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| RAHMAN,ASIM; ALAM,MAHMOOD; RAO,SUDHA; CAI,LIN; LUTHER T.,CLARK; SHAFIQ,SAYID; SIDDIQUI,M.A.Q. |
| Doxorubicin (Dox) is a potent anti-cancer agent with cardiotoxic side-effects but the mechanism of its cardiotoxicity and its effect on expression of the vasoactive atrial natriuretic peptide (ANP), an important marker for cardiac hypertrophy, are little understood. The present study examined Dox-induced changes in vivo in hearts of 6 mongrel dogs and 5 Sprague-Dawley rats and in vitro in cardiac cultures of neonatal rats. Quantitative RT-PCR analysis using g32-p labeled primers for ß-actin, phospholamban (PLB) and ANP showed a selective 5-fold increase of ANP mRNA in Dox-treated dog hearts in comparison to controls. Similarly, northern analysis of GAPD, ß-actin, cardiac a-actin and ANP gave a selective 4.5-fold increase in ANP transcripts in Dox-treated... |
| Tipo: Journal article |
Palavras-chave: Atrial natriuretic peptide; Gene expression; Adriamycin; Heart failure. |
| Ano: 2001 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602001000300007 |
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| We determined whether ANP (atrial natriuretic peptide) concentrations, measured by radioimmunoassay, in the ANPergic cerebral regions involved in regulation of sodium intake and excretion and pituitary gland correlated with differences in sodium preference among 40 Wistar male rats (180-220 g). Sodium preference was measured as mean spontaneous ingestion of 1.5% NaCl solution during a test period of 12 days. The relevant tissues included the olfactory bulb (OB), the posterior and anterior lobes of the pituitary gland (PP and AP, respectively), the median eminence (ME), the medial basal hypothalamus (MBH), and the region anteroventral to the third ventricle (AV3V). We also measured ANP content in the right (RA) and left atrium (LA) and plasma. The... |
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Palavras-chave: Sodium chloride intake; Sodium chloride preference; Atrial natriuretic peptide. |
| Ano: 1997 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000100010 |
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| Carvalho,K.M.; Nava,R.A.; França,M.S.F.; Medeiros,M.A.S.; Camarão,G.C.; Juliano,L.. |
| A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human liver using successive steps of chromatography on DEAE-cellulose, hydroxyapatite and Sephacryl S-200. The purified enzyme hydrolyzed the Pro7-Phe8 bond of bradykinin and the Ser25-Tyr26 bond of atrial natriuretic peptide. No cleavage was produced in other peptide hormones such as vasopressin, oxytocin or Met- and Leu-enkephalin. This enzyme activity was inhibited by 1 mM divalent cation chelators such as EDTA, EGTA and o-phenanthroline and was insensitive to 1 µM phosphoramidon and captopril, specific inhibitors of neutral endopeptidase (EC 3.4.24.11) and angiotensin-converting enzyme (EC 3.4.15.1), respectively. With Mr 85 kDa, the enzyme exhibits optimal... |
| Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Liver metalloendopeptidase; Bradykinin; Atrial natriuretic peptide. |
| Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100007 |
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