Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression

Joel Montané Mogas

Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression

Título traducido de la contribución: Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression

Joel Montané Mogas

Facultad de Ciencias de la Salud Blanquerna

Producción científica: Contribución a una conferencia › Contribución

Resumen

Diabetologia. 60:Suppl 1; 602; S273-274.

Título traducido de la contribución	Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression
Idioma original	Inglés
Páginas	S273-274
Número de páginas	2
Estado	Publicada - 1 ene 2014
Evento	European Association for Study of Diabetes. EASD Annual Conference. Vienna - Viena, Austria Duración: 1 ene 2014 → 1 ene 2014

Conferencia

Conferencia	European Association for Study of Diabetes. EASD Annual Conference. Vienna
País/Territorio	Austria
Ciudad	Viena
Período	1/01/14 → 1/01/14

ODS de las Naciones Unidas

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ODS 3: Salud y bienestar

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https://link.springer.com/article/10.1007/s00125-014-3355-0Licencia: Sin especificar

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@conference{371293a864c84b04a9abbb55b11956d0,

title = "Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression",

abstract = "In type 2 diabetes and islet transplantation beta-cell dysfunction is thought to be due to several causes, one being the formation of toxic protein aggregates called islet amyloid, formed by accumulations of misfolded human islet amyloid polypeptide (hIAPP). The process of hIAPP misfolding and aggregation is one of the factors that may perturb the endoplasmic reticulum (ER) homeostasis, leading to beta cell dysfunction and ultimately, cell death. Molecular chaperones have been described to be important for regulation of ER response to ER stress by stabilizing protein conformation and improving ER capacity. The aim of the present work is to determine whether chaperone treatment is able to counteract hIAPP-induced beta cell dysfunction and, ultimately, diminish amyloid formation and cell death in pancreatic islets.",

author = "\{Montan{\'e} Mogas\}, Joel",

note = "Diabetologia. 60:Suppl 1; 602. Joel Montane, Lisa Cadavez, Carlos Casta{\~n}o, Anna Novials; European Association for Study of Diabetes. EASD Annual Conference. Vienna ; Conference date: 01-01-2014 Through 01-01-2014",

year = "2014",

month = jan,

day = "1",

language = "English",

pages = "S273--274",

}

TY - CONF

T1 - Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression

AU - Montané Mogas, Joel

N1 - Diabetologia. 60:Suppl 1; 602. Joel Montane, Lisa Cadavez, Carlos Castaño, Anna Novials

PY - 2014/1/1

Y1 - 2014/1/1

N2 - In type 2 diabetes and islet transplantation beta-cell dysfunction is thought to be due to several causes, one being the formation of toxic protein aggregates called islet amyloid, formed by accumulations of misfolded human islet amyloid polypeptide (hIAPP). The process of hIAPP misfolding and aggregation is one of the factors that may perturb the endoplasmic reticulum (ER) homeostasis, leading to beta cell dysfunction and ultimately, cell death. Molecular chaperones have been described to be important for regulation of ER response to ER stress by stabilizing protein conformation and improving ER capacity. The aim of the present work is to determine whether chaperone treatment is able to counteract hIAPP-induced beta cell dysfunction and, ultimately, diminish amyloid formation and cell death in pancreatic islets.

AB - In type 2 diabetes and islet transplantation beta-cell dysfunction is thought to be due to several causes, one being the formation of toxic protein aggregates called islet amyloid, formed by accumulations of misfolded human islet amyloid polypeptide (hIAPP). The process of hIAPP misfolding and aggregation is one of the factors that may perturb the endoplasmic reticulum (ER) homeostasis, leading to beta cell dysfunction and ultimately, cell death. Molecular chaperones have been described to be important for regulation of ER response to ER stress by stabilizing protein conformation and improving ER capacity. The aim of the present work is to determine whether chaperone treatment is able to counteract hIAPP-induced beta cell dysfunction and, ultimately, diminish amyloid formation and cell death in pancreatic islets.

M3 - Contribution

SP - S273-274

T2 - European Association for Study of Diabetes. EASD Annual Conference. Vienna

Y2 - 1 January 2014 through 1 January 2014

ER -

Chaperones ameliorate beta cell dysfunction and amyloid formation associated with islet amyloid polypeptide overexpression

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ODS de las Naciones Unidas

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