PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9648916-3 1998 Treatment with 1-10 microM CD resulted in an increased 1) incidence of rounded cells, 2) relative PAI-1 mRNA content, and 3) fraction of PAI-1 protein-expressing cells. Cytochalasin D 27-29 serpin family E member 2 Rattus norvegicus 98-103 10098935-2 1999 Induced transcription of the plasminogen activator inhibitor type-1 (PAI-1) gene in serum-free cultures of normal rat kidney (NRK-52E) cells following disruption of actin microfilament structures with cytochalasin D (CD) provides a simple model to probe mechanisms underlying shape-related expression control. Cytochalasin D 201-215 serpin family E member 2 Rattus norvegicus 29-67 10098935-2 1999 Induced transcription of the plasminogen activator inhibitor type-1 (PAI-1) gene in serum-free cultures of normal rat kidney (NRK-52E) cells following disruption of actin microfilament structures with cytochalasin D (CD) provides a simple model to probe mechanisms underlying shape-related expression control. Cytochalasin D 201-215 serpin family E member 2 Rattus norvegicus 69-74 10098935-2 1999 Induced transcription of the plasminogen activator inhibitor type-1 (PAI-1) gene in serum-free cultures of normal rat kidney (NRK-52E) cells following disruption of actin microfilament structures with cytochalasin D (CD) provides a simple model to probe mechanisms underlying shape-related expression control. Cytochalasin D 217-219 serpin family E member 2 Rattus norvegicus 29-67 10098935-2 1999 Induced transcription of the plasminogen activator inhibitor type-1 (PAI-1) gene in serum-free cultures of normal rat kidney (NRK-52E) cells following disruption of actin microfilament structures with cytochalasin D (CD) provides a simple model to probe mechanisms underlying shape-related expression control. Cytochalasin D 217-219 serpin family E member 2 Rattus norvegicus 69-74 10098935-4 1999 Stimulated expression occurred rapidly (i.e., within 2 h of CD addition), involved increases in both PAI-1 mRNA abundance and de novo protein synthesis, and was dependent upon the concentration of CD used. Cytochalasin D 60-62 serpin family E member 2 Rattus norvegicus 101-106 10098935-4 1999 Stimulated expression occurred rapidly (i.e., within 2 h of CD addition), involved increases in both PAI-1 mRNA abundance and de novo protein synthesis, and was dependent upon the concentration of CD used. Cytochalasin D 197-199 serpin family E member 2 Rattus norvegicus 101-106 10098935-5 1999 A series of culture conditions were designed (e.g., use of bacteriological surfaces, poly-HEMA coated surfaces, maintenance in suspension on agarose) to discriminate cell shape from adhesive influences on CD-stimulated PAI-1 expression. Cytochalasin D 205-207 serpin family E member 2 Rattus norvegicus 219-224 10098935-6 1999 Cytoskeletal disruption, and not simply changes in cell shape, was a critical aspect of CD-mediated PAI-1 expression in NRK cells cultured under serum-free conditions; induced expression was independent of substrate anchorage. Cytochalasin D 88-90 serpin family E member 2 Rattus norvegicus 100-105 10098935-7 1999 Low concentrations of CD (1-2 microM) failed to cause cell arborization or increase either relative PAI-1 mRNA/protein abundance levels suggesting, however, that cell rounding may be a necessary but not sufficient aspect in CD-mediated PAI-1 induction. Cytochalasin D 224-226 serpin family E member 2 Rattus norvegicus 236-241 10098935-8 1999 Transfection of PAI-1 promoter-CAT reporter constructs into NRK cells followed by stimulation with CD or serum additionally indicated that CD-induced PAI-1 expression did not utilize the same functional complement of serum-responsive promoter sequences, thus, further defining differences in the growth factor- and cytoskeletal-mediated pathways of PAI-1 gene regulation. Cytochalasin D 139-141 serpin family E member 2 Rattus norvegicus 16-21 10098935-8 1999 Transfection of PAI-1 promoter-CAT reporter constructs into NRK cells followed by stimulation with CD or serum additionally indicated that CD-induced PAI-1 expression did not utilize the same functional complement of serum-responsive promoter sequences, thus, further defining differences in the growth factor- and cytoskeletal-mediated pathways of PAI-1 gene regulation. Cytochalasin D 139-141 serpin family E member 2 Rattus norvegicus 150-155 10098935-8 1999 Transfection