PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6284819-1 1981 We have examined the regulation of two key enzymes that control polyamine biosynthesis-L-ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC) - by agents increasing cAMP in S49 lymphoma cells. Polyamines 64-73 S-adenosylmethionine decarboxylase 1 Mus musculus 123-157 3178757-5 1988 Addition of either spermidine or spermine to the cells treated with the AdoMetDC inhibitors led to a decrease in ODC activity, indicating that either polyamine can bring about this effect, but spermidine produced effects at concentrations similar to those found in the control cells and appears to be the physiologically important regulator. Polyamines 150-159 S-adenosylmethionine decarboxylase 1 Mus musculus 72-80 3663117-6 1987 These results demonstrate the importance of cellular spermine concentrations in regulating the activity of AdoMetDC, which is a key enzyme controlling polyamine synthesis. Polyamines 151-160 S-adenosylmethionine decarboxylase 1 Mus musculus 107-115 22610166-2 2012 Tumor promoter treatment induces the rate-limiting enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC), and S-adenosylmethionine decarboxylase (AdoMetDC), and targeted ODC overexpression is sufficient for tumor promotion in initiated mouse skin. Polyamines 62-71 S-adenosylmethionine decarboxylase 1 Mus musculus 157-165 29566247-7 2018 Comparative gene expression analysis reveals that S-Adenosylmethionine decarboxylase (Amd1) and Spermine oxidase (Smox), two components of polyamine pathway metabolism, are downregulated in the TA but not in the triceps of dy2j/dy2j mice. Polyamines 139-148 S-adenosylmethionine decarboxylase 1 Mus musculus 86-90 22610166-11 2012 AdoMetDC-expressing mice will enable more refined spatial and temporal manipulation of polyamine biosynthesis during tumorigenesis and in other models of human disease. Polyamines 87-96 S-adenosylmethionine decarboxylase 1 Mus musculus 0-8 21742865-5 2011 A yeast-two-hybrid screen showed that HtpB interacted with S-adenosylmethionine decarboxylase (SAMDC), an essential yeast enzyme (encoded by SPE2) that is required for polyamine biosynthesis. Polyamines 168-177 S-adenosylmethionine decarboxylase 1 Mus musculus 95-100 21809077-7 2012 CAG-SpdS/MHC-AdoMetDC bitransgenic animals were produced at the expected frequency and exhibited cardiac polyamine levels comparable to MHC-AdoMetDC littermates. Polyamines 105-114 S-adenosylmethionine decarboxylase 1 Mus musculus 13-21 21742865-7 2011 A pharmacological inhibitor of SAMDC significantly reduced L. pneumophila replication in L929 mouse cells and U937 macrophages, whereas exogenously added polyamines moderately favored intracellular growth, confirming that polyamines and host SAMDC activity promote L. pneumophila proliferation. Polyamines 222-232 S-adenosylmethionine decarboxylase 1 Mus musculus 31-36 21742865-8 2011 Bioinformatic analysis revealed that most known enzymes required for polyamine biosynthesis in bacteria (including SAMDC) are absent in L. pneumophila, further suggesting a need for exogenous polyamines. Polyamines 69-78 S-adenosylmethionine decarboxylase 1 Mus musculus 115-120 21742865-8 2011 Bioinformatic analysis revealed that most known enzymes required for polyamine biosynthesis in bacteria (including SAMDC) are absent in L. pneumophila, further suggesting a need for exogenous polyamines. Polyamines 192-202 S-adenosylmethionine decarboxylase 1 Mus musculus 115-120 18390925-6 2008 Real-time PCR confirms that expression of genes encoding polyamine biosynthetic enzymes, ornithine decarboxylase (Odc1), and S-adenosylmethionine decarboxylase (Amd1), is reduced in ARKO muscle, suggesting androgens act through regulation of polyamine biosynthesis. Polyamines 57-66 S-adenosylmethionine decarboxylase 1 Mus musculus 161-165 18390925-6 2008 Real-time PCR confirms that expression of genes encoding polyamine biosynthetic enzymes, ornithine decarboxylase (Odc1), and S-adenosylmethionine decarboxylase (Amd1), is reduced in ARKO muscle, suggesting androgens act through regulation of polyamine biosynthesis. Polyamines 242-251 S-adenosylmethionine decarboxylase 1 Mus musculus 161-165 16423999-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the synthesis of polyamines essential for cell growth and proliferation. Polyamines 82-92 S-adenosylmethionine decarboxylase 1 Mus musculus 0-34 17371283-3 2007 The enzymes ODC (ornithine decarboxylase), AdoMetDC (S-adenosylmethionine decarboxylase) and SSAT (spermidine/spermine N(1)-acetyltransferase) are