The Experts below are selected from a list of 32010 Experts worldwide ranked by ideXlab platform
Ciro Abbondanza - One of the best experts on this subject based on the ideXlab platform.
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steroid induced androgen receptor oestradiol receptor β src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
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steroid induced androgen receptor oestradiol receptor beta src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
John E. Volanakis - One of the best experts on this subject based on the ideXlab platform.
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down regulation of secretion of human complement component c2 by the product of an alternatively spliced c2 messenger rna
Journal of Immunology, 1996Co-Authors: Hidekazu Tsukamoto, Richard B Marchase, Albert Tousson, John E. VolanakisAbstract:We have previously described alternatively spliced transcripts of the human C2 gene. Among those, C2delta(17), in which exon 17 has been spliced out, encodes a polypeptide that contains the C4b binding and the CIs cleavage sites of C2, but lacks the serine protease active center. To study the possible function of this variant, we constructed C2delta(17) cDNA by deletional mutagenesis and expressed it transiently in COS Cells. Transfected COS Cells secreted only trace amounts of the C2delta(17) polypeptide, which had no detectable hemolytic activity and could not be cleaved by CIs. Pulse-chase experiments using [35S]methionine demonstrated that the majority of the 88-kDa C2delta(17) remained intracellular. Control wild-type (wt) C2 in the intracellular compartment consisted of two bands of 93 and 99 kDa, the latter corresponding to mature secreted C2. Intracellular C2delta(17) and only the 93-kDa wt C2 were sensitive to endoglyCOSidase H, a marker for transport from the endoplasmic reticulum (ER) to the Golgi. Experiments using brefeldin A and double label immunofluorescence staining indicated that C2delta(17) exhibited a typical ER distribution pattern, while wt C2 accumulated in the ER-Golgi intermediate compartment. Secretion of C2 by COS Cells cotransfected with wt C2 and C2delta(17) cDNA was significantly decreased compared with that by Cells transfected with wt C2 alone. These combined results indicate that C2delta(17) is retained in the ER probably because it is incorrectly folded and that it could down-regulate the expression of the wt C2 gene.
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down regulation of secretion of human complement component c2 by the product of an alternatively spliced c2 messenger rna
Journal of Immunology, 1996Co-Authors: Hidekazu Tsukamoto, Richard B Marchase, Albert Tousson, John E. VolanakisAbstract:We have previously described alternatively spliced transcripts of the human C2 gene. Among those, C2delta(17), in which exon 17 has been spliced out, encodes a polypeptide that contains the C4b binding and the CIs cleavage sites of C2, but lacks the serine protease active center. To study the possible function of this variant, we constructed C2delta(17) cDNA by deletional mutagenesis and expressed it transiently in COS Cells. Transfected COS Cells secreted only trace amounts of the C2delta(17) polypeptide, which had no detectable hemolytic activity and could not be cleaved by CIs. Pulse-chase experiments using [35S]methionine demonstrated that the majority of the 88-kDa C2delta(17) remained intracellular. Control wild-type (wt) C2 in the intracellular compartment consisted of two bands of 93 and 99 kDa, the latter corresponding to mature secreted C2. Intracellular C2delta(17) and only the 93-kDa wt C2 were sensitive to endoglyCOSidase H, a marker for transport from the endoplasmic reticulum (ER) to the Golgi. Experiments using brefeldin A and double label immunofluorescence staining indicated that C2delta(17) exhibited a typical ER distribution pattern, while wt C2 accumulated in the ER-Golgi intermediate compartment. Secretion of C2 by COS Cells cotransfected with wt C2 and C2delta(17) cDNA was significantly decreased compared with that by Cells transfected with wt C2 alone. These combined results indicate that C2delta(17) is retained in the ER probably because it is incorrectly folded and that it could down-regulate the expression of the wt C2 gene.
Antimo Migliaccio - One of the best experts on this subject based on the ideXlab platform.
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steroid induced androgen receptor oestradiol receptor β src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
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steroid induced androgen receptor oestradiol receptor beta src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
Hidekazu Tsukamoto - One of the best experts on this subject based on the ideXlab platform.
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down regulation of secretion of human complement component c2 by the product of an alternatively spliced c2 messenger rna
Journal of Immunology, 1996Co-Authors: Hidekazu Tsukamoto, Richard B Marchase, Albert Tousson, John E. VolanakisAbstract:We have previously described alternatively spliced transcripts of the human C2 gene. Among those, C2delta(17), in which exon 17 has been spliced out, encodes a polypeptide that contains the C4b binding and the CIs cleavage sites of C2, but lacks the serine protease active center. To study the possible function of this variant, we constructed C2delta(17) cDNA by deletional mutagenesis and expressed it transiently in COS Cells. Transfected COS Cells secreted only trace amounts of the C2delta(17) polypeptide, which had no detectable hemolytic activity and could not be cleaved by CIs. Pulse-chase experiments using [35S]methionine demonstrated that the majority of the 88-kDa C2delta(17) remained intracellular. Control wild-type (wt) C2 in the intracellular compartment consisted of two bands of 93 and 99 kDa, the latter corresponding to mature secreted C2. Intracellular C2delta(17) and only the 93-kDa wt C2 were sensitive to endoglyCOSidase H, a marker for transport from the endoplasmic reticulum (ER) to the Golgi. Experiments using brefeldin A and double label immunofluorescence staining indicated that C2delta(17) exhibited a typical ER distribution pattern, while wt C2 accumulated in the ER-Golgi intermediate compartment. Secretion of C2 by COS Cells cotransfected with wt C2 and C2delta(17) cDNA was significantly decreased compared with that by Cells transfected with wt C2 alone. These combined results indicate that C2delta(17) is retained in the ER probably because it is incorrectly folded and that it could down-regulate the expression of the wt C2 gene.
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down regulation of secretion of human complement component c2 by the product of an alternatively spliced c2 messenger rna
Journal of Immunology, 1996Co-Authors: Hidekazu Tsukamoto, Richard B Marchase, Albert Tousson, John E. VolanakisAbstract:We have previously described alternatively spliced transcripts of the human C2 gene. Among those, C2delta(17), in which exon 17 has been spliced out, encodes a polypeptide that contains the C4b binding and the CIs cleavage sites of C2, but lacks the serine protease active center. To study the possible function of this variant, we constructed C2delta(17) cDNA by deletional mutagenesis and expressed it transiently in COS Cells. Transfected COS Cells secreted only trace amounts of the C2delta(17) polypeptide, which had no detectable hemolytic activity and could not be cleaved by CIs. Pulse-chase experiments using [35S]methionine demonstrated that the majority of the 88-kDa C2delta(17) remained intracellular. Control wild-type (wt) C2 in the intracellular compartment consisted of two bands of 93 and 99 kDa, the latter corresponding to mature secreted C2. Intracellular C2delta(17) and only the 93-kDa wt C2 were sensitive to endoglyCOSidase H, a marker for transport from the endoplasmic reticulum (ER) to the Golgi. Experiments using brefeldin A and double label immunofluorescence staining indicated that C2delta(17) exhibited a typical ER distribution pattern, while wt C2 accumulated in the ER-Golgi intermediate compartment. Secretion of C2 by COS Cells cotransfected with wt C2 and C2delta(17) cDNA was significantly decreased compared with that by Cells transfected with wt C2 alone. These combined results indicate that C2delta(17) is retained in the ER probably because it is incorrectly folded and that it could down-regulate the expression of the wt C2 gene.
Maria Vittoria Barone - One of the best experts on this subject based on the ideXlab platform.
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steroid induced androgen receptor oestradiol receptor β src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
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steroid induced androgen receptor oestradiol receptor beta src complex triggers prostate cancer cell proliferation
The EMBO Journal, 2000Co-Authors: Antimo Migliaccio, Gabriella Castoria, Marina Di Domenico, Antonietta De Falco, Antonio Bilancio, Maria Lombardi, Maria Vittoria Barone, Donatella Ametrano, Maria Stella Zannini, Ciro AbbondanzaAbstract:Treatment of human prostate carcinoma-derived LNCaP Cells with androgen or oestradiol triggers simultaneous association of androgen receptor and oestradiol receptor beta with Src, activates the Src/Raf-1/Erk-2 pathway and stimulates cell proliferation. Surprisingly, either androgen or oestradiol action on each of these steps is inhibited by both anti-androgens and anti-oestrogens. Similar findings for oestradiol receptor alpha were observed in MCF-7 or T47D Cells stimulated by either oestradiol or androgens. Microinjection of LNCaP, MCF-7 and T47D Cells with SrcK(-) abolishes steroid-stimulated S-phase entry. Data from transfected COS Cells confirm and extend the findings from these Cells. Hormone-stimulated Src interaction with the androgen receptor and oestradiol receptor alpha or beta is detected using glutathione S:-transferase fusion constructs. Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. The role of this phosphotyrosine is stressed by its requirement for association of oestradiol receptor alpha with Src and consequent activation of Src in intact COS Cells.
