RGD Reference Report - Proteomic characterization of protein phosphatase 1 complexes in ischemia-reperfusion and ischemic tolerance. - Rat Genome Database

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Proteomic characterization of protein phