Manuel Aureliano, PhD

Assistant Professor

Biochemistry, Inorganic Biochemistry and Cell Biology

 

DQB, FCT, Algarve University, Faro, Portugal

e-mail: maalves@ualg.pt

 

M. Aureliano has been Director and vice-director of the Biochemistry degree (Algarve University) from 1997/98 to 2002/03.

(Link to:http://www.ualg.pt/fct/quimica/Bioquimica.html) or http://www.fct.ualg.pt/bioquimica.

 

Disciplines

first semestre: Bioquímica Geral I (2nd year) Metais e Metabolismo (3 and 4th years);

second semestre: Biologia Celular(first year); Tópicos Avançados em Biologia Celular (3 and 4th years)


Information 2004/05:


Licenciatura em Bioquímica

Biologia Celular (1º ano)

2004/2005

Informação final após exame (01/07/05)

Nome do aluno, nº

Classificação

Rita Pessoa, 27936

16

Maria Rodrigues, 27928

16

Andreia Loureço, 21564

15

Célia Domingos, 27918

15

Paulo Ferreira, 27933

14

Denise Schrama, 25557

14

Ana Eufigénia, 23613

14

Diana Lopes, 27920

14

Telma Silva, 25914

14

Joana Cristo, 27925

14

Joana Alho, 25038

13

Míriam Jesus, 25045

13

Sabrina Bota, 25053

13

Catarina Nobre, 27917

13

Pedro Ramos, 25049

13

Henrique Batista, 27924

13

Joel Pires, 27926

13

Ana Correia, 27914

13

Ana Jesus, 28984

13

Mário Borges, 25042

13

Susana Viegas, 28985

12

Sara Evaristo, 27938

12

Rosa Brissos, 25052

12

Diogo Cordeiro, 27927

12

Cláudia Pedro, 27919

12

Vânia Martins, 28987

12

João Roberto, 21841

12

Telma Mateus, 28986

12

Regina Silva, 27934

11

Heloísa Neto, 27923

11

Filipa Rodrigues, 27922

11

Ana Fidalgo, 23614

11

Mónica Gomes, 27930

11

Maria Fernandes, 29147

11

Mónica Faria, 27931

10

Rui Lopes, 27937

10

Andreia Silva, 24171

10

Prof. M. Aureliano Alves

Campus de Gambelas, 4 de Julho de 2005

 

Tópicos Avançados em Biologia Celular

(Lic. Bioquímica; 4º ano, 2ºS, 2004/05)

(Informação Final de Frequência)

 

1

Nome

Artigo A

Apresentação Oral e Defesa

20%

Artigo B

Apresentação Oral e Defesa

20%

Monografia 1

20%

Monografia Final

 40%

Classif.

Final

Claúdia Oliveira,17107

16,5

16

16,5

18

17

Karina Pires, 19324

16

16

16

18

17

Vanda Pinto, 18931

17

18

17

19

18

Margarida Neto, 20139

15

15

15

17

16

Dorinda Silva, 21563

16

17

16,5

18

17

Susana Ramos, 24034

18

19

17

19

19

Rogério Rodrigues, 17512

16

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*

Pedro Bastos

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*

 

Research topics:

1)    Interaction of vanadate with myosin/actin

2)    Vanadate complexes effects on calcium pump

3)    Cellular responses induced by vanadate

(Link to: http://www.ualg.pt/fct/quimica/Aureliano_Alves.html)

 

Research team:

Postdoctoral fellow: Rui Duarte

PhD students: Teresa Tiago, Sandra Soares, Daniel Tiago, Gisela Borges.

Gradute students: Andrea Sousa, (Master Student) Ricardo Gândara, Maria João Pereira, Adélia Moderno

Undergraduate students: Ana Pereira, Sandra Alves, Sónia Simão

(Link to: http://www.fct.ualg.pt/biovanadium)

 

Resume of scientific interest

Vanadium is widely known for its toxic effects, however it is vestigial in muscles and other tissues and is considered an essential oligoelement for humans. Its biological role is far from a clear identification. Vanadium is present in petroleum, coal and gasoline, used as alloys and catalysts for industry and is well known for its environmental and biological impact.

Most of the biological importance of vanadium is associated with the +5 oxidation state (vanadate) probably due to similarities between the phosphate and vanadate chemistries in solution. In vanadium (+5) solutions different oligomeric (n=1 to 10) vanadate species can occur simultaneously in equilibrium such as monomeric (V1), dimeric (V2), tetrameric (V4) and decameric (V10) and, in same cases, with different states of protonation and forms.

