists of Myc transactivation activity, we set out to determine if one of these Max associated Proteins, Mxi1, could affect the regulation of ODC expression by Myc/Max and if this regulation was correlated to growth status. Our results show that overexpression of Mxi1 does in fact inhibit ODC gene expression in a dose-dependent manner both in vivo and in vitro. In addition, evidence is presented which shows that levels of Mxi1 are up-regulated during long term quiescence and down-regulated following growth stimulation by serum. These results suggest that alterations in the levels of Max-associated Proteins such as Mxi1 can modulate critical levels of functional Myc/Max Protein complexes. This can alter transcriptional transactivation of Myc-regulated targets and as a consequence affect levels of genes essential for initiation and/or maintenance of growth.

  • regulation of human ornithine decarboxylase expression by the c myc Max Protein complex
    Journal of Biological Chemistry, 1993
    Co-Authors: A Pena, Dianne Robert Soprano, C D Reddy, N J Hickok, E P Reddy, Gladys Yumet, Kenneth J Soprano
    Abstract:

    The presence of a CACGTG element within a region of the human ornithine decarboxylase (ODC) promoter located at -491 to -474 base pairs 5' to the start site of transcription suggested that the c-Myc.Max Protein complex may play a role in the regulation of ODC expression during growth. Electrophoretic mobility shift assays and methylation interference analysis showed that the nuclei of WI-38 cells expressing ODC contained Proteins that bound to this region of the ODC gene in a manner that correlated with growth-associated ODC expression. Also, use of antibodies against c-Myc and Max and purified recombinant c-Myc and Max Protein in the electrophoretic mobility shift assay confirmed that these Proteins can specifically bind this portion of the human ODC promoter. Transient transfection studies showed that increase in the level of c-Myc and/or Max led to a significant enhancement of expression of a human ODC promoter-CAT reporter construct. Moreover, treatment of actively growing WI-38 cells with an antisense oligomer to c-Myc reduced the amount of endogenous Protein complex formed and the amount of endogenous ODC mRNA expressed. These studies show that the c-Myc.Max Protein complex plays a role in the transcriptional regulation of human ODC in vivo.

Gregory C. Lanzaro - One of the best experts on this subject based on the ideXlab platform.

  • ANTIGENIC DIVERSITY IN MaxADILAN, A SALIVARY Protein FROM THE SAND FLY VECTOR OF AMERICAN VISCERAL LEISHMANIASIS
    The American journal of tropical medicine and hygiene, 2004
    Co-Authors: Rania S. Milleron, John Paul Mutebi, Sonia Valle, Alberto Montoya, Huaizhi Yin, Lynn Soong, Gregory C. Lanzaro
    Abstract:

    The salivary Protein Maxadilan (Max) is a vasodilator and immunomodulator from the sand fly vector of the protozoan parasite Leishmania chagasi. Vaccinating BALB/c mice with sand fly salivary gland extracts or with Max protects the host against L. major infection. Because of the potential use of Max in an anti-Leishmania vaccine, we characterized the vertebrate host IgG response to Max in the present study. Our immunochemical analysis indicated that antibodies to Max were detected in BALB/c mice, as well as in pigs and humans, from a area in Nicaragua endemic for Lutzomyia longipalpis. Previous studies demonstrate that the Max Protein is polymorphic on the amino acid level. Our findings suggested that naturally occurring Max variants were recognized specifically by the host immune system and antigenicity appeared to be associated with amino-acid sequence variability. Thus, antigenic diversity of Max and possibly of other arthropod salivary Proteins may dictate the development of vector-based vaccines(s).

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

  • 2004a) Antigenic diversity in Maxadilan, a salivary Protein from the sand fly vector of American visceral leishmaniasis
    2015
    Co-Authors: Rania S. Milleron, John Paul Mutebi, Sonia Valle, Alberto Montoya, Huaizhi Yin, Lynn Soong, C. Lanzaro
    Abstract:

    Abstract. The salivary Protein Maxadilan (Max) is a vasodilator and immunomodulator from the sand fly vector of the protozoan parasite Leishmania chagasi. Vaccinating BALB/c mice with sand fly salivary gland extracts or with Max protects the host against L. major infection. Because of the potential use of Max in an anti-Leishmania vaccine, we characterized the vertebrate host IgG response to Max in the present study. Our immunochemical analysis indicated that antibodies to Max were detected in BALB/c mice, as well as in pigs and humans, from a area in Nicaragua endemic for Lutzomyia longipalpis. Previous studies demonstrate that the Max Protein is polymorphic on the amino acid level. Our findings suggested that naturally occurring Max variants were recognized specifically by the host immune system and antigenicity appeared to be associated with amino-acid sequence variability. Thus, antigenic diversity of Max and possibly of other arthropod salivary Proteins may dictate the development of vector-based vaccines(s)

