Spectroscopic and structural analysis of somatic and N-domain angiotensin I-converting enzyme isoforms from mesangial cells from Wistar and spontaneously hypertensive rats

Autor(es):Mostrar menos -

de Andrade, Maria C. C. ^[1] ; Affonso, Regina ^{[2, 3]} ; Fernandes, Fernanda B. ^[1] ; Febba, Andreia C. ^[1] ; da Silva, Ismael D. C. G. ^[3] ; Stella, Regina C. R. ^[1] ; Marson, Odair ^[1] ; Jubilut, Guita N. ^[4] ; Hirata, Izaura Y. ^[4] ; Carmona, Adriana K. ^[4] ; Corradi, Hazel ^[5] ; Acharya, K. Ravi ^[5] ; Sturrock, Edward D. ^{[6, 7]} ; Casarini, Dulce E. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Fed Sao Paulo, Escola Paulista Med, Dept Med, Disciplina Nefrol, BR-04023900 Sao Paulo - Brazil

^[2] IPEN CNEN SP, Sao Paulo - Brazil

^[3] Univ Fed Sao Paulo, Dept Obstet & Ginecol, BR-04023900 Sao Paulo - Brazil

^[4] Univ Fed Sao Paulo, Dept Biofis, BR-04023900 Sao Paulo - Brazil

^[5] Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon - England

^[6] Univ Cape Town, Div Med Biochem, ZA-7925 Observatory - South Africa

^[7] Univ Cape Town, Inst Infect Dis & Mol Med, ZA-7925 Observatory - South Africa

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 47, n. 2, p. 238-243, AUG 1 2010.
• Citações Web of Science: 1

Resumo

Angiotensin I-converting enzyme (ACE) plays a key role in the renin-angiotesin aldosterone cascade. We analysed the secondary structure and structural organization of a purified 65 kDa N-domain ACE (nACE) from Wistar rat mesangial cells, a 90 kDa nACE from spontaneously hypertensive rats and a 130 kDa somatic ACE. The C-terminal alignment of the 65 kDa nACE with rat ACE revealed that the former was truncated at Ser(482), and the sequence of the 90 kDa nACE ended at Pro(629). Protein's secondary structure consisted predominantly of a-helices. The 90 and 65 kDa isoforms were the most stable in guanidine and at low pH, respectively. Enzymatic activity decreased with loss in secondary structure, except in the case of guanidine HCl where the 90 kDa fragment loses its secondary structure faster than its enzymatic activity. We identified and characterized the activity and stability of these isoforms and these findings would be helpful on the understanding of the role of nACE isoforms in hypertension. (C) 2010 Elsevier B.V. All rights reserved. (AU)

• Processo FAPESP: 03/02575-9 - Estudo molecular e funcional das isoformas N-domínio da enzima conversora de angiotensina I (ECA) de 65 kDa e 90 kDa (possível marcador genético de hipertensão) nas células mesangiais (cm) de ratos Wistar e SHR
• Beneficiário: Maria Claudina Camargo de Andrade
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 02/13290-2 - Isoforma (90 kDa) da enzima conversora de Angiotensina I, potencial marcador genético de hipertensão: processamento, caracterização molecular e funcional, e segregação genética
• Beneficiário: Dulce Elena Casarini
• Modalidade de apoio: Auxílio à Pesquisa - Temático