PMID- 19607692
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20091211
LR  - 20211020
IS  - 1477-5956 (Electronic)
IS  - 1477-5956 (Linking)
VI  - 7
DP  - 2009 Jul 16
TI  - Proteins altered by elevated levels of palmitate or glucose implicated in 
      impaired glucose-stimulated insulin secretion.
PG  - 24
LID - 10.1186/1477-5956-7-24 [doi]
AB  - BACKGROUND: Development of type 2 diabetes mellitus (T2DM) is characterized by 
      aberrant insulin secretory patterns, where elevated insulin levels at 
      non-stimulatory basal conditions and reduced hormonal levels at stimulatory 
      conditions are major components. To delineate mechanisms responsible for these 
      alterations we cultured INS-1E cells for 48 hours at 20 mM glucose in absence or 
      presence of 0.5 mM palmitate, when stimulatory secretion of insulin was reduced 
      or basal secretion was elevated, respectively. RESULTS: After culture, cells were 
      protein profiled by SELDI-TOF-MS and 2D-PAGE. Differentially expressed proteins 
      were discovered and identified by peptide mass fingerprinting. Complimentary 
      protein profiles were obtained by the two approaches with SELDI-TOF-MS being more 
      efficient in separating proteins in the low molecular range and 2D-PAGE in the 
      high molecular range. Identified proteins included alpha glucosidase, calmodulin, 
      gars, glucose-6-phosphate dehydrogenase, heterogenous nuclear ribonucleoprotein 
      A3, lon peptidase, nicotineamide adenine dinucleotide hydrogen (NADH) 
      dehydrogenase, phosphoglycerate kinase, proteasome p45, rab2, pyruvate kinase and 
      t-complex protein. The observed glucose-induced differential protein expression 
      pattern indicates enhanced glucose metabolism, defense against reactive oxygen 
      species, enhanced protein translation, folding and degradation and decreased 
      insulin granular formation and trafficking. Palmitate-induced changes could be 
      related to altered exocytosis. CONCLUSION: The identified altered proteins 
      indicate mechanism important for altered beta-cell function in T2DM.
FAU - Sol, E-ri M
AU  - Sol ER
AD  - Department of Medical Cell Biology, Uppsala University, Sweden. 
      E-ri.Sol@mcb.uu.se
FAU - Hovsepyan, Meri
AU  - Hovsepyan M
FAU - Bergsten, Peter
AU  - Bergsten P
LA  - eng
PT  - Journal Article
DEP - 20090716
PL  - England
TA  - Proteome Sci
JT  - Proteome science
JID - 101170539
PMC - PMC2732594
EDAT- 2009/07/18 09:00
MHDA- 2009/07/18 09:01
PMCR- 2009/07/16
CRDT- 2009/07/18 09:00
PHST- 2009/02/16 00:00 [received]
PHST- 2009/07/16 00:00 [accepted]
PHST- 2009/07/18 09:00 [entrez]
PHST- 2009/07/18 09:00 [pubmed]
PHST- 2009/07/18 09:01 [medline]
PHST- 2009/07/16 00:00 [pmc-release]
AID - 1477-5956-7-24 [pii]
AID - 10.1186/1477-5956-7-24 [doi]
PST - epublish
SO  - Proteome Sci. 2009 Jul 16;7:24. doi: 10.1186/1477-5956-7-24.