  • ANTIGENIC DIVERSITY IN MaxADILAN, A SALIVARY Protein FROM THE SAND FLY VECTOR OF AMERICAN VISCERAL LEISHMANIASIS
    The American journal of tropical medicine and hygiene, 2004
    Co-Authors: Rania S. Milleron, John Paul Mutebi, Sonia Valle, Alberto Montoya, Huaizhi Yin, Lynn Soong, Gregory C. Lanzaro
    Abstract:

    The salivary Protein Maxadilan (Max) is a vasodilator and immunomodulator from the sand fly vector of the protozoan parasite Leishmania chagasi. Vaccinating BALB/c mice with sand fly salivary gland extracts or with Max protects the host against L. major infection. Because of the potential use of Max in an anti-Leishmania vaccine, we characterized the vertebrate host IgG response to Max in the present study. Our immunochemical analysis indicated that antibodies to Max were detected in BALB/c mice, as well as in pigs and humans, from a area in Nicaragua endemic for Lutzomyia longipalpis. Previous studies demonstrate that the Max Protein is polymorphic on the amino acid level. Our findings suggested that naturally occurring Max variants were recognized specifically by the host immune system and antigenicity appeared to be associated with amino-acid sequence variability. Thus, antigenic diversity of Max and possibly of other arthropod salivary Proteins may dictate the development of vector-based vaccines(s).

Dianne Robert Soprano - One of the best experts on this subject based on the ideXlab platform.

  • overexpression of mxi1 inhibits the induction of the human ornithine decarboxylase gene by the myc Max Protein complex
    Oncogene, 1996
    Co-Authors: A Pena, A Korcz, Dianne Robert Soprano, Kenneth J Soprano
    Abstract:

    We have previously shown that the Myc/Max Protein complex plays a role in the growth-associated expression of the human ornithine decarboxylase gene. Mxi1 and Mad, novel Max-associated Proteins have been identified and shown to form heterodimers with Max which bind efficiently to the Myc/Max consensus recognition sequence, CACGTG, in vitro. However, formation of Max/Mxi1 or Max/Mad heterodimers results in a reduction in Myc/Max dependent transcriptional activation of reporter plasmid constructs containing the consensus element. In light of the evidence that ODC is transcriptionally regulated in vitro and in vivo by the Myc/Max Protein complex and the potential role of Mxi1 and Mad as antagonists of Myc transactivation activity, we set out to determine if one of these Max associated Proteins, Mxi1, could affect the regulation of ODC expression by Myc/Max and if this regulation was correlated to growth status. Our results show that overexpression of Mxi1 does in fact inhibit ODC gene expression in a dose-dependent manner both in vivo and in vitro. In addition, evidence is presented which shows that levels of Mxi1 are up-regulated during long term quiescence and down-regulated following growth stimulation by serum. These results suggest that alterations in the levels of Max-associated Proteins such as Mxi1 can modulate critical levels of functional Myc/Max Protein complexes. This can alter transcriptional transactivation of Myc-regulated targets and as a consequence affect levels of genes essential for initiation and/or maintenance of growth.

  • regulation of human ornithine decarboxylase expression by the c myc Max Protein complex
    Journal of Biological Chemistry, 1993
    Co-Authors: A Pena, Dianne Robert Soprano, C D Reddy, N J Hickok, E P Reddy, Gladys Yumet, Kenneth J Soprano
    Abstract:

    The presence of a CACGTG element within a region of the human ornithine decarboxylase (ODC) promoter located at -491 to -474 base pairs 5' to the start site of transcription suggested that the c-Myc.Max Protein complex may play a role in the regulation of ODC expression during growth. Electrophoretic mobility shift assays and methylation interference analysis showed that the nuclei of WI-38 cells expressing ODC contained Proteins that bound to this region of the ODC gene in a manner that correlated with growth-associated ODC expression. Also, use of antibodies against c-Myc and Max and purified recombinant c-Myc and Max Protein in the electrophoretic mobility shift assay confirmed that these Proteins can specifically bind this portion of the human ODC promoter. Transient transfection studies showed that increase in the level of c-Myc and/or Max led to a significant enhancement of expression of a human ODC promoter-CAT reporter construct. Moreover, treatment of actively growing WI-38 cells with an antisense oligomer to c-Myc reduced the amount of endogenous Protein complex formed and the amount of endogenous ODC mRNA expressed. These studies show that the c-Myc.Max Protein complex plays a role in the transcriptional regulation of human ODC in vivo.