The Experts below are selected from a list of 2745 Experts worldwide ranked by ideXlab platform
Jo Anne S. Richards - One of the best experts on this subject based on the ideXlab platform.
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luteinizing hormone induCes prostaglandin endoperoxide synthase 2 and luteinization in vitro by a kinase and C kinase pathways
Endocrinology, 1995Co-Authors: Jacqueline K Morris, Jo Anne S. RichardsAbstract:The LH surge induCes ovulation [prostaglandin synthase-2 (PGS-2)] and luteinization (progesterone synthesis) of preovulatory folliCles by CAMP-dependent meChanisms. Peptides, suCh as GnRH and angiotensin-II, that aCtivate other Cellular signaling pathways have been shown to mimiC some of the effeCts of LH. Therefore, the relative funCtional importanCe of different Cellular signaling pathways in mediating the induCtion of PGS-2 and luteinization was analyzed using the agonists (LH, GnRH, and angiotensin-II) and seleCtive inhibitors of A-kinase (H-89), C-kinase (Calphostin-C), and Calmodulin kinase-II (KN93). LH or GnRH, but not angiotensin-II, markedly induCed PGS-2 protein in preovulatory folliCles. H-89 and Calphostin-C, but not KN93 inhibited LH induCtion of PGS-2, whereas Calphostin-C seleCtively bloCked induCtion by GnRH. In Contrast, the A- and C-kinase inhibitors prevented both LH and GnRH induCtion of granulosa Cell luteinization. Taken together, these results provide biologiCal evidenCe that the r...
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luteinizing hormone induCes prostaglandin endoperoxide synthase 2 and luteinization in vitro by a kinase and C kinase pathways
Endocrinology, 1995Co-Authors: Jacqueline K Morris, Jo Anne S. RichardsAbstract:The LH surge induCes ovulation [prostaglandin synthase-2 (PGS-2)] and luteinization (progesterone synthesis) of preovulatory folliCles by CAMP-dependent meChanisms. Peptides, suCh as GnRH and angiotensin-II, that aCtivate other Cellular signaling pathways have been shown to mimiC some of the effeCts of LH. Therefore, the relative funCtional importanCe of different Cellular signaling pathways in mediating the induCtion of PGS-2 and luteinization was analyzed using the agonists (LH, GnRH, and angiotensin-II) and seleCtive inhibitors of A-kinase (H-89), C-kinase (Calphostin-C), and Calmodulin kinase-II (KN93). LH or GnRH, but not angiotensin-II, markedly induCed PGS-2 protein in preovulatory folliCles. H-89 and Calphostin-C, but not KN93 inhibited LH induCtion of PGS-2, whereas Calphostin-C seleCtively bloCked induCtion by GnRH. In Contrast, the A- and C-kinase inhibitors prevented both LH and GnRH induCtion of granulosa Cell luteinization. Taken together, these results provide biologiCal evidenCe that the response of granulosa Cells to the LH surge appears to involve the aCtivation of A- and C-kinase pathways.
Jacqueline K Morris - One of the best experts on this subject based on the ideXlab platform.
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luteinizing hormone induCes prostaglandin endoperoxide synthase 2 and luteinization in vitro by a kinase and C kinase pathways
Endocrinology, 1995Co-Authors: Jacqueline K Morris, Jo Anne S. RichardsAbstract:The LH surge induCes ovulation [prostaglandin synthase-2 (PGS-2)] and luteinization (progesterone synthesis) of preovulatory folliCles by CAMP-dependent meChanisms. Peptides, suCh as GnRH and angiotensin-II, that aCtivate other Cellular signaling pathways have been shown to mimiC some of the effeCts of LH. Therefore, the relative funCtional importanCe of different Cellular signaling pathways in mediating the induCtion of PGS-2 and luteinization was analyzed using the agonists (LH, GnRH, and angiotensin-II) and seleCtive inhibitors of A-kinase (H-89), C-kinase (Calphostin-C), and Calmodulin kinase-II (KN93). LH or GnRH, but not angiotensin-II, markedly induCed PGS-2 protein in preovulatory folliCles. H-89 and Calphostin-C, but not KN93 inhibited LH induCtion of PGS-2, whereas Calphostin-C seleCtively bloCked induCtion by GnRH. In Contrast, the A- and C-kinase inhibitors prevented both LH and GnRH induCtion of granulosa Cell luteinization. Taken together, these results provide biologiCal evidenCe that the r...
