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Protection of Islets by in SituPeptide-mediated Transduction of the IκB Kinase Inhibitor Nemo-binding Domain Peptide
- Source :
- Journal of Biological Chemistry. 278:9862-9868
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- We have previously demonstrated that adenoviral gene transfer of the NF-kappaB inhibitor IkappaB to human islets results in protection from interleukin (IL)-1beta-mediated dysfunction and apoptosis. Here we report that human and mouse islets can be efficiently transduced by a cationic peptide transduction domain (PTD-5) without impairment of islet function. PTD mediated delivery of a peptide inhibitor of the IL-1beta-induced IkappaB kinase (IKK), derived from IKKbeta (NBD; Nemo-binding domain), and completely blocked the detrimental effects of IL-1beta on islet function and NF-kappaB activity, in a similar manner to Ad-IkappaB. We also demonstrate that mouse islets can be transduced in situ by infusion of the transduction peptide through the bile duct prior to isolation, resulting in 40% peptide transduction of the beta-cells. Delivery of the IKK inhibitor transduction fusion peptide (PTD-5-NBD) in situ to mouse islets resulted in improved islet function and viability after isolation. These results demonstrate the feasibility of using PTD-mediated delivery to transiently modify islets in situ to improve their viability and function during isolation, prior to transplantation.
- Subjects :
- endocrine system
Cell Survival
Recombinant Fusion Proteins
Apoptosis
IκB kinase
Protein Serine-Threonine Kinases
Biology
Biochemistry
Adenoviridae
Islets of Langerhans
Mice
Transduction (genetics)
Animals
Humans
Insulin
Molecular Biology
Cells, Cultured
Mice, Inbred BALB C
geography
geography.geographical_feature_category
Gene Transfer Techniques
NF-kappa B
Transcription Factor RelA
I-Kappa-B Kinase
Cell Biology
Islet
NFKB1
I-kappa B Kinase
Protein Structure, Tertiary
Cell biology
Transplantation
Protein Transport
Glucose
Microscopy, Fluorescence
Signal transduction
Peptides
Signal Transduction
Binding domain
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 278
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....03e69b853f3346bf0b175d2390018004
- Full Text :
- https://doi.org/10.1074/jbc.m207700200