Many of these vanadate species are not taken in consideration in the majority of the biological studies, although it is known that they may also influence enzyme activity. The effects can be conveniently analysed combining kinetic with spectroscopy studies. With the sarcoplasmic reticulum calcium pump and myosin experiments can be design to detect different interactions and different effects for several oligomeric vanadate species. Allegorically, vanadate studies in biological systems compare to iceberg phenomena, being of crucial importance to precisely characterize the vanadate species and the interactions with the system before attempting to understand the promoted effects.

1) Myosin is a highly specialized protein that converts the chemical energy of ATP hydrolysis to mechanical work. This activity is greatly enhanced when actin binds to myosin forming the actomyosin complex. It is known that myosin is inhibited by vanadate due to the similarity with phosphate. However, the effects of other species of vanadate on the activity of myosin and actomyosin have not yet been clarified. It was demonstrated that, under conditions near physiological ones, decameric vanadate differs from vanadate oligomers present in metavanadate solutions due to its strong interaction with the phosphorylated enzyme and myosin ATPase inhibition. Besides, ATP decreases the affinity of myosin for tetravanadate, induces the interaction with monomeric vanadate, whereas does not affect decameric vanadate interaction. Moreover, is was described that the binding of decavanadate to high affinity sites in myosin are due to local conformational change(s) near the tryptophans of myosin more accessible to water in the three-dimensional structure of this protein (Tiago et. al., 2002a and 2002b).

          2) Sarcoplasmic reticulum (SR) Ca2+-ATPase is a transmembrane transport system, which accumulates Ca2+ at expense of ATP splitting during the process of muscle relaxation. ATP is used in a process involving the transfer of the phosphoryl group to the Ca2+-ATPase with subsequent breakdown of the phosphorylated enzyme. The mechanism by which the Ca2+ pumping is associated with ATP hydrolysis is not fully understood in clear molecular terms and is usually summarized by a cycle of sequential reaction steps with two major states of the enzyme, E1 and E2, with high and low affinity for Ca2+ and ATP, respectively. Initially it was thought that vanadate affected this Ca2+ pump in the same way as other P-type ATPases, but recent studies show the existence of Ca2+ ATPases with different sensitivities to vanadate. It was demonstrated that some of the interactions, e.g. decameric species, disrupt the energetic coupling and the enzyme turnover. Other interactions of vanadium, e.g. monomeric species, may be without effect or even improve the coupling of Ca2+ pumping (Aureliano e Madeira, 1998; Aureliano, 2000).

3) Oxidative stress studies induced by cadmium, zinc, selenium, copper and vanadium are also almost limited to hepatic and renal injury studies. On other hand, the contribution of vanadate oligomers to vanadium toxicity is usually not considered. The different responses obtained on in vivo and in vitro studies proves that in vivo metals metabolism is very complex and great care must be taken on extrapolation from in vitro conditions. Recently, it was demonstrated that decameric vanadate species are responsible for a strong increase on lipid peroxidation and a decrease in cytosolic catalase activity thus contributing to oxidative stress responses upon vanadate intoxication. Furthermore, acute exposure studies suggest a different in vivo metabolic pattern for decameric vanadate species, pointing out the importance of vanadate speciation on the evaluation of vanadium toxicity (Aureliano et al., 2002; Soares et al, 2003).

 

Recent articles

M. Aureliano, V.M.C. Madeira (1998) in: J.O Nriagu (Ed.), Vanadium in the Environment, part 1: Chemistry and Biochemistry, J.Wiley, New York, 1998, chapter. 14, pp 333-357.

 

M. Aureliano (2000) “Vanadate oligomers inhibition of passive and active Ca2+ translocation by the Ca2+ pump of sarcoplasmic reticulum” J. Inorg. Biochem. 80: 145-147.

 

Teresa Tiago, Manuel Aureliano, Carlos Gutiérrez-Merino (2002) “Quenching of myosin intrinsic fluorescence unravels the existence of a high affinity binding site for decavanadate” J. Fluorescence, 12: 87-90.

 

M. Aureliano, N. Joaquim, A. Sousa, H. Martins, J.M Coucelo (2002) Oxidative stress in toadisfh (Halobactrachus didactylus) cardiac muscle: Acute exposure to vanadate oligomers” J. Inorg. Biochem. 90: 159-165.

 

T. Tiago, M. Aureliano, R.O.Duarte, J.J.G. Moura (2002) “Vanadate oligomers interaction with phosporylated myosin” Inorg. Chim. Acta 339: 317-321.

 

S.S. Soares, M. Aureliano*, N. Joaquim, J.M. Coucelo (2003) “Cadmium and vanadate oligomers effects on methaemoglobin reductase activity from Lusitanian toadfish”: J. Inorg. Biochem 94: 285-290.

 

 

link to :Bioquímica da FCT da Ualg: http://www.fct.ualg.pt/bioquimica