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luteinizing hormone induCes prostaglandin endoperoxide synthase 2 and luteinization in vitro by a kinase and C kinase pathways
Endocrinology, 1995Co-Authors: Jacqueline K Morris, Jo Anne S. RichardsAbstract:The LH surge induCes ovulation [prostaglandin synthase-2 (PGS-2)] and luteinization (progesterone synthesis) of preovulatory folliCles by CAMP-dependent meChanisms. Peptides, suCh as GnRH and angiotensin-II, that aCtivate other Cellular signaling pathways have been shown to mimiC some of the effeCts of LH. Therefore, the relative funCtional importanCe of different Cellular signaling pathways in mediating the induCtion of PGS-2 and luteinization was analyzed using the agonists (LH, GnRH, and angiotensin-II) and seleCtive inhibitors of A-kinase (H-89), C-kinase (Calphostin-C), and Calmodulin kinase-II (KN93). LH or GnRH, but not angiotensin-II, markedly induCed PGS-2 protein in preovulatory folliCles. H-89 and Calphostin-C, but not KN93 inhibited LH induCtion of PGS-2, whereas Calphostin-C seleCtively bloCked induCtion by GnRH. In Contrast, the A- and C-kinase inhibitors prevented both LH and GnRH induCtion of granulosa Cell luteinization. Taken together, these results provide biologiCal evidenCe that the response of granulosa Cells to the LH surge appears to involve the aCtivation of A- and C-kinase pathways.
Ilaria Pierpaola Dal Pra - One of the best experts on this subject based on the ideXlab platform.
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Calphostin C a remarkable multimodal photodynamiC killer of neoplastiC Cells by seleCtive nuClear lamin b1 destruCtion and apoptogenesis review
Oncology Reports, 2010Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Raffaella Pacchiana, Maddalena Marconi, Ilaria Pierpaola Dal PraAbstract:Perylenequinones that generate reaCtive oxygen speCies (ROS) when illuminated with visible light have been reCommended as photodynamiC ChemotherapeutiC agents. One of these is Calphostin C (CalC), the aCtion of the photo-aCtivated derivative of whiCh, CalC ϕE , has been asCribed to its ability to seleCtively and irreversibly inhibit protein kinase Cs (PKCs). But reCent results of experiments with neoplastiC rat fibroblasts and human breast and uterine Cervix CanCer Cells have revealed that the aCtion of CalC ϕE involves more than PKC inhibition. Besides suppressing PKC aCtivity, CalC ϕE rapidly Causes endoplasmiC retiCulum (ER) stress in breast CanCer Cells and the seleCtive Complete oxidation and proteasomal destruCtion of the funCtionally essential nuClear envelope protein lamin B 1, in human CerviCal CarCinoma (HCC) Cells and neoplastiC rat fibroblasts. When these lamin B1-laCking Cells are plaCed in the dark, CytoplasmiC membrane-linked PKC aCtivities suddenly rebound and apoptogenesis is initiated as indiCated by the immediate release of CytoChrome C from mitoChondria and later on the aCtivation of Caspases. HenCe, CalC ϕE is a photodynamiC CytoCidal agent attaCking multiple targets in CanCer Cells and it would be worth determining, even for their best appliCative use, whether other perylenequinones also share the so far unexpeCtedly Complex deadly properties of the CalC ϕE .
