Angiotensin converting enzyme of Thalassophryne nattereri venom

被引：6

作者：

da Costa Marques, Maria Elizabeth ^{[1
]}

Tenorio, Humberto de Araujo ^{[1
]}

Victor dos Santos, Claudio Wilian ^{[1
]}

dos Santos, Daniel Moreira ^{[2
]}

de Lima, Maria Elena ^{[2
]}

Vieira Pereira, Hugo Juarez ^{[1
]}

机构：

[1] Univ Fed Alagoas, Inst Quim & Biotecnol, Ave Lourival Melo Mota S-N, BR-57072970 Maceio, AL, Brazil

[2] Univ Fed Minas Gerais, Dept Bioquim & Imunol, Belo Horizonte, MG, Brazil

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2016年 / 91卷

关键词：

Angiotensin converting enzyme; Venom; Natterin; 1; FISH VENOM; KININOGENASE ACTIVITY; CLEAVAGE; LOCALIZATION; INHIBITION; BRADYKININ; SUBSTRATE; PEPTIDES; PROTEINS; DOMAIN;

D O I：

10.1016/j.ijbiomac.2016.06.051

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Animal venoms are complex mixtures, including peptides, proteins (i.e., enzymes), and other compounds produced by animals in predation, digestion, and defense. These molecules have been investigated regarding their molecular mechanisms associated with physiological action and possible pharmacological applications. Recently, we have described the presence of a type of angiotensin converting enzyme (ACE) activity in the venom of Thalassophryne nattereri. It is a zinc-dependent peptidase with a wide range of effects. By removing dipeptide His-Leu from terminal C, the ACE converts angiotensinI (AngI) into angiotensin II (AngII) and inactivates bradykinin, there by regulating blood pressure and electrolyte homeostasis. The fractionation of T. nattereri venom in CM-Sepharose indicated a peak (CM2) with angiotensin-converting activity, converting AngI into Ang II. Electrophoresis on polyacrylamide gel (12%) revealed one band with 30 kDa for CM2 similar in size to natterins, which are toxins with proteolytic activity found in T. nattereri venom. Mass spectrometry indicated that the protein sequence of the ACE purified from T. nattereri venom corresponds to natterin 1. The isolated protein has also demonstrated inhibition through captopril and EDTA and is characterized as a classic ACE. Thus, the isolated enzyme purified from T. nattereri venom is the first ACE isolated from fish venom. (C) 2016 Elsevier B.V. All rights reserved.

引用

页码：980 / 986

页数：7

共 38 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] Brown Spider (Loxosceles genus) Venom Toxins: Tools for Biological Purposes [J].

Chaim, Olga Meiri ;

Trevisan-Silva, Dilza ;

Chaves-Moreira, Daniele ;

Wille, Ana Carolina M. ;

Ferrer, Valeria Pereira ;

Matsubara, Fernando Hitomi ;

Mangili, Oldemir Carlos ;

da Silveira, Rafael Bertoni ;

Gremski, Luiza Helena ;

Gremski, Waldemiro ;

Senff-Ribeiro, Andrea ;

Veiga, Silvio Sanches .

TOXINS, 2011, 3 (03) :309-344

[3] INHIBITION O HOMOGENEOUS ANGIOTENSIN-CONVERTING ENZYME OF RABBIT LUNG BY SYNTHETIC VENOM PEPTIDES OF BOTHROPS-JARARACA [J].

CHEUNG, HS ;

CUSHMAN, DW .

BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 293 (02) :451-463

[4] The pharmacological activity of fish venoms [J].

Church, JE ;

Hodgson, WC .

TOXICON, 2002, 40 (08) :1083-1093

[5] Angiotensin-converting enzyme 2 is an essential regulator of heart function [J].

Crackower, MA ;

Sarao, R ;

Oudit, GY ;

Yagil, C ;

Kozieradzki, I ;

Scanga, SE ;

Oliveira-dos-Santos, AJ ;

da Costa, J ;

Zhang, LY ;

Pei, Y ;

Scholey, J ;

Ferrario, CM ;

Manoukian, AS ;

Chappell, MC ;

Backx, PH ;

Yagil, Y ;

Penninger, JM .

NATURE, 2002, 417 (6891) :822-828

[6] N-domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme angiotensin-(1-7) and Keto-ACE [J].

Deddish, PA ;

Marcic, B ;

Jackman, HL ;

Wang, HZ ;

Skidgel, RA ;

Erdös, EG .

HYPERTENSION, 1998, 31 (04) :912-917

[7] Dipeptidase-inactivated tACE action in vivo: Selective inhibition of sperm-zona pellucida binding in the mouse [J].

Deguchi, Eishi ;

Tani, Taeko ;

Watanabe, Hitomi ;

Yamada, Shuichi ;

Kondoh, Gen .

BIOLOGY OF REPRODUCTION, 2007, 77 (05) :794-802

[8] RAPID AFFINITY CHROMATOGRAPHIC PURIFICATION OF HUMAN-LUNG AND KIDNEY ANGIOTENSIN-CONVERTING ENZYME WITH THE NOVEL N-CARBOXYALKYL DIPEPTIDE INHIBITOR N-[1(S)-CARBOXY-5-AMINOPENTYL]GLYCYLGLYCINE [J].

EHLERS, MRW ;

MAEDER, DL ;

KIRSCH, RE .

BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 883 (02) :361-372

[9] Pathologic consequences of increased angiotensin II activity [J].

Ferrario, CM ;

Flack, JM .

CARDIOVASCULAR DRUGS AND THERAPY, 1996, 10 (05) :511-518

[10] ISOLATION OF BRADYKININ-POTENTIATING PEPTIDES FROM BOTHROPS-JARARACA VENOM [J].

FERREIRA, SH ;

BARTELT, DC ;

GREENE, LJ .

BIOCHEMISTRY, 1970, 9 (13) :2583-&

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