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Molecular and Immunochemical Evidences Demonstrate That Endooligopeptidase A Is the Predominant Cytosolic Oligopeptidase of Rabbit Brain

Hayashi, Mirian A.F. ; Portaro, Fernanda C.V. ; Tambourgi, Denise V. ; Sucupira, Mauro ; Yamane, Tetsuo ; Fernandes, Beatriz L. ; Ferro, Emer S. ; Rebouças, Nancy A. ; de Camargo, Antonio C.M.

Biochemical and biophysical research communications, 2000-03, Vol.269 (1), p.7-13 [Revista revisada por pares]

United States: Elsevier Inc

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Título:
Molecular and Immunochemical Evidences Demonstrate That Endooligopeptidase A Is the Predominant Cytosolic Oligopeptidase of Rabbit Brain
Autor: Hayashi, Mirian A.F. ; Portaro, Fernanda C.V. ; Tambourgi, Denise V. ; Sucupira, Mauro ; Yamane, Tetsuo ; Fernandes, Beatriz L. ; Ferro, Emer S. ; Rebouças, Nancy A. ; de Camargo, Antonio C.M.
Materias: Amino Acid Sequence ; Animals ; Antibodies ; Base Sequence ; Brain - enzymology ; Cloning, Molecular ; Cytosol - enzymology ; DNA, Complementary - genetics ; Immunochemistry ; Male ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - genetics ; Metalloendopeptidases - immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Rabbits ; Rats ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Tissue Distribution
Es parte de: Biochemical and biophysical research communications, 2000-03, Vol.269 (1), p.7-13
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descripción: Oligopeptidases are tissue endopeptidases that do not attack proteins and are likely to be involved in the maturation and degradation of peptide hormones and neuropeptides. The rabbit brain endooligopeptidase A and the rat testes soluble metallopeptidase (EC 3.4.24.15) are thiol-activated oligopeptidases which are able to generate enkephalin from a number of opiod peptides and to inactivate bradykinin and neurotensin by hydrolyzing the same peptide bonds. A monospecific antibody raised against the purified rabbit brain endooligopeptidase A allowed the identification of a 2.3 kb cDNA coding for a truncated enzyme of 512 amino acids, displaying the same enzymatic features as endooligopeptidase A. In spite of all efforts, employing several strategies, the full-length cDNA could not be cloned until now. The analysis of the deduced amino acid sequence showed no similarity to the rat testes metalloendopeptidase sequence, except for the presence of the typical metalloprotease consensus sequence [HEXXH]. The antibody raised against recombinant endooligopeptidase A specifically inhibited its own activity and reduced the thiol-activated oligopeptidase activity of rabbit brain cytosol to less than 30%. Analysis of the endooligopeptidase A tissue distribution indicated that this enzyme is mainly expressed in the CNS, whereas the soluble metallo EC 3.4.24.15 is mainly expressed in peripheral tissues.
Editor: United States: Elsevier Inc
Idioma: Inglés

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Molecular and Immunochemical Evidences Demonstrate That Endooligopeptidase A Is the Predominant Cytosolic Oligopeptidase of Rabbit Brain

Hayashi, Mirian A.F. ; Portaro, Fernanda C.V. ; Tambourgi, Denise V. ; Sucupira, Mauro ; Yamane, Tetsuo ; Fernandes, Beatriz L. ; Ferro, Emer S. ; Rebouças, Nancy A. ; de Camargo, Antonio C.M.

United States: Elsevier Inc

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