AT Rich Sequence

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

  • sATb2 suppresses the progression of colorectal cancer cells via inactivATion of mek5 erk5 signaling
    FEBS Journal, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Kenji Kurita, Keisuke Uehara, Toshio Kokuryo, Michinari Hamaguchi, Masahide Takahashi, Masato Nagino, Takeshi Senga
    Abstract:

    Special AT-Rich Sequence binding protein 2 (SATB2) is an evolutionarily conserved transcription factor thAT has multiple roles in neuronal development, osteoblast differentiATion, and craniofacial pATterning. SATB2 binds to the nuclear mATrix ATtachment region, and regulATes the expression of diverse sets of genes by altering chromATin structure. Recent studies have reported thAT high expression of SATB2 is associATed with favorable prognosis in colorectal and laryngeal cancer; however, it remains uncertain whether SATB2 has tumor-suppressive functions in cancer cells. In this study, we examined the effects of SATB2 expression on the malignant characteristics of colorectal cancer cells. Expression of SATB2 repressed the proliferATion of cancer cells in vitro and in vivo, and also suppressed their migrATion and invasion. Extracellular signal-regulATed kinase 5 (ERK5) is a mitogen-activATed protein kinase thAT is associATed with an aggressive phenotype in various types of cancer. SATB2 expression reduced the activity of ERK5, and constitutive activATion of ERK5 restored the proliferATion, anchorage-independent growth, migrATion and invasion of SATB2-expressing cells. Our results demonstrATe the existence of a novel regulATory mechanism of SATB2-mediATed tumor suppression via ERK5 inactivATion.

  • special AT Rich Sequence binding protein 2 suppresses invadopodia formATion in hct116 cells via palladin inhibition
    Experimental Cell Research, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Michinari Hamaguchi, Masahide Takahashi, Eri Asano, Khondker Ayesha Akter, Takeshi Senga
    Abstract:

    Invadopodia are specialized actin-based microdomains of the plasma membrane thAT combine adhesive properties with mATrix degrading activities. Proper functioning of the bone, immune, and vascular systems depend on these organelles, and their relevance in cancer cells is linked to tumor metastasis. The elucidATion of the mechanisms driving invadopodia formATion is a prerequisite to understanding their role and ultimATely to controlling their functions. Special AT-Rich Sequence-binding protein 2 (SATB2) was reported to suppress tumor cell migrATion and metastasis. However, the mechanism of action of SATB2 is unknown. Here, we show thAT SATB2 inhibits invadopodia formATion in HCT116 cells and thAT the molecular scaffold palladin is inhibited by exogenous expression of SATB2. To confirm this associATion, we elucidATed the function of palladin in HCT116 using a knock down strATegy. Palladin knock down reduced cell migrATion and invasion and inhibited invadopodia formATion. This phenotype was confirmed by a rescue experiment. We then demonstrATed thAT palladin expression in SATB2-expressing cells restored invasion and invadopodia formATion. Our results showed thAT SATB2 action is mediATed by palladin inhibition and the SATB2/palladin pAThway is associATed with invadopodia formATion in colorectal cancer cells.

  • SATB2 suppresses the progression of colorectal cancer cells via inactivATion of MEK5/ERK5 signaling
    FEBS Journal, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Kenji Kurita, Keisuke Uehara, Toshio Kokuryo, Michinari Hamaguchi, Masahide Takahashi, Masato Nagino, Takeshi Senga
    Abstract:

    Abstract Special AT-Rich Sequence binding protein 2 (SATB2) is an evolutionarily conserved transcription factor thAT has multiple roles in neuronal development, osteoblast differentiATion, and craniofacial pATterning. SATB2 binds to the nuclear mATrix ATtachment region, and regulATes the expression of diverse sets of genes by altering chromATin structure. Recent studies have reported thAT high expression of SATB2 is associATed with favorable prognosis in colorectal and laryngeal cancer; however, it remains uncertain whether SATB2 has tumor-suppressive functions in cancer cells. In this study, we examined the effects of SATB2 expression on the malignant characteristics of colorectal cancer cells. Expression of SATB2 repressed the proliferATion of cancer cells in vitro and in vivo, and also suppressed their migrATion and invasion. Extracellular signal-regulATed kinase 5 (ERK5) is a mitogen-activATed protein kinase thAT is associATed with an aggressive phenotype in various types of cancer. SATB2 expression reduced the activity of ERK5, and constitutive activATion of ERK5 restored the proliferATion, anchorage-independent growth, migrATion and invasion of SATB2-expressing cells. Our results demonstrATe the existence of a novel regulATory mechanism of SATB2-mediATed tumor suppression via ERK5 inactivATion.

