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Texto completo
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| Autor(es): |
Dores-Silva, Paulo Roberto
[1, 2]
;
Cauvi, David M.
[2]
;
Kiraly, Vanessa T. R.
[1]
;
Borges, Julio C.
[1]
;
De Maio, Antonio
[2, 3]
Número total de Autores: 5
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| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Paulo - Brazil
[2] Univ Calif San Diego, Sch Med, Dept Surg, Div Trauma Crit Care Burns & Acute Care Surg, La Jolla, CA 92093 - USA
[3] Univ Calif San Diego, Sch Med, Dept Neurosci, Div Trauma Crit Care Burns & Acute Care Surg, La Jolla, CA 92093 - USA
Número total de Afiliações: 3
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| Tipo de documento: |
Artigo Científico
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| Fonte: |
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES;
v. 1862,
n. 11
NOV 1 2020.
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| Citações Web of Science: |
0
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| Resumo |
Mitochondrial Hsp70 (HSPA9, mtHsp70, mortalin) in conjunction with a complex set of other proteins is involved in the transport of polypeptides across the mitochondrial matrix. This observation allows us to hypothesize that HSPA9 might interact with membranes directly, similarly to other Hsp70s. Thus, we investigated whether human HSPA9 could also get inserted into lipid membranes. Human HSPA9 was incubated with liposomes made of lipids found within the mitochondrial membrane, such as 1', 3'-bis {[}1, 2-dimyristoyl-sn-glycero-3-phospho]-glycerol (CL), palmitoyl-oleoyl phosphocholine (POPC), palmitoyl-oleoyl phosphoserine (POPS), and palmitoyl-oleoyl phosphoethanolamine (POPE). HSPA9 displayed a predilection for CL and POPS, and low affinity for POPC and POPE, suggesting that the proteins have high specificity for negatively charged phospholipids. Then, liposomes were made with a composition resembling either the outer or inner mitochondrial membrane (OMM or IMM, respectively). We observed that HSPA9 has a higher affinity for IMM than OMM, which is consistent with the higher content of CL in the IMM. A comparison for the incorporation into POPS or CL liposomes by HSPA9 or HSPA1 indicated that both proteins behaved very similarly when exposed to CL liposomes, but differently with POPS liposomes, which was further corroborated by their susceptibility to proteinase K digestion after incorporation into liposomes. The measurement of thermodynamic parameters also showed that the interaction of both proteins with CL and POPS liposomes was different. Overall, our data showed that HSPA9 is prone to interact with membranes resembling the IMM that may be important for its role in the translocation of proteins into the mitochondria. (AU) |
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| Processo FAPESP: |
16/22477-1 - Mortalina humana: interação com lipossomos, membrana mitocondrial, beta-amiloides e efeito de sua presença na toxicidade de beta-amiloides em neurônios
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| Beneficiário: | Paulo Roberto das Dores da Silva |
| Linha de fomento: |
Bolsas no Exterior - Estágio de Pesquisa - Pós-Doutorado
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| Processo FAPESP: |
17/07335-9 - Estudos das isoformas da HSP70 humana residentes no citoplasma e mitocôndria e de seus oligômeros de alta massa molecular: interação com co-chaperonas e proteínas clientes
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| Beneficiário: | Julio Cesar Borges |
| Linha de fomento: |
Auxílio à Pesquisa - Regular
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| Processo FAPESP: |
14/16646-0 - Mortalina humana: interação com co-chaperonas, p53 e mutantes, cinética de agregação, regulação/modulação e secreção por vesículas
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| Beneficiário: | Paulo Roberto das Dores da Silva |
| Linha de fomento: |
Bolsas no Brasil - Pós-Doutorado
|
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| Processo FAPESP: |
12/50161-8 - Estudo da estrutura e função da chaperona Hsp90 com ênfase no seu papel em homeostase celular
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| Beneficiário: | Carlos Henrique Inacio Ramos |
| Linha de fomento: |
Auxílio à Pesquisa - Temático
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