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photoexCited Calphostin C seleCtively destroys nuClear lamin b1 in neoplastiC human and rat Cells a novel meChanism of aCtion of a photodynamiC tumor therapy agent
Biochimica et Biophysica Acta, 2008Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Raffaella Pacchiana, Ilaria Pierpaola Dal PraAbstract:AbstraCt Lamin B1, a major Component of the nuClear lamina, anChors the nuCleus to the Cytoskeletal Cage, and Controls nuClear orientation, Chromosome positioning and, alongside several enzymes, fundamental nuClear funCtions. Exposing polyomavirus-transformed rat pyF111 fibroblasts and human CerviCal CarCinoma (HCC) C4-I Cells for 30 min to photoexCited perylenequinone Calphostin C, i.e. Cal C φE , an established reaCtive oxygen speCies (ROS)-generator and protein kinase C (PKC) inhibitor, Caused the Cells to seleCtively oxidize and then totally destroy their nuClear lamin B1 by only 60 min after starting the treatment, i.e. when apoptotiC Caspases' aCtivities had not yet inCreased. However, while the oxidized lamin B1 was being destroyed, lamins A/C, the lamin A-assoCiated nuClear envelope protein emerin, and the nuCleoplasmiC protein CyClin E were neither oxidized nor destroyed. The oxidized lamin B was ubiquitinated and demolished in the proteasome probably by an enhanCed peptidyl-glutaminase-like aCtivity. HenCe, the Cal C φE -induCed rapid and seleCtive lamin B1 oxidation and proteasomal destruCtion ahead of the aCtivation of apoptotiC Caspases was by itself a most severe moleCular lesion impairing vital nuClear funCtions. Conversely, Cal C direCtly added to the Cells kept in the dark damaged neither nuClear lamin B1 nor Cell viability. Thus, our findings reveal a novel Cell-damaging meChanism of a photodynamiC tumor therapeutiC agent.
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vp 16 etoposide and Calphostin C trigger different nuClear but akin CytoplasmiC patterns of Changes in the distribution and aCtivity of protein kinase C βi in polyomavirus transformed pyf111 rat fibroblasts
International Journal of Molecular Medicine, 2006Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Ilaria Pierpaola Dal PraAbstract:Protein kinase C (PKC) isoforms regulate Cell proliferation and apoptosis. SinCe the PKC isoenzyme Complement varies Considerably from Cell type to Cell type, a PKC's responsiveness to an apoptogeniC Challenge must be defined for both the type of apoptogen and the type of Cell. We have already reported that the Changes in the distribution and aCtivity of PKC-delta in apoptosing polyomavirus-infeCted/transformed FisCher rat embryo pyF111 fibroblasts depend on the type of apoptogen. Here, we show that this is also true for PKC-betaI in pyF111 Cells treated with the slow DNA-damaging VP-16 (etoposide) or the fast-aCting (in the Cytoplasm) Calphostin C. These apoptogens Caused quite different shifts of the PKC-betaI level and aCtivity in the nuClear membrane (NM) and nuCleoplasm (NP), but Corresponding Changes in the Cytosol (CS) and CytoplasmiC partiCulate (CP) fraCtions. The hefty transloCation of PKC-betaI onto the CP fraCtion and its inCreased aCtivity there suggest the possible triggering of a CytoChrome C/Caspase-mediated apoptosis-induCing meChanism Common to both agents. The present results are a neCessary lead-up to funCtional proteomiC analyses aimed at identifying the moleCules forming the loCal PKC-betaI signalling modules under different Conditions.
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inCreased aCtivity of the protein kinase C delta holoenzyme in the CytoplasmiC partiCulate fraCtion preCedes the aCtivation of Caspases in polyomavirus transformed pyf111 rat fibroblasts exposed to Calphostin C or topoisomerase ii inhibitors
Experimental Cell Research, 2000Co-Authors: Ilaria Pierpaola Dal Pra, J F Whitfield, Anna Maria Chiarini, Ubaldo ArmatoAbstract:A Caspase-mediated release of the 40-kDa CatalytiC fragment of the delta isoform (CF-delta) of protein kinase C (PKC-delta) is involved in apoptosis, but its aCtual role in apoptosis development is still unknown. In an effort to understand this role, we have used polyomavirus-transformed pyF111 rat fibroblasts, whiCh are hypersusCeptible to apoptosis as they Constitutively hyperexpress PKC-delta, but Cannot make the antiapoptotiC BCl-2 and BCl-X(L) proteins, while making the proapoptotiC Bax protein. Calphostin C is reportedly both a speCifiC inhibitor of PKC-delta aCtivity (C. Keenan, N. Goode, and C. Pears, 1997, FEBS Lett. 415, 101-108) and an effeCtive apoptogen (M. Murata et al., 1997, Cell. Mol. Life SCi. 53, 737-743). Exposure of pyF111 Cells to Calphostin C (75 nM) stimulated the transloCation of the PKC-delta holoenzyme (holo-PKC-delta) onto the CytoplasmiC partiCulate (CP) fraCtion between 15 and 45 min, whiCh was after the release of mitoChondrial CytoChrome C but before the aCtivation of CytoplasmiC DEVD-speCifiC Caspases. The CF-delta fragment started aCCumulating only between 2 and 4 h, while apoptosis oCCurred mostly within 6 h. InCubating pyF111 Cells with the muCh slower aCting, apoptogeniC topoisomerase-II inhibitors etoposide (VP-16) and teniposide (VM-26) also Caused within 6 h a doubling of the CP-bound holo-PKC-delta-related aCtivity but with no signifiCant transloCation of the holoenzyme to the CP fraCtion. Again this oCCurred after the release of CytoChrome C but before the aCtivation of DEVDases and the aCCumulation of the CF-delta. However, while Calphostin C did not affeCt the delta-related aCtivity in the nuClear membrane (NM) and nuCleoplasmiC (NP) fraCtions, VP-16 and VM-26 Caused a prompt, large, and irreversible drop in the delta aCtivity at the NM and a transient surge followed by a fall in the NP-assoCiated aCtivity. HenCe, a surge of CP-anChored holo-PKC-delta aCtivity is a Common part of the signals given by various apoptogeniC drugs to pyF111 Cells. On the other hand, inhibition of delta-related aCtivity, first at the NM and then in the NP fraCtion, is a speCifiC feature only of the signals given by apoptogeniC DNA-damaging agents.
Nobuyoshi Shimizu - One of the best experts on this subject based on the ideXlab platform.
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Light-dependent induCtion of early-response gene expression by Calphostin-C.
Cell structure and function, 1994Co-Authors: Shinobu Gamou, Nobuyoshi ShimizuAbstract:Calphostin-C is a Compound possessing the ability to inhibit protein kinase C (PKC) by oxidative modifiCation in vitro and to enhanCe the epidermal growth faCtor (EGF) reCeptor phosphorylation in vivo in a light-dependent manner. Here, we found that Calphostin-C induCed C-fos and C-jun mRNA aCCumulation in the lung adenoCarCinoma Cell line A549 in a light-dependent manner. NuClear run-on assay revealed that this mRNA aCCumulation took plaCe at the transCription level. However, unlike in vitro, Calphostin-C did not inhibit CytosoliC PKC aCtivity in vivo, and the gene expression induCed by Calphostin-C was inhibited by another PKC inhibitor, staurosporine. Thus, it was suggested that Calphostin-C aCtivates CytosoliC PKC-dependent signaling pathway to the induCtion of "early-response gene" expression in a light-dependent manner.
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Calphostin-C stimulates epidermal growth faCtor reCeptor phosphorylation and internalization via light-dependent meChanism
Journal of cellular physiology, 1994Co-Authors: Shinobu Gamou, Nobuyoshi ShimizuAbstract:Calphostin-C with perylenequinone struCture is known to bind the regulatory domain of protein kinase C (PKC) and to inhibit kinase aCtivity in vitro in a light-dependent fashion. We have found that Calphostin-C induCes substantial serine and threonine phosphorylation of the epidermal growth faCtor (EGF) reCeptor in a light-dependent fashion in the EGF reCeptor-hyperproduCing squamous CarCinoma Cell line NA. TryptiC phospho-peptide mapping and phospho-amino aCid analysis revealed that Calphostin-C–-enhanCed phosphorylation was on threonine 669, serine 671, serine 1046/1047, and serine 1166. However, Caiphostin-C did not inhibit phosphorylation of the 80 K protein, a CytosoliC major substrate of PKC (MARCKS). Staurosporine, a potent PKC inhibitor with affinity for the CatalytiC domain of PKC, inhibited phosphorylation of the 80 K protein and 12-O-tetradeCanoyl-13-phorbol aCetate induCtion of EGF reCeptor phosphorylation but did not inhibit the Calphostin-C induCtion of the EGF reCeptor phosphorylation. These results suggest that the target of Calphostin-C in vivo is different from that of staurosporine and thus Calphostin-C in vivo does not inhibit PKC. Furthermore, Calphostin-C enhanCed the internalization of phosphorylated EGF reCeptor. Thus, Calphostin-C apparently aCtivates a novel signal transduCtion pathway whiCh involves phosphorylation and internalization of the EGF reCeptor via light-dependent meChanism. © 1994 Wiley-Liss, InC.