Takeshi Senga - One of the best experts on this subject based on the ideXlab platform.

  • sATb2 suppresses the progression of colorectal cancer cells via inactivATion of mek5 erk5 signaling
    FEBS Journal, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Kenji Kurita, Keisuke Uehara, Toshio Kokuryo, Michinari Hamaguchi, Masahide Takahashi, Masato Nagino, Takeshi Senga
    Abstract:

    Special AT-Rich Sequence binding protein 2 (SATB2) is an evolutionarily conserved transcription factor thAT has multiple roles in neuronal development, osteoblast differentiATion, and craniofacial pATterning. SATB2 binds to the nuclear mATrix ATtachment region, and regulATes the expression of diverse sets of genes by altering chromATin structure. Recent studies have reported thAT high expression of SATB2 is associATed with favorable prognosis in colorectal and laryngeal cancer; however, it remains uncertain whether SATB2 has tumor-suppressive functions in cancer cells. In this study, we examined the effects of SATB2 expression on the malignant characteristics of colorectal cancer cells. Expression of SATB2 repressed the proliferATion of cancer cells in vitro and in vivo, and also suppressed their migrATion and invasion. Extracellular signal-regulATed kinase 5 (ERK5) is a mitogen-activATed protein kinase thAT is associATed with an aggressive phenotype in various types of cancer. SATB2 expression reduced the activity of ERK5, and constitutive activATion of ERK5 restored the proliferATion, anchorage-independent growth, migrATion and invasion of SATB2-expressing cells. Our results demonstrATe the existence of a novel regulATory mechanism of SATB2-mediATed tumor suppression via ERK5 inactivATion.

  • special AT Rich Sequence binding protein 2 suppresses invadopodia formATion in hct116 cells via palladin inhibition
    Experimental Cell Research, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Michinari Hamaguchi, Masahide Takahashi, Eri Asano, Khondker Ayesha Akter, Takeshi Senga
    Abstract:

    Invadopodia are specialized actin-based microdomains of the plasma membrane thAT combine adhesive properties with mATrix degrading activities. Proper functioning of the bone, immune, and vascular systems depend on these organelles, and their relevance in cancer cells is linked to tumor metastasis. The elucidATion of the mechanisms driving invadopodia formATion is a prerequisite to understanding their role and ultimATely to controlling their functions. Special AT-Rich Sequence-binding protein 2 (SATB2) was reported to suppress tumor cell migrATion and metastasis. However, the mechanism of action of SATB2 is unknown. Here, we show thAT SATB2 inhibits invadopodia formATion in HCT116 cells and thAT the molecular scaffold palladin is inhibited by exogenous expression of SATB2. To confirm this associATion, we elucidATed the function of palladin in HCT116 using a knock down strATegy. Palladin knock down reduced cell migrATion and invasion and inhibited invadopodia formATion. This phenotype was confirmed by a rescue experiment. We then demonstrATed thAT palladin expression in SATB2-expressing cells restored invasion and invadopodia formATion. Our results showed thAT SATB2 action is mediATed by palladin inhibition and the SATB2/palladin pAThway is associATed with invadopodia formATion in colorectal cancer cells.

  • SATB2 suppresses the progression of colorectal cancer cells via inactivATion of MEK5/ERK5 signaling
    FEBS Journal, 2015
    Co-Authors: Mohammed A Mansour, Toshinori Hyodo, Kenji Kurita, Keisuke Uehara, Toshio Kokuryo, Michinari Hamaguchi, Masahide Takahashi, Masato Nagino, Takeshi Senga
    Abstract:

    Abstract Special AT-Rich Sequence binding protein 2 (SATB2) is an evolutionarily conserved transcription factor thAT has multiple roles in neuronal development, osteoblast differentiATion, and craniofacial pATterning. SATB2 binds to the nuclear mATrix ATtachment region, and regulATes the expression of diverse sets of genes by altering chromATin structure. Recent studies have reported thAT high expression of SATB2 is associATed with favorable prognosis in colorectal and laryngeal cancer; however, it remains uncertain whether SATB2 has tumor-suppressive functions in cancer cells. In this study, we examined the effects of SATB2 expression on the malignant characteristics of colorectal cancer cells. Expression of SATB2 repressed the proliferATion of cancer cells in vitro and in vivo, and also suppressed their migrATion and invasion. Extracellular signal-regulATed kinase 5 (ERK5) is a mitogen-activATed protein kinase thAT is associATed with an aggressive phenotype in various types of cancer. SATB2 expression reduced the activity of ERK5, and constitutive activATion of ERK5 restored the proliferATion, anchorage-independent growth, migrATion and invasion of SATB2-expressing cells. Our results demonstrATe the existence of a novel regulATory mechanism of SATB2-mediATed tumor suppression via ERK5 inactivATion.

Maija R J Kohonencorish - One of the best experts on this subject based on the ideXlab platform.

  • loss of special AT Rich Sequence binding protein 1 sATb1 predicts poor survival in pATients with colorectal cancer
    Histopathology, 2014
    Co-Authors: Sam Alsohaily, Christopher Henderson, Christina I Selinger, Laurent Pangon, Eva Segelov, Maija R J Kohonencorish
    Abstract:

    Aim Special AT-Rich Sequence-binding protein 1 (SATB1) is a cell type-specific mATrix ATtachment region binding protein, functioning as a global genome organizer. This study aims to investigATe the expression pATtern and the prognostic value of SATB1 in colorectal cancer. Methods and results Prospectively collected dATa were obtained and tissue microarrays were constructed from a cohort of 352 pATients. SATB1 protein expression was evaluATed by immunohistochemistry and scored by two independent investigATors. SATB1 expression was predominantly nuclear in both normal and cancer tissues. Loss of SATB1 nuclear expression was seen in 22% of colorectal cancers compared to 1.5% of adjacent normal colorectal tissue, and was associATed with worse overall survival (P = 0.02) independent of age and stage of disease (HR 2.48 with 95% CI 1.31–4.70). Loss of SATB1 expression was more evident in younger pATients (P = 0.03), tumours with mucinous or signet ring histology (P = 0.0001) and poor differentiATion (P = 0.005). SATB1 expression was associATed with a survival advantage in pATients with Dukes C tumours who received adjuvant chemotherapy. Conclusion Loss of SATB1 nuclear expression correlATes with poor survival and a less favourable response to adjuvant chemotherapy in colorectal cancer. The value of SATB1 in individualized colorectal cancer therapy warrants further evaluATion.

Yukio Sugiura - One of the best experts on this subject based on the ideXlab platform.

  • Alpha-helix substitution: novel approach for the design of a new zinc finger peptides for AT-Rich Sequence.
    Nucleic Acids Symposium Series, 2002
    Co-Authors: Makoto Nagaoka, Yoshihide Doi, Jun Kuwahara, Yukio Sugiura
    Abstract:

    A novel strATegy for the design of a zinc finger peptide on the basis of alpha-helix substitution has been demonstrATed. Sp1HM is a helix-substituted mutant for the wild-type Sp1(zf123) and its alpha-helix of each finger is replaced by thAT of fingers 4-6 of CF2-II. The circular dichroism spectrum of Sp1HM suggests thAT Sp1HM has an ordered secondary structure similar to Sp1(zf123). From the analyses of the DNA binding affinity and specificity by gel mobility shift assay, it is clearly indicATed thAT Sp1HM specifically binds to the AT-Rich Sequence (5'-GTA TAT ATA-3') with 3 nM dissociATion constants. Moreover, the zinc finger peptides for the Sequence alternATing between the AT- and GC-Rich subsites can also be creATed by the alpha-helix substitution. This strATegy is evidently effective and is also more convenient than the phage display method. Consequently, our design method is widely applicable to creATing zinc finger peptides with novel binding specificities.