critical for polyamine pool maintenance. Polyamines 160-169 S-adenosylmethionine decarboxylase 1 Mus musculus 43-51 17371283-3 2007 The enzymes ODC (ornithine decarboxylase), AdoMetDC (S-adenosylmethionine decarboxylase) and SSAT (spermidine/spermine N(1)-acetyltransferase) are critical for polyamine pool maintenance. Polyamines 160-169 S-adenosylmethionine decarboxylase 1 Mus musculus 53-87 17371283-8 2007 We found that this cross-talk modulated the expression of ODC and AdoMetDC, enzymes limiting polyamine biosynthesis, but not SSAT. Polyamines 93-102 S-adenosylmethionine decarboxylase 1 Mus musculus 66-74 16423999-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the synthesis of polyamines essential for cell growth and proliferation. Polyamines 82-92 S-adenosylmethionine decarboxylase 1 Mus musculus 36-44 11235918-3 2001 The present study demonstrates a novel link between alterations in phorbol ester tumour promoter mediated regulation during malignant conversion and the expression of ornithine decarboxylase and S-adenosylmethionine decarboxylase, key rate-limiting and regulatory activities in the biosynthesis of polyamines. Polyamines 298-308 S-adenosylmethionine decarboxylase 1 Mus musculus 195-229 16153183-1 2006 The present study was designed to provide a better understanding of the role played by AdoMetDC (S-adenosylmethionine decarboxylase), the key rate-controlling enzyme in the synthesis of spermidine and spermine, in controlling polyamine levels and the importance of polyamines in cardiac physiology. Polyamines 226-235 S-adenosylmethionine decarboxylase 1 Mus musculus 87-95 16153183-1 2006 The present study was designed to provide a better understanding of the role played by AdoMetDC (S-adenosylmethionine decarboxylase), the key rate-controlling enzyme in the synthesis of spermidine and spermine, in controlling polyamine levels and the importance of polyamines in cardiac physiology. Polyamines 226-235 S-adenosylmethionine decarboxylase 1 Mus musculus 97-131 16153183-1 2006 The present study was designed to provide a better understanding of the role played by AdoMetDC (S-adenosylmethionine decarboxylase), the key rate-controlling enzyme in the synthesis of spermidine and spermine, in controlling polyamine levels and the importance of polyamines in cardiac physiology. Polyamines 265-275 S-adenosylmethionine decarboxylase 1 Mus musculus 87-95 16153183-1 2006 The present study was designed to provide a better understanding of the role played by AdoMetDC (S-adenosylmethionine decarboxylase), the key rate-controlling enzyme in the synthesis of spermidine and spermine, in controlling polyamine levels and the importance of polyamines in cardiac physiology. Polyamines 265-275 S-adenosylmethionine decarboxylase 1 Mus musculus 97-131 15604241-1 2004 Adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of polyamines, is often up-regulated in cancers. Polyamines 81-91 S-adenosylmethionine decarboxylase 1 Mus musculus 0-32 15604241-1 2004 Adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of polyamines, is often up-regulated in cancers. Polyamines 81-91 S-adenosylmethionine decarboxylase 1 Mus musculus 34-42 12545203-4 2002 Catecholamine depletion evoked by reserpine drastically decreases the folate-induced activity of S-adenosylmethionine decarboxylase (AdoMetDC), which limits polyamine biosynthesis, but has no effect on SSAT activity augmented by CB 3717. Polyamines 157-166 S-adenosylmethionine decarboxylase 1 Mus musculus 97-131 12545203-4 2002 Catecholamine depletion evoked by reserpine drastically decreases the folate-induced activity of S-adenosylmethionine decarboxylase (AdoMetDC), which limits polyamine biosynthesis, but has no effect on SSAT activity augmented by CB 3717. Polyamines 157-166 S-adenosylmethionine decarboxylase 1 Mus musculus 133-141 11235918-10 2001 The status of the cellular polyamine levels was also an important determinant of the PMA-mediated alterations that occurred in ODC and in SAMDC expression in these H-ras transformed cells. Polyamines 27-36 S-adenosylmethionine decarboxylase 1 Mus musculus 138-143 9615732-1 1998 Polyamines and their biosynthetic enzymes, such as ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are crucial for normal and neoplastic cell growth and differentiation. Polyamines 0-10 S-adenosylmethionine decarboxylase 1 Mus musculus 85-119 11114236-4 2000 When a sub-G(1)peak appeared at 4 h after dexamethasone treatment, the activity of the polyamine catabolic enzyme spermidine/spermine N(1)-acetyltransferase (SSAT) was significantly