PubMed:11712085 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":27,"end":41},"obj":"protein"},{"id":"T2","span":{"begin":85,"end":99},"obj":"protein"},{"id":"T3","span":{"begin":101,"end":104},"obj":"protein"},{"id":"T4","span":{"begin":184,"end":187},"obj":"protein"},{"id":"T5","span":{"begin":239,"end":250},"obj":"protein"},{"id":"T6","span":{"begin":252,"end":256},"obj":"protein"},{"id":"T7","span":{"begin":262,"end":295},"obj":"protein"},{"id":"T8","span":{"begin":297,"end":301},"obj":"protein"},{"id":"T9","span":{"begin":304,"end":308},"obj":"protein"},{"id":"T10","span":{"begin":327,"end":358},"obj":"protein"},{"id":"T11","span":{"begin":374,"end":377},"obj":"protein"},{"id":"T12","span":{"begin":487,"end":523},"obj":"protein"},{"id":"T13","span":{"begin":525,"end":530},"obj":"protein"},{"id":"T14","span":{"begin":617,"end":621},"obj":"protein"},{"id":"T15","span":{"begin":716,"end":762},"obj":"protein"},{"id":"T16","span":{"begin":795,"end":798},"obj":"protein"},{"id":"T17","span":{"begin":853,"end":856},"obj":"protein"},{"id":"T18","span":{"begin":993,"end":997},"obj":"protein"},{"id":"T19","span":{"begin":999,"end":1003},"obj":"protein"},{"id":"T20","span":{"begin":1008,"end":1017},"obj":"protein"},{"id":"T21","span":{"begin":1019,"end":1022},"obj":"protein"},{"id":"T22","span":{"begin":1044,"end":1058},"obj":"protein"},{"id":"T23","span":{"begin":1173,"end":1176},"obj":"protein"},{"id":"T24","span":{"begin":1336,"end":1339},"obj":"protein"},{"id":"T25","span":{"begin":1361,"end":1364},"obj":"protein"},{"id":"T26","span":{"begin":1395,"end":1403},"obj":"protein"},{"id":"T27","span":{"begin":1497,"end":1500},"obj":"protein"},{"id":"T28","span":{"begin":1505,"end":1510},"obj":"protein"},{"id":"T29","span":{"begin":1587,"end":1590},"obj":"protein"},{"id":"T30","span":{"begin":1729,"end":1732},"obj":"protein"}],"text":"Expression and function of adrenomedullin and its receptors in Conn's adenoma cells.\nAdrenomedullin (ADM) is a hypotensive peptide, that derives from the proteolytic cleavage of pro(p)ADM and acts through two subtypes of receptors, called L1-receptor (L1-R) and calcitonin receptor-like receptor (CRLR). CRLR may function as a calcitonin gene-related peptide or a selective ADM receptor depending on the expression of the subtype 1 or the subtypes 2 and 3 of a family of proteins, named receptor-activity modifying proteins (RAMPs). Reverse transcription (RT)-polymerase chain reaction (PCR) allowed the detection of pADM mRNA in dispersed cells of eight Conn's adenomas (aldosteronomas). These cells also expressed peptidyl-glycine alpha-amidating monooxigenase, the enzyme converting immature ADM to the mature form, and contained sizeable amounts of ADM-immunoreactivity as measured by radioimmunoassay. RT-PCR also demonstrated the presence in aldosteronoma cells of the specific mRNAs of L1-R, CRLR and RAMPs 1-3. ADM (10(-8) M) inhibited angiotensin-II (10(-9) M)-simulated aldosterone secretion from cultured aldosteronoma cells, without affecting basal production. ADM (10(-8) M) also enhanced basal proliferation rate of cultured cells, as estimated by the 5-bromo-2'-deoxyuridine immunocytochemical technique. Both effects of ADM were annulled by the ADM-receptor selective antagonist ADM22-52 (10(-7) M). In conclusion, our study provides evidence that aldosteronoma cells express both ADM and ADM22-52-sensitive receptors. These findings, coupled with the demonstration that ADM exerts an aldosterone antisecretagogue action and a proliferogenic effect on cultured aldosteronoma cells, make it likely that endogenous ADM system plays a potentially important role in the paracrine or autocrine functional control of Conn's adenomas."}

{"project":"PIR-corpus2","denotations":[{"id":"T1","span":{"begin":27,"end":41},"obj":"protein"},{"id":"T2","span":{"begin":50,"end":59},"obj":"protein"},{"id":"T3","span":{"begin":86,"end":105},"obj":"protein"},{"id":"T4","span":{"begin":111,"end":130},"obj":"protein"},{"id":"T5","span":{"begin":178,"end":187},"obj":"protein"},{"id":"T6","span":{"begin":221,"end":230},"obj":"protein"},{"id":"T7","span":{"begin":239,"end":257},"obj":"protein"},{"id":"T8","span":{"begin":262,"end":295},"obj":"protein"},{"id":"T9","span":{"begin":304,"end":308},"obj":"protein"},{"id":"T10","span":{"begin":327,"end":358},"obj":"protein"},{"id":"T11","span":{"begin":364,"end":386},"obj":"protein"},{"id":"T12","span":{"begin":487,"end":504},"obj":"protein"},{"id":"T13","span":{"begin":617,"end":621},"obj":"protein"},{"id":"T14","span":{"begin":716,"end":762},"obj":"protein"},{"id":"T15","span":{"begin":786,"end":798},"obj":"protein"},{"id":"T16","span":{"begin":853,"end":856},"obj":"protein"},{"id":"T17","span":{"begin":993,"end":997},"obj":"protein"},{"id":"T18","span":{"begin":999,"end":1003},"obj":"protein"},{"id":"T19","span":{"begin":1008,"end":1015},"obj":"protein"},{"id":"T20","span":{"begin":1019,"end":1022},"obj":"protein"},{"id":"T21","span":{"begin":1044,"end":1058},"obj":"protein"},{"id":"T22","span":{"begin":1173,"end":1176},"obj":"protein"},{"id":"T23","span":{"begin":1336,"end":1339},"obj":"protein"},{"id":"T24","span":{"begin":1361,"end":1373},"obj":"protein"},{"id":"T25","span":{"begin":1497,"end":1500},"obj":"protein"},{"id":"T26","span":{"begin":1524,"end":1533},"obj":"protein"},{"id":"T27","span":{"begin":1587,"end":1590},"obj":"protein"},{"id":"T28","span":{"begin":1729,"end":1732},"obj":"protein"}],"text":"Expression and function of adrenomedullin and its receptors in Conn's adenoma cells.\nAdrenomedullin (ADM) is a hypotensive peptide, that derives from the proteolytic cleavage of pro(p)ADM and acts through two subtypes of receptors, called L1-receptor (L1-R) and calcitonin receptor-like receptor (CRLR). CRLR may function as a calcitonin gene-related peptide or a selective ADM receptor depending on the expression of the subtype 1 or the subtypes 2 and 3 of a family of proteins, named receptor-activity modifying proteins (RAMPs). Reverse transcription (RT)-polymerase chain reaction (PCR) allowed the detection of pADM mRNA in dispersed cells of eight Conn's adenomas (aldosteronomas). These cells also expressed peptidyl-glycine alpha-amidating monooxigenase, the enzyme converting immature ADM to the mature form, and contained sizeable amounts of ADM-immunoreactivity as measured by radioimmunoassay. RT-PCR also demonstrated the presence in aldosteronoma cells of the specific mRNAs of L1-R, CRLR and RAMPs 1-3. ADM (10(-8) M) inhibited angiotensin-II (10(-9) M)-simulated aldosterone secretion from cultured aldosteronoma cells, without affecting basal production. ADM (10(-8) M) also enhanced basal proliferation rate of cultured cells, as estimated by the 5-bromo-2'-deoxyuridine immunocytochemical technique. Both effects of ADM were annulled by the ADM-receptor selective antagonist ADM22-52 (10(-7) M). In conclusion, our study provides evidence that aldosteronoma cells express both ADM and ADM22-52-sensitive receptors. These findings, coupled with the demonstration that ADM exerts an aldosterone antisecretagogue action and a proliferogenic effect on cultured aldosteronoma cells, make it likely that endogenous ADM system plays a potentially important role in the paracrine or autocrine functional control of Conn's adenomas."}

{"project":"PIR-corpus1","denotations":[{"id":"T1","span":{"begin":27,"end":41},"obj":"protein"},{"id":"T2","span":{"begin":50,"end":59},"obj":"protein"},{"id":"T3","span":{"begin":86,"end":99},"obj":"protein"},{"id":"T4","span":{"begin":101,"end":104},"obj":"acronym"},{"id":"T5","span":{"begin":123,"end":130},"obj":"protein"},{"id":"T6","span":{"begin":178,"end":187},"obj":"protein"},{"id":"T7","span":{"begin":221,"end":230},"obj":"protein"},{"id":"T8","span":{"begin":239,"end":250},"obj":"protein"},{"id":"T9","span":{"begin":252,"end":256},"obj":"acronym"},{"id":"T10","span":{"begin":262,"end":295},"obj":"protein"},{"id":"T11","span":{"begin":297,"end":301},"obj":"acronym"},{"id":"T12","span":{"begin":304,"end":308},"obj":"protein"},{"id":"T13","span":{"begin":327,"end":358},"obj":"protein"},{"id":"T14","span":{"begin":374,"end":386},"obj":"protein"},{"id":"T15","span":{"begin":471,"end":479},"obj":"protein"},{"id":"T16","span":{"begin":487,"end":504},"obj":"protein"},{"id":"T17","span":{"begin":525,"end":530},"obj":"acronym"},{"id":"T18","span":{"begin":716,"end":762},"obj":"protein"},{"id":"T19","span":{"begin":768,"end":774},"obj":"protein"},{"id":"T20","span":{"begin":795,"end":798},"obj":"protein"},{"id":"T21","span":{"begin":806,"end":817},"obj":"protein"},{"id":"T22","span":{"begin":993,"end":997},"obj":"protein"},{"id":"T23","span":{"begin":999,"end":1003},"obj":"protein"},{"id":"T24","span":{"begin":1008,"end":1017},"obj":"compound-protein"},{"id":"T25","span":{"begin":1019,"end":1022},"obj":"protein"},{"id":"T26","span":{"begin":1044,"end":1058},"obj":"protein"},{"id":"T27","span":{"begin":1173,"end":1176},"obj":"protein"},{"id":"T28","span":{"begin":1336,"end":1339},"obj":"protein"},{"id":"T29","span":{"begin":1497,"end":1500},"obj":"protein"},{"id":"T30","span":{"begin":1524,"end":1533},"obj":"protein"},{"id":"T31","span":{"begin":1587,"end":1590},"obj":"protein"},{"id":"T32","span":{"begin":1729,"end":1732},"obj":"protein"}],"text":"Expression and function of adrenomedullin and its receptors in Conn's adenoma cells.