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Your search keyword '"Portaro, Fernanda C.V."' showing total 25 results
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25 results on '"Portaro, Fernanda C.V."'

8. Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase activity by disrupted-in-schizophrenia 1

Author

Hayashi, Mirian A.F., Portaro, Fernanda C.V., Bastos, Marta F., Guerreiro, Juliano R., Oliveira, Vitor, Gorrao, Silvia S., Tambourgi, Denise V., Sant'Anna, Osvaldo A., Whiting, Paul J., Camargo, L. Miguel, Konno, Katsuhiro, Brandon, Nicholas J., and Camargo, Antonio C.M.

Subjects
Schizophrenia -- Research, Schizophrenia -- Physiological aspects, Schizophrenia -- Causes of, Oligopeptides -- Research, Oligopeptides -- Physiological aspects, Science and technology
Abstract

Recently, nuclear distribution element-like (NUDEL) has been implicated to play a role in lissencephaly and schizophrenia through interactions with the lissencephaly gene 1 (Lis1) and disrupted-in-schizophrenia 1 (DISC1) products, respectively. Interestingly, NUDEL is the same protein as endooligopeptidase A (EOPA), a thiol-activated peptidase involved in conversion and inactivation of a number of bioactive peptides. In this study, we have cloned EOPA from the human brain and have confirmed that it is equivalent to NUDEL, leading us to suggest a single name, NUDEL-oligopeptidase. In the brain, the monomeric form of NUDEL-oligopeptidase is responsible for the peptidase activity whose catalytic mechanism is likely to involve a reactive cysteine, because mutation of Cys-273 fully abolished NUDEL-oligopeptidase activity without disrupting the protein's secondary structure. Cys-273 is very close to the DISC1-binding site on NUDEL-oligopeptidase. Intriguingly, DISC1 inhibits NUDEL-oligopeptidase activity in a competitive fashion. We suggest that the activity of NUDEL-oligopeptidase is under tight regulation through protein-protein interactions and that disruption of these interactions, as postulated in a Scottish DISC1 translocation schizophrenia cohort, may lead to aberrant regulation of NUDEL-oligopeptidase, perhaps providing a substrate for the pathology of schizophrenia. endooligopeptidase A | neuropeptide metabolism | cysteine peptidase | neurodevelopmental pathology

Published
2005

14. Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts

Author

Nagler, Dorit K., Storer, Andrew C., Portaro, Fernanda C.V., Carmona, Euridice, Juliano, Luiz, and Menard, Robert

Subjects
Cysteine proteinases -- Analysis, Enzymes -- Structure-activity relationship, Biological sciences, Chemistry
Abstract

NMR signal detection was utilized to site an evidence of side-to-side interactions among isolated transmembrane domains of the EGF receptor as a class I receptor tyrosine kinase. The transmembrane domain of the EGF receptor displays a low density to formation of homodimers/oligomers in fluid phospholipid membranes. Peptide-peptide interactions were detected through their effects on the backbone motion and conformation.

Published
1997

21. Neuropeptide Specificity and Inhibition of Recombinant Isoforms of the Endopeptidase 3.4.24.16 Family: Comparison with the Related Recombinant Endopeptidase 3.4.24.15

Author

Rioli, Vanessa, primary, Kato, Akira, additional, Portaro, Fernanda C.V., additional, Cury, Gabriela K., additional, te Kaat, Kai, additional, Vincent, Bruno, additional, Checler, Frederic, additional, Camargo, Antonio C.M., additional, Glucksman, Marc J., additional, Roberts, James L., additional, Hirose, Shigehisa, additional, and Ferro, Emer S., additional

Published
1998
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24. The Mycobacterium leprae hsp65 Displays Proteolytic Activity,. Mutagenesis Studies Indicate That the M. leprae hsp65 Proteolytic Activity Is Catalytically Related to the HsIVU Protease.

Author

Portaro, Fernanda C.V., Hayashi, Mirian A.F., de Arauz, Luciana J., Palma, Mario S., Assakura, Marina T., Silva, Célio L., and de Camargo, Antonio C.M.

Subjects
*HEAT shock proteins, *MYCOBACTERIUM leprae, *OLIGOPEPTIDES
Abstract

Evaluates the proteolytic activity of the recombinant heat shock proteins (hsp) 65 from Mycobacterium leprae against oligopeptides. Functional roles of hsp 60; Implication of microbial hsp60 in autoimmune disease; Utilization of Mycobacterium leprae hsp60 for tuberculosis vaccination.

Published
2002
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25. Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity,induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage.

Author

Portaro, Fernanda C.V., Hayashi, Mirian A.F., Silva, Celio L., and de Camargo, Antonio C.M.

Subjects
*ADENOSINE triphosphate, *OLIGOPEPTIDES
Abstract

Examines adenosine triphosphate inhibition of thimet oligopeptidase (TOP) activity. Induction of autophosphorylation; Control of oligopeptide degradation in macrophage; Influence of kinase on TOP phosphorylation.

Published
2001
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