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Nickel binding to Cap43 protein: an NMR study

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glh International Symposium on Metal lons in Biology and Medicine Book of Abatracta

9

th

INTERNATIONAL SYMPOSIUM

ON MET AL IONS IN

BIOLOGY AND MEDICINE

May, 21-24, 2006

Centro de Congressos da Universidade Cat6lica

Lisboa, Portugal

(3)

Capa: Concepçào do Gabinete de Imagem da Universidade de Coimbra

Titulo: Metallons Role in Life: An Integrated View

I mpressao e acabamentos:

Redhorse - Industria Grafica, Lda Rua Casal dos Vagares - Alto de S Joào Tel: 230702210

Fax: 239701239

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9 .. International Symposium on Metallons in Biology and Medicine Book of Abstracts

NICKEL BINDING TO CAP43 PROTEIN: AN NMR STUDY

Maria Antonietta l.oroddu, Massimiliano Peana, Serenella Medici Unìversily ofSassari, J)cpartmcnt ofChcmislry. Via Vienna 2. 07100 Sassari, Italy:

Em,lil: zoroddu@uniss.it

P-57

Cap43 has been reported ta be specifically induced by nickel compounds in a variety of celi lines. Ailhough lhe funetion of ,he Cap43 protein (MW 43,000) is noi clear, il docs appear to be induced in respanse lo an increase in intracellular concentration of Ca2+, caused by Ilickcl ion exposure in cultured human cclls, for this rcason it is named Cap43: Calcium protcin 43,000. Cap43 prolein is commonly expressed al low

levels in normal tissues, but it is overexpressed in a variety of cancer cells. Thc high leve!

or

expression in a cancerous status combined with the elcvated stability or Cap43 protein makes il an exceJlent canccr markcr. A possible way to better understand the molecular mechanisms implicated in toxicity and carcinogenicity 01' nickel compounds is to study the characteristics ofthc proteins cxpressed by the gcnes speeifically induecd by these earcinogens.

For this reason wc foeused QlIr attenlion LO investigate thc interaction ability of nicke\ to Cap43 protein. The peculiarity ofCap43 is its new mono-histidinie motifeonsisling

01' ten amino acids (TRSRSHTSEG) rcpeated three timcs in the C-tcrminus. Wc have

analyzed. for Ni(lI) binding, the 3D-amino aeid C-terminai scquenee of the protein,

TRSRSHTSEG-TRSRSHTSEG-TRSRSHTSEG. by the use of differen' NMR

techniques sue h as I

D

,

NOESY. TOCSY and ROESY experiments.

Our rcsuhs support the existcnce of an interesting binding site for Ni(lI) al the

C-terminai domain of Cap43 protein.

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