increased and the activity of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC) was significantly decreased compared to the activities found in the thymi of control mice. Polyamines 87-96 S-adenosylmethionine decarboxylase 1 Mus musculus 246-280 11114236-4 2000 When a sub-G(1)peak appeared at 4 h after dexamethasone treatment, the activity of the polyamine catabolic enzyme spermidine/spermine N(1)-acetyltransferase (SSAT) was significantly increased and the activity of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC) was significantly decreased compared to the activities found in the thymi of control mice. Polyamines 87-96 S-adenosylmethionine decarboxylase 1 Mus musculus 282-290 11455586-1 2001 The hypothesis that H-ras transformed cells contain alterations in signalling pathways important in controlling the expression of S-adenosylmethionine decarboxylase, (SAMDC) a highly regulated activity in the biosynthesis of polyamines was tested. Polyamines 225-235 S-adenosylmethionine decarboxylase 1 Mus musculus 167-172 10570962-7 1999 Lower concentrations of polyamines affect both stimulation and inhibition of AdoMetDC synthesis, through the uORF in the mRNA, than affect general protein synthesis. Polyamines 24-34 S-adenosylmethionine decarboxylase 1 Mus musculus 77-85 10430664-1 1999 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of polyamines. Polyamines 85-95 S-adenosylmethionine decarboxylase 1 Mus musculus 0-34 10430664-1 1999 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of polyamines. Polyamines 85-95 S-adenosylmethionine decarboxylase 1 Mus musculus 36-44 9615732-1 1998 Polyamines and their biosynthetic enzymes, such as ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are crucial for normal and neoplastic cell growth and differentiation. Polyamines 0-10 S-adenosylmethionine decarboxylase 1 Mus musculus 121-129 9133651-1 1997 The competitive S-adenosylmethionine decarboxylase (SAMdc; EC 4.1.1.50) inhibitor 4-amidinoindan-1-one 2"-amidinohydrazone (CGP 48664A) inhibits growth more effectively than the irreversible SAMdc inhibitor 5"-[[(Z)-4-amino-2-butenyl]methylamino]-5"-deoxyadenosine (AbeAdo), while having similar effects on polyamine contents. Polyamines 307-316 S-adenosylmethionine decarboxylase 1 Mus musculus 16-50 9133651-1 1997 The competitive S-adenosylmethionine decarboxylase (SAMdc; EC 4.1.1.50) inhibitor 4-amidinoindan-1-one 2"-amidinohydrazone (CGP 48664A) inhibits growth more effectively than the irreversible SAMdc inhibitor 5"-[[(Z)-4-amino-2-butenyl]methylamino]-5"-deoxyadenosine (AbeAdo), while having similar effects on polyamine contents. Polyamines 307-316 S-adenosylmethionine decarboxylase 1 Mus musculus 52-57 7634128-1 1995 S-adenosylmethionine decarboxylase (AdoMetDC), one of three key enzymes in polyamine biosynthesis, is present in minute concentrations in adult tissues, whereas increased AdoMetDC activity occurs in conjunction with differentiation and growth. Polyamines 75-84 S-adenosylmethionine decarboxylase 1 Mus musculus 0-34 9027363-7 1997 The cellular uptake of polyamines in the liver from tg+ mice showed an increase and considerable changes were observed in the activity of ornithine decarboxylase (ODC) in the liver and kidney and S-adenosylmethionine decarboxylase (AdoMetDC) in the liver. Polyamines 23-33 S-adenosylmethionine decarboxylase 1 Mus musculus 196-230 9027363-7 1997 The cellular uptake of polyamines in the liver from tg+ mice showed an increase and considerable changes were observed in the activity of ornithine decarboxylase (ODC) in the liver and kidney and S-adenosylmethionine decarboxylase (AdoMetDC) in the liver. Polyamines 23-33 S-adenosylmethionine decarboxylase 1 Mus musculus 232-240 9078276-1 1997 Mammalian S-adenosylmethionine decarboxylase (AdoMetDC) catalyses a regulatory important step in the biosynthesis of polyamines and is a potential target for therapeutic agents against various parasitic diseases and proliferative disorders. Polyamines 117-127 S-adenosylmethionine decarboxylase 1 Mus musculus 10-44 9078276-1 1997 Mammalian S-adenosylmethionine decarboxylase (AdoMetDC) catalyses a regulatory important step in the biosynthesis of polyamines and is a potential target for therapeutic agents against various parasitic diseases and proliferative disorders. Polyamines 117-127 S-adenosylmethionine decarboxylase 1 Mus musculus 46-54 7634128-1 1995 S-adenosylmethionine decarboxylase (AdoMetDC), one of three key enzymes in polyamine biosynthesis, is present in minute concentrations in adult tissues, whereas