\nAdrenomedullin (ADM) is a hypotensive peptide, that derives from the proteolytic cleavage of pro(p)ADM and acts through two subtypes of receptors, called L1-receptor (L1-R) and calcitonin receptor-like receptor (CRLR). CRLR may function as a calcitonin gene-related peptide or a selective ADM receptor depending on the expression of the subtype 1 or the subtypes 2 and 3 of a family of proteins, named receptor-activity modifying proteins (RAMPs). Reverse transcription (RT)-polymerase chain reaction (PCR) allowed the detection of pADM mRNA in dispersed cells of eight Conn's adenomas (aldosteronomas). These cells also expressed peptidyl-glycine alpha-amidating monooxigenase, the enzyme converting immature ADM to the mature form, and contained sizeable amounts of ADM-immunoreactivity as measured by radioimmunoassay. RT-PCR also demonstrated the presence in aldosteronoma cells of the specific mRNAs of L1-R, CRLR and RAMPs 1-3. ADM (10(-8) M) inhibited angiotensin-II (10(-9) M)-simulated aldosterone secretion from cultured aldosteronoma cells, without affecting basal production. ADM (10(-8) M) also enhanced basal proliferation rate of cultured cells, as estimated by the 5-bromo-2'-deoxyuridine immunocytochemical technique. Both effects of ADM were annulled by the ADM-receptor selective antagonist ADM22-52 (10(-7) M). In conclusion, our study provides evidence that aldosteronoma cells express both ADM and ADM22-52-sensitive receptors. These findings, coupled with the demonstration that ADM exerts an aldosterone antisecretagogue action and a proliferogenic effect on cultured aldosteronoma cells, make it likely that endogenous ADM system plays a potentially important role in the paracrine or autocrine functional control of Conn's adenomas."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":27,"end":41},"obj":"gene:133"},{"id":"T1","span":{"begin":70,"end":77},"obj":"disease:C0001430"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Expression and function of adrenomedullin and its receptors in Conn's adenoma cells.\nAdrenomedullin (ADM) is a hypotensive peptide, that derives from the proteolytic cleavage of pro(p)ADM and acts through two subtypes of receptors, called L1-receptor (L1-R) and calcitonin receptor-like receptor (CRLR). CRLR may function as a calcitonin gene-related peptide or a selective ADM receptor depending on the expression of the subtype 1 or the subtypes 2 and 3 of a family of proteins, named receptor-activity modifying proteins (RAMPs). Reverse transcription (RT)-polymerase chain reaction (PCR) allowed the detection of pADM mRNA in dispersed cells of eight Conn's adenomas (aldosteronomas). These cells also expressed peptidyl-glycine alpha-amidating monooxigenase, the enzyme converting immature ADM to the mature form, and contained sizeable amounts of ADM-immunoreactivity as measured by radioimmunoassay. RT-PCR also demonstrated the presence in aldosteronoma cells of the specific mRNAs of L1-R, CRLR and RAMPs 1-3. ADM (10(-8) M) inhibited angiotensin-II (10(-9) M)-simulated aldosterone secretion from cultured aldosteronoma cells, without affecting basal production. ADM (10(-8) M) also enhanced basal proliferation rate of cultured cells, as estimated by the 5-bromo-2'-deoxyuridine immunocytochemical technique. Both effects of ADM were annulled by the ADM-receptor selective antagonist ADM22-52 (10(-7) M). In conclusion, our study provides evidence that aldosteronoma cells express both ADM and ADM22-52-sensitive receptors. These findings, coupled with the demonstration that ADM exerts an aldosterone antisecretagogue action and a proliferogenic effect on cultured aldosteronoma cells, make it likely that endogenous ADM system plays a potentially important role in the paracrine or autocrine functional control of Conn's adenomas."}