of PAI-1 promoter-CAT reporter constructs into NRK cells followed by stimulation with CD or serum additionally indicated that CD-induced PAI-1 expression did not utilize the same functional complement of serum-responsive promoter sequences, thus, further defining differences in the growth factor- and cytoskeletal-mediated pathways of PAI-1 gene regulation. Cytochalasin D 139-141 serpin family E member 2 Rattus norvegicus 150-155 2332454-0 1990 p52 induction by cytochalasin D in rat kidney fibroblasts: homologies between p52 and plasminogen activator inhibitor type-1. Cytochalasin D 17-31 serpin family E member 2 Rattus norvegicus 86-124 9648916-3 1998 Treatment with 1-10 microM CD resulted in an increased 1) incidence of rounded cells, 2) relative PAI-1 mRNA content, and 3) fraction of PAI-1 protein-expressing cells. Cytochalasin D 27-29 serpin family E member 2 Rattus norvegicus 137-142 9648916-5 1998 Maximal levels of induced PAI-1 transcripts (18-fold that of control) occurred 4 hours post-CD addition and declined thereafter but remained elevated (by at least tenfold) for 24 hours. Cytochalasin D 92-94 serpin family E member 2 Rattus norvegicus 26-31 9648916-6 1998 Assessment of the metabolic requirements for CD-induced PAI-1 expression by using the protein synthesis inhibitors puromycin and cycloheximide indicated that PAI-1 transcripts were regulated in a complex manner in response to CD. Cytochalasin D 45-47 serpin family E member 2 Rattus norvegicus 56-61 9648916-6 1998 Assessment of the metabolic requirements for CD-induced PAI-1 expression by using the protein synthesis inhibitors puromycin and cycloheximide indicated that PAI-1 transcripts were regulated in a complex manner in response to CD. Cytochalasin D 45-47 serpin family E member 2 Rattus norvegicus 158-163 9648916-6 1998 Assessment of the metabolic requirements for CD-induced PAI-1 expression by using the protein synthesis inhibitors puromycin and cycloheximide indicated that PAI-1 transcripts were regulated in a complex manner in response to CD. Cytochalasin D 226-228 serpin family E member 2 Rattus norvegicus 56-61 9648916-6 1998 Assessment of the metabolic requirements for CD-induced PAI-1 expression by using the protein synthesis inhibitors puromycin and cycloheximide indicated that PAI-1 transcripts were regulated in a complex manner in response to CD. Cytochalasin D 226-228 serpin family E member 2 Rattus norvegicus 158-163 9648916-9 1998 Relative abundance of PAI-1 transcripts in suspended cells cultured in the presence of CD, however, closely approximated that of plastic-adherent, CD-treated cells (13-fold over control). Cytochalasin D 87-89 serpin family E member 2 Rattus norvegicus 22-27 9648916-12 1998 A protein tyrosine kinase is likely involved in the CD-mediated signal-transduction cascade, since induced PAI-1 expression can be down-regulated by genistein and herbimycin A but not by calphostin C or tyrphostin B46. Cytochalasin D 52-54 serpin family E member 2 Rattus norvegicus 107-112 1471975-1 1992 The microfilament-disrupting agent cytochalasin D (CD) increased (by 10-22-fold) the synthesis de novo and extracellular matrix deposition of plasminogen-activator inhibitor type-1 [p52(PAI-1)] in normal rat kidney (NRK) cells. Cytochalasin D 35-49 serpin family E member 2 Rattus norvegicus 142-180 1471975-1 1992 The microfilament-disrupting agent cytochalasin D (CD) increased (by 10-22-fold) the synthesis de novo and extracellular matrix deposition of plasminogen-activator inhibitor type-1 [p52(PAI-1)] in normal rat kidney (NRK) cells. Cytochalasin D 51-53 serpin family E member 2 Rattus norvegicus 142-180 1599429-11 1992 Like actin, CD-induced p52(PAI-1) synthesis, cellular content, and partitioning to the detergent-insoluble cytoskeletal compartment reflected a corresponding increase in p52(PAI-1) mRNA. Cytochalasin D 12-14 serpin family E member 2 Rattus norvegicus 27-32 1599429-11 1992 Like actin, CD-induced p52(PAI-1) synthesis, cellular content, and partitioning to the detergent-insoluble cytoskeletal compartment reflected a corresponding increase in p52(PAI-1) mRNA. Cytochalasin D 12-14 serpin family E member 2 Rattus norvegicus 174-179 1599429-13 1992 p52(PAI-1) expression in the NRK-cell system is thus responsive to CD-mediated shape changes and requires ongoing RNA synthesis for its induction. Cytochalasin D 67-69 serpin family E member 2 Rattus norvegicus 4-9