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malfunction
excess of aminopeptidase A in the brain elevates blood pressure via the angiotensin II type 1 and bradykinin B2 receptors without dipsogenic effect
malfunction
higher APA activity is observed in the kidney and lower activity in lung of ob/ob mice. High aminopeptidase A (APA) activity contributes to blood pressure control in ob/ob mice through an AT2 receptor-dependent mechanism
malfunction
influence of thyroid disorders on the kidney expression and plasma activity of aminopeptidase A. In plasma, hyperthyroid rats demonstrate slight but significantly lower levels of AP A than euthyroid (control) rats
malfunction
mutagenic replacement of Arg-878 with an alanine or a lysine residue decreases the affinity of the recombinant enzymes for the acidic substrate, alpha-L-glutamyl-beta-naphthylamide, with a slight decrease in substrate hydrolysis velocity either with or without Ca2+. In the absence of Ca2+, the mutations modify the substrate specificity of enzyme APA for the acidic substrate. The mutated enzymes hydrolyse more efficiently basic and neutral substrates, although the addition of Ca2+ partially restores the acidic substrate specificity
malfunction
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higher APA activity is observed in the kidney and lower activity in lung of ob/ob mice. High aminopeptidase A (APA) activity contributes to blood pressure control in ob/ob mice through an AT2 receptor-dependent mechanism
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malfunction
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influence of thyroid disorders on the kidney expression and plasma activity of aminopeptidase A. In plasma, hyperthyroid rats demonstrate slight but significantly lower levels of AP A than euthyroid (control) rats
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malfunction
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excess of aminopeptidase A in the brain elevates blood pressure via the angiotensin II type 1 and bradykinin B2 receptors without dipsogenic effect
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metabolism
Tricorn, and its interacting factors, F1, F2, and F3 convert proteins efficiently into amino acids. It is quite likely that Tricorn also acts in vivo downstream of the proteasome and, in cooperation with its interacting factors, completes protein catabolic pathways
metabolism
thyroid disorders affect blood pressure and renal function through changes in the components of the local renin-angiotensin system such as aminopeptidase A (AP A or GluAP), which metabolizes angiotensin II (Ang II) to angiotensin III (Ang III), consequently regulating their functions
metabolism
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thyroid disorders affect blood pressure and renal function through changes in the components of the local renin-angiotensin system such as aminopeptidase A (AP A or GluAP), which metabolizes angiotensin II (Ang II) to angiotensin III (Ang III), consequently regulating their functions
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physiological function
enzyme acts as a multifunctional adhesin, binding to both heparin and plasminogen. It binds plasminogen and facilitates its activation by tissue plasminogen activator. Plasmin cleaves host extracellular matrix proteins and activates matrix metalloproteases, generating peptide substrates for the enzyme and a source of amino acids for growth of Mycoplasma hyopneumoniae
physiological function
aminopeptidase A (APA) is a membrane-bound zinc metalloprotease cleaving, in the brain, the N-terminal aspartyl residue of angiotensin II to generate angiotensin III, which exerts a tonic stimulatory effect on the control of blood pressure in hypertensive animals
physiological function
aminopeptidase A (APA) is an enzyme that hydrolyzes the N-terminal amino acid of peptides, it is expressed in both periphery and brain. Peripheral APA is reported to have the potency to act as both protective and harmful agent on cardiovascular disease. Brain APA contributes to neurogenic hypertension. Conversion of Ang II to Ang III by APA may require elevated blood pressure in the brain. An increase in brain APA elevates the blood pressure via enzymatic activity in a dose-dependent manner. The increase in brain APA does not evoke drinking behavior. AT1 and B2 receptors contribute to the pressor response to brain APA. Increased brain APA activity evokes a pressor response via the AT1 and B2 receptors without dipsogenic effect
physiological function
aminopeptidase A (PepA) belongs to the group of metallopeptidases with two bound metal ions per subunit, M1M2-PepA, it is specific for the cleavage of N-terminal glutamic (Glu) and aspartic acid (Asp) and, in low amounts, serine (Ser) residues
physiological function
aminopeptidase A enzyme metabolizes angiotensin (ANG) II into ANG III, a peptide associated with intrarenal angiotensin type 2 (AT2) receptor activation and induction of natriuresis. Role of AT2 receptor and APA as active mechanisms regulating blood pressure in ob/ob mice, overview
physiological function
an early high increase in the excretion or activity of the enzyme in supernatant of urine from cisplatin-treated rats are correlated with the extent of renal damage
physiological function
glutamyl-aminopeptidase (GAP) is a zinc metallopeptidase with angiotensinase activity highly expressed in kidney tissues, its expression and activity are associated with tumour development, role for GAP in the neoplastic development of renal tumours. Patient survival curves according to the membrane-bound and soluble glutamyl-aminopeptidase activity levels, overview
physiological function
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enzyme acts as a multifunctional adhesin, binding to both heparin and plasminogen. It binds plasminogen and facilitates its activation by tissue plasminogen activator. Plasmin cleaves host extracellular matrix proteins and activates matrix metalloproteases, generating peptide substrates for the enzyme and a source of amino acids for growth of Mycoplasma hyopneumoniae
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physiological function
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aminopeptidase A (PepA) belongs to the group of metallopeptidases with two bound metal ions per subunit, M1M2-PepA, it is specific for the cleavage of N-terminal glutamic (Glu) and aspartic acid (Asp) and, in low amounts, serine (Ser) residues
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physiological function
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aminopeptidase A enzyme metabolizes angiotensin (ANG) II into ANG III, a peptide associated with intrarenal angiotensin type 2 (AT2) receptor activation and induction of natriuresis. Role of AT2 receptor and APA as active mechanisms regulating blood pressure in ob/ob mice, overview
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physiological function
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an early high increase in the excretion or activity of the enzyme in supernatant of urine from cisplatin-treated rats are correlated with the extent of renal damage
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physiological function
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aminopeptidase A (APA) is an enzyme that hydrolyzes the N-terminal amino acid of peptides, it is expressed in both periphery and brain. Peripheral APA is reported to have the potency to act as both protective and harmful agent on cardiovascular disease. Brain APA contributes to neurogenic hypertension. Conversion of Ang II to Ang III by APA may require elevated blood pressure in the brain. An increase in brain APA elevates the blood pressure via enzymatic activity in a dose-dependent manner. The increase in brain APA does not evoke drinking behavior. AT1 and B2 receptors contribute to the pressor response to brain APA. Increased brain APA activity evokes a pressor response via the AT1 and B2 receptors without dipsogenic effect
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additional information
residue Arg878 together with Ca2+ is responsible in mouse aminopeptidase A for the substrate specificity for N-terminal acidic amino-acid residues by ensuring the optimal positioning of acidic substrates during catalysis. Docking and molecular dynamics simulations using the crystal structure of human aminopeptidase A complexed with Glu and Ca2+, PDB ID 4KXD, overview
additional information
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residue Arg878 together with Ca2+ is responsible in mouse aminopeptidase A for the substrate specificity for N-terminal acidic amino-acid residues by ensuring the optimal positioning of acidic substrates during catalysis. Docking and molecular dynamics simulations using the crystal structure of human aminopeptidase A complexed with Glu and Ca2+, PDB ID 4KXD, overview