increased AdoMetDC activity occurs in conjunction with differentiation and growth. Polyamines 75-84 S-adenosylmethionine decarboxylase 1 Mus musculus 36-44 8232285-3 1993 S-Adenosylmethionine decarboxylase (AdoMetDC) catalyzes a key step in the polyamine biosynthetic pathway. Polyamines 74-83 S-adenosylmethionine decarboxylase 1 Mus musculus 0-34 8232285-12 1993 The present results indicate that analogs of MGBG, having a greater specificity against AdoMetDC, might be valuable for studies concerning polyamines and cell proliferation. Polyamines 139-149 S-adenosylmethionine decarboxylase 1 Mus musculus 88-96 8232285-3 1993 S-Adenosylmethionine decarboxylase (AdoMetDC) catalyzes a key step in the polyamine biosynthetic pathway. Polyamines 74-83 S-adenosylmethionine decarboxylase 1 Mus musculus 36-44 8461048-2 1993 However, in the present study, we demonstrate that aminoguanidine, besides affecting the degradation of polyamines, may affect one of the important regulatory enzymes in the biosynthesis of polyamines, namely S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 104-114 S-adenosylmethionine decarboxylase 1 Mus musculus 209-243 8319678-3 1993 One of the key steps in the polyamine biosynthetic pathway is catalyzed by S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 28-37 S-adenosylmethionine decarboxylase 1 Mus musculus 75-109 8319678-3 1993 One of the key steps in the polyamine biosynthetic pathway is catalyzed by S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 28-37 S-adenosylmethionine decarboxylase 1 Mus musculus 111-119 8484773-0 1993 Polyamine regulation of S-adenosylmethionine decarboxylase synthesis through the 5"-untranslated region of its mRNA. Polyamines 0-9 S-adenosylmethionine decarboxylase 1 Mus musculus 24-58 8484773-1 1993 The effect of the 5"-untranslated region (5"-UTR) of S-adenosylmethionine decarboxylase (SAMDC) mRNA and of polyamines on the translation of SAMDC mRNA was studied in a rabbit reticulocyte cell-free system. Polyamines 108-118 S-adenosylmethionine decarboxylase 1 Mus musculus 141-146 8484773-2 1993 Using synthetic SAMDC mRNAs possessing different sizes of 5"-UTR, it was shown that nucleotides in the 5"-end of 5"-UTR were responsible for polyamine inhibition at high concentrations. Polyamines 141-150 S-adenosylmethionine decarboxylase 1 Mus musculus 16-21 8484773-4 1993 When poly(A)+ RNA from mouse SAMDC-overproducing cells was used as mRNA, the degree of polyamine inhibition at high concentrations was nearly the same, but that of polyamine stimulation at low concentrations was greater than with synthetic SAMDC mRNAs. Polyamines 87-96 S-adenosylmethionine decarboxylase 1 Mus musculus 29-34 8484773-4 1993 When poly(A)+ RNA from mouse SAMDC-overproducing cells was used as mRNA, the degree of polyamine inhibition at high concentrations was nearly the same, but that of polyamine stimulation at low concentrations was greater than with synthetic SAMDC mRNAs. Polyamines 164-173 S-adenosylmethionine decarboxylase 1 Mus musculus 29-34 8461048-2 1993 However, in the present study, we demonstrate that aminoguanidine, besides affecting the degradation of polyamines, may affect one of the important regulatory enzymes in the biosynthesis of polyamines, namely S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 104-114 S-adenosylmethionine decarboxylase 1 Mus musculus 245-253 8461048-2 1993 However, in the present study, we demonstrate that aminoguanidine, besides affecting the degradation of polyamines, may affect one of the important regulatory enzymes in the biosynthesis of polyamines, namely S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 190-200 S-adenosylmethionine decarboxylase 1 Mus musculus 209-243 8461048-2 1993 However, in the present study, we demonstrate that aminoguanidine, besides affecting the degradation of polyamines, may affect one of the important regulatory enzymes in the biosynthesis of polyamines, namely S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 190-200 S-adenosylmethionine decarboxylase 1 Mus musculus 245-253 1449493-4 1992 The polyamines, spermidine and spermine, have been shown to inhibit AdoMetDC mRNA translation. Polyamines 4-14 S-adenosylmethionine decarboxylase 1 Mus musculus 68-76 1958536-1 1991 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine biosynthesis. Polyamines 103-112 S-adenosylmethionine decarboxylase 1 Mus musculus 34-68 1958536-1 1991 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine biosynthesis. Polyamines 103-112 S-adenosylmethionine decarboxylase 1 Mus musculus 70-78