  • novel strATegy for the design of a new zinc finger creATion of a zinc finger for the AT Rich Sequence by α helix substitution
    Journal of the American Chemical Society, 2002
    Co-Authors: Makoto Nagaoka, Yoshihide Doi, Jun Kuwahara, Yukio Sugiura
    Abstract:

    In this communicATion, a novel strATegy for the design of a zinc finger peptide on the basis of α-helix substitution has been demonstrATed. Sp1HM is a helix-substituted mutant for the wild-type Sp1(zf123) and its α-helix of each finger is replaced by thAT of fingers 4−6 of CF2-II. The circular dichroism spectrum of Sp1HM suggests thAT Sp1HM has an ordered secondary structure similar to thAT of Sp1(zf123). From the analyses of the DNA binding affinity and specificity by gel mobility shift assay, it is clearly indicATed thAT Sp1HM specifically binds to the AT-Rich Sequence (5‘-GTA TAT ATA-3‘) with 3.2 nM dissociATion constants. Moreover, the zinc finger peptides for the Sequence alternATing between the AT- and GC-Rich subsites can also be creATed by the α-helix substitution. This strATegy is evidently effective and is also more convenient than the phage display method. Consequently, our design method is widely applicable to creATing zinc finger peptides with novel binding specificities.

Makoto Nagaoka - One of the best experts on this subject based on the ideXlab platform.

  • Alpha-helix substitution: novel approach for the design of a new zinc finger peptides for AT-Rich Sequence.
    Nucleic Acids Symposium Series, 2002
    Co-Authors: Makoto Nagaoka, Yoshihide Doi, Jun Kuwahara, Yukio Sugiura
    Abstract:

    A novel strATegy for the design of a zinc finger peptide on the basis of alpha-helix substitution has been demonstrATed. Sp1HM is a helix-substituted mutant for the wild-type Sp1(zf123) and its alpha-helix of each finger is replaced by thAT of fingers 4-6 of CF2-II. The circular dichroism spectrum of Sp1HM suggests thAT Sp1HM has an ordered secondary structure similar to Sp1(zf123). From the analyses of the DNA binding affinity and specificity by gel mobility shift assay, it is clearly indicATed thAT Sp1HM specifically binds to the AT-Rich Sequence (5'-GTA TAT ATA-3') with 3 nM dissociATion constants. Moreover, the zinc finger peptides for the Sequence alternATing between the AT- and GC-Rich subsites can also be creATed by the alpha-helix substitution. This strATegy is evidently effective and is also more convenient than the phage display method. Consequently, our design method is widely applicable to creATing zinc finger peptides with novel binding specificities.

  • novel strATegy for the design of a new zinc finger creATion of a zinc finger for the AT Rich Sequence by α helix substitution
    Journal of the American Chemical Society, 2002
    Co-Authors: Makoto Nagaoka, Yoshihide Doi, Jun Kuwahara, Yukio Sugiura
    Abstract:

    In this communicATion, a novel strATegy for the design of a zinc finger peptide on the basis of α-helix substitution has been demonstrATed. Sp1HM is a helix-substituted mutant for the wild-type Sp1(zf123) and its α-helix of each finger is replaced by thAT of fingers 4−6 of CF2-II. The circular dichroism spectrum of Sp1HM suggests thAT Sp1HM has an ordered secondary structure similar to thAT of Sp1(zf123). From the analyses of the DNA binding affinity and specificity by gel mobility shift assay, it is clearly indicATed thAT Sp1HM specifically binds to the AT-Rich Sequence (5‘-GTA TAT ATA-3‘) with 3.2 nM dissociATion constants. Moreover, the zinc finger peptides for the Sequence alternATing between the AT- and GC-Rich subsites can also be creATed by the α-helix substitution. This strATegy is evidently effective and is also more convenient than the phage display method. Consequently, our design method is widely applicable to creATing zinc finger peptides with novel binding specificities.