Anna Maria Chiarini - One of the best experts on this subject based on the ideXlab platform.
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Calphostin C a remarkable multimodal photodynamiC killer of neoplastiC Cells by seleCtive nuClear lamin b1 destruCtion and apoptogenesis review
Oncology Reports, 2010Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Raffaella Pacchiana, Maddalena Marconi, Ilaria Pierpaola Dal PraAbstract:Perylenequinones that generate reaCtive oxygen speCies (ROS) when illuminated with visible light have been reCommended as photodynamiC ChemotherapeutiC agents. One of these is Calphostin C (CalC), the aCtion of the photo-aCtivated derivative of whiCh, CalC ϕE , has been asCribed to its ability to seleCtively and irreversibly inhibit protein kinase Cs (PKCs). But reCent results of experiments with neoplastiC rat fibroblasts and human breast and uterine Cervix CanCer Cells have revealed that the aCtion of CalC ϕE involves more than PKC inhibition. Besides suppressing PKC aCtivity, CalC ϕE rapidly Causes endoplasmiC retiCulum (ER) stress in breast CanCer Cells and the seleCtive Complete oxidation and proteasomal destruCtion of the funCtionally essential nuClear envelope protein lamin B 1, in human CerviCal CarCinoma (HCC) Cells and neoplastiC rat fibroblasts. When these lamin B1-laCking Cells are plaCed in the dark, CytoplasmiC membrane-linked PKC aCtivities suddenly rebound and apoptogenesis is initiated as indiCated by the immediate release of CytoChrome C from mitoChondria and later on the aCtivation of Caspases. HenCe, CalC ϕE is a photodynamiC CytoCidal agent attaCking multiple targets in CanCer Cells and it would be worth determining, even for their best appliCative use, whether other perylenequinones also share the so far unexpeCtedly Complex deadly properties of the CalC ϕE .
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photoexCited Calphostin C seleCtively destroys nuClear lamin b1 in neoplastiC human and rat Cells a novel meChanism of aCtion of a photodynamiC tumor therapy agent
Biochimica et Biophysica Acta, 2008Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Raffaella Pacchiana, Ilaria Pierpaola Dal PraAbstract:AbstraCt Lamin B1, a major Component of the nuClear lamina, anChors the nuCleus to the Cytoskeletal Cage, and Controls nuClear orientation, Chromosome positioning and, alongside several enzymes, fundamental nuClear funCtions. Exposing polyomavirus-transformed rat pyF111 fibroblasts and human CerviCal CarCinoma (HCC) C4-I Cells for 30 min to photoexCited perylenequinone Calphostin C, i.e. Cal C φE , an established reaCtive oxygen speCies (ROS)-generator and protein kinase C (PKC) inhibitor, Caused the Cells to seleCtively oxidize and then totally destroy their nuClear lamin B1 by only 60 min after starting the treatment, i.e. when apoptotiC Caspases' aCtivities had not yet inCreased. However, while the oxidized lamin B1 was being destroyed, lamins A/C, the lamin A-assoCiated nuClear envelope protein emerin, and the nuCleoplasmiC protein CyClin E were neither oxidized nor destroyed. The oxidized lamin B was ubiquitinated and demolished in the proteasome probably by an enhanCed peptidyl-glutaminase-like aCtivity. HenCe, the Cal C φE -induCed rapid and seleCtive lamin B1 oxidation and proteasomal destruCtion ahead of the aCtivation of apoptotiC Caspases was by itself a most severe moleCular lesion impairing vital nuClear funCtions. Conversely, Cal C direCtly added to the Cells kept in the dark damaged neither nuClear lamin B1 nor Cell viability. Thus, our findings reveal a novel Cell-damaging meChanism of a photodynamiC tumor therapeutiC agent.
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vp 16 etoposide and Calphostin C trigger different nuClear but akin CytoplasmiC patterns of Changes in the distribution and aCtivity of protein kinase C βi in polyomavirus transformed pyf111 rat fibroblasts
International Journal of Molecular Medicine, 2006Co-Authors: Anna Maria Chiarini, J F Whitfield, Ubaldo Armato, Ilaria Pierpaola Dal PraAbstract:Protein kinase C (PKC) isoforms regulate Cell proliferation and apoptosis. SinCe the PKC isoenzyme Complement varies Considerably from Cell type to Cell type, a PKC's responsiveness to an apoptogeniC Challenge must be defined for both the type of apoptogen and the type of Cell. We have already reported that the Changes in the distribution and aCtivity of PKC-delta in apoptosing polyomavirus-infeCted/transformed FisCher rat embryo pyF111 fibroblasts depend on the type of apoptogen. Here, we show that this is also true for PKC-betaI in pyF111 Cells treated with the slow DNA-damaging VP-16 (etoposide) or the fast-aCting (in the Cytoplasm) Calphostin C. These apoptogens Caused quite different shifts of the PKC-betaI level and aCtivity in the nuClear membrane (NM) and nuCleoplasm (NP), but Corresponding Changes in the Cytosol (CS) and CytoplasmiC partiCulate (CP) fraCtions. The hefty transloCation of PKC-betaI onto the CP fraCtion and its inCreased aCtivity there suggest the possible triggering of a CytoChrome C/Caspase-mediated apoptosis-induCing meChanism Common to both agents. The present results are a neCessary lead-up to funCtional proteomiC analyses aimed at identifying the moleCules forming the loCal PKC-betaI signalling modules under different Conditions.
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inCreased aCtivity of the protein kinase C delta holoenzyme in the CytoplasmiC partiCulate fraCtion preCedes the aCtivation of Caspases in polyomavirus transformed pyf111 rat fibroblasts exposed to Calphostin C or topoisomerase ii inhibitors
Experimental Cell Research, 2000Co-Authors: Ilaria Pierpaola Dal Pra, J F Whitfield, Anna Maria Chiarini, Ubaldo ArmatoAbstract:A Caspase-mediated release of the 40-kDa CatalytiC fragment of the delta isoform (CF-delta) of protein kinase C (PKC-delta) is involved in apoptosis, but its aCtual role in apoptosis development is still unknown. In an effort to understand this role, we have used polyomavirus-transformed pyF111 rat fibroblasts, whiCh are hypersusCeptible to apoptosis as they Constitutively hyperexpress PKC-delta, but Cannot make the antiapoptotiC BCl-2 and BCl-X(L) proteins, while making the proapoptotiC Bax protein. Calphostin C is reportedly both a speCifiC inhibitor of PKC-delta aCtivity (C. Keenan, N. Goode, and C. Pears, 1997, FEBS Lett. 415, 101-108) and an effeCtive apoptogen (M. Murata et al., 1997, Cell. Mol. Life SCi. 53, 737-743). Exposure of pyF111 Cells to Calphostin C (75 nM) stimulated the transloCation of the PKC-delta holoenzyme (holo-PKC-delta) onto the CytoplasmiC partiCulate (CP) fraCtion between 15 and 45 min, whiCh was after the release of mitoChondrial CytoChrome C but before the aCtivation of CytoplasmiC DEVD-speCifiC Caspases. The CF-delta fragment started aCCumulating only between 2 and 4 h, while apoptosis oCCurred mostly within 6 h. InCubating pyF111 Cells with the muCh slower aCting, apoptogeniC topoisomerase-II inhibitors etoposide (VP-16) and teniposide (VM-26) also Caused within 6 h a doubling of the CP-bound holo-PKC-delta-related aCtivity but with no signifiCant transloCation of the holoenzyme to the CP fraCtion. Again this oCCurred after the release of CytoChrome C but before the aCtivation of DEVDases and the aCCumulation of the CF-delta. However, while Calphostin C did not affeCt the delta-related aCtivity in the nuClear membrane (NM) and nuCleoplasmiC (NP) fraCtions, VP-16 and VM-26 Caused a prompt, large, and irreversible drop in the delta aCtivity at the NM and a transient surge followed by a fall in the NP-assoCiated aCtivity. HenCe, a surge of CP-anChored holo-PKC-delta aCtivity is a Common part of the signals given by various apoptogeniC drugs to pyF111 Cells. On the other hand, inhibition of delta-related aCtivity, first at the NM and then in the NP fraCtion, is a speCifiC feature only of the signals given by apoptogeniC DNA-damaging agents.
