The present study was designed to reveal protein modifications in control cases related with postmortem delay and temperature of storage in 3 paradigms in which the same postmortem tissue sample (frontal cortex) was frozen a short time after death or stored at 1°C, 4°C, or room temperature and then frozen at -80°C at different intervals. No evidence of protein degradation as revealed with monodimensional gel electrophoresis and Western blotting was observed in samples artificially stored at 1°C and then frozen at different intervals up to 50 hours after death. However, the levels of several proteins were modified in samples stored at 4°C and this effect was more marked in samples stored at room temperature. Two-dimensional gel electrophoresis and mass spectrometry further corroborated these observations and permitted the identification of other proteins vulnerable or resistant to postmortem delay. Finally, gel electrophoresis and Western blotting of sarkosyl-insoluble fractions in Alzheimer disease showed reduced intensity of phospho-tau-specific bands with postmortem delay with the effects being more dramatic when the brain samples were stored at room temperature for long periods. These results emphasize the necessity of reducing the body temperature after death to minimize protein degradation. © 2007 American Association of Neuropathologists, Inc.

Brain protein preservation largely depends on the postmortem storage temperature: Implications for study of proteins in human neurologic diseases and management of brain banks: A BrainNet Europe study / Ferrer I.; Santpere G.; Arzberger T.; Bell J.; Blanco R.; Boluda S.; Budka H.; Carmona M.; Giaccone G.; Krebs B.; Limido L.; Parchi P.; Puig B.; Strammiello R.; Strobel T.; Kretzschmar H.. - In: JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY. - ISSN 0022-3069. - STAMPA. - 66:1(2007), pp. 35-46. [10.1097/nen.0b013e31802c3e7d]

Brain protein preservation largely depends on the postmortem storage temperature: Implications for study of proteins in human neurologic diseases and management of brain banks: A BrainNet Europe study

PARCHI, PIERO;
2007

Abstract

The present study was designed to reveal protein modifications in control cases related with postmortem delay and temperature of storage in 3 paradigms in which the same postmortem tissue sample (frontal cortex) was frozen a short time after death or stored at 1°C, 4°C, or room temperature and then frozen at -80°C at different intervals. No evidence of protein degradation as revealed with monodimensional gel electrophoresis and Western blotting was observed in samples artificially stored at 1°C and then frozen at different intervals up to 50 hours after death. However, the levels of several proteins were modified in samples stored at 4°C and this effect was more marked in samples stored at room temperature. Two-dimensional gel electrophoresis and mass spectrometry further corroborated these observations and permitted the identification of other proteins vulnerable or resistant to postmortem delay. Finally, gel electrophoresis and Western blotting of sarkosyl-insoluble fractions in Alzheimer disease showed reduced intensity of phospho-tau-specific bands with postmortem delay with the effects being more dramatic when the brain samples were stored at room temperature for long periods. These results emphasize the necessity of reducing the body temperature after death to minimize protein degradation. © 2007 American Association of Neuropathologists, Inc.
2007
Brain protein preservation largely depends on the postmortem storage temperature: Implications for study of proteins in human neurologic diseases and management of brain banks: A BrainNet Europe study / Ferrer I.; Santpere G.; Arzberger T.; Bell J.; Blanco R.; Boluda S.; Budka H.; Carmona M.; Giaccone G.; Krebs B.; Limido L.; Parchi P.; Puig B.; Strammiello R.; Strobel T.; Kretzschmar H.. - In: JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY. - ISSN 0022-3069. - STAMPA. - 66:1(2007), pp. 35-46. [10.1097/nen.0b013e31802c3e7d]
Ferrer I.; Santpere G.; Arzberger T.; Bell J.; Blanco R.; Boluda S.; Budka H.; Carmona M.; Giaccone G.; Krebs B.; Limido L.; Parchi P.; Puig B.; Strammiello R.; Strobel T.; Kretzschmar H.
File in questo prodotto:
Eventuali allegati, non sono esposti

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/38478
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 150
  • ???jsp.display-item.citation.isi??? 141
social impact