Inactivation and polymerization of human neuroserpin

Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R

Risultato della ricerca: Paper

Abstract

Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation and polymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.
Lingua originaleEnglish
Stato di pubblicazionePublished - 2010

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Polymerization
Serpins
Polymers
Chemical stability
Liquid chromatography
Emission spectroscopy
Pathology
Dynamic light scattering
Oligomers
Self assembly
Elongation
Temperature
neuroserpin
Enzymes

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Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R (2010). Inactivation and polymerization of human neuroserpin.

Inactivation and polymerization of human neuroserpin. / Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R.

2010.

Risultato della ricerca: Paper

Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R 2010, 'Inactivation and polymerization of human neuroserpin'.
Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R. Inactivation and polymerization of human neuroserpin. 2010.
Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R. / Inactivation and polymerization of human neuroserpin.
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AU - Manno, A; Mangione, Mr; Ricagno, S; Pezzullo, M; Bolognesi, M; Martorana, V; Noto, R

AU - Levantino, Matteo

AU - Santangelo, Maria Grazia

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N2 - Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation and polymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.

AB - Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation and polymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.

KW - human neuroserpin, polymerization, conformational changes

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