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Concerted action of dipeptidyl peptidase IV and glutaminyl cyclase results in formation of pyroglutamate-modified amyloid peptides in vitro.
Antonyan, Alvard; Schlenzig, Dagmar; Schilling, Stephan; Naumann, Marcel; Sharoyan, Svetlana; Mardanyan, Sona; Demuth, Hans-Ulrich.
Afiliación
  • Antonyan A; H. Buniatian Institute of Biochemistry of Armenian NAS, Yerevan 0014, Armenia. Electronic address: biochem@ipia.sci.am.
  • Schlenzig D; Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, Halle, Germany.
  • Schilling S; Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, Halle, Germany.
  • Naumann M; Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, Halle, Germany.
  • Sharoyan S; H. Buniatian Institute of Biochemistry of Armenian NAS, Yerevan 0014, Armenia.
  • Mardanyan S; H. Buniatian Institute of Biochemistry of Armenian NAS, Yerevan 0014, Armenia.
  • Demuth HU; Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, Halle, Germany.
Neurochem Int ; 113: 112-119, 2018 02.
Article en En | MEDLINE | ID: mdl-29224965
Compelling evidence suggests a crucial role of amyloid beta peptides (Aß(1-40/42)) in the etiology of Alzheimer's disease (AD). The N-terminal truncation of Aß(1-40/42) and their modification, e.g. by glutaminyl cyclase (QC), is expected to enhance the amyloid toxicity. In this work, the MALDI-TOF mass spectrometry application proved N-terminal cleavage of Aß(1-40/42) by purified dipeptidyl peptidase IV (DPPIV) in vitro observed earlier. The subsequent transformation of resulted Aß(3-40/42) to pE-Aß(3-40/42) in QC catalyzed glutamate cyclization was manifested. Hence, consecutive conversion of Aß(1-40/42) by DPPIV and QC can be assumed as a potential mechanism of formation of non-degrading pyroglutamated pE-Aß(3-40/42), which might accumulate and contribute to AD progression. The in vitro acceleration of Aß(1-40) aggregation in the simultaneous presence of DPPIV and QC was shown also.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Ácido Pirrolidona Carboxílico / Péptidos beta-Amiloides / Dipeptidil Peptidasa 4 / Aminoaciltransferasas Límite: Animals / Humans Idioma: En Revista: Neurochem Int Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Ácido Pirrolidona Carboxílico / Péptidos beta-Amiloides / Dipeptidil Peptidasa 4 / Aminoaciltransferasas Límite: Animals / Humans Idioma: En Revista: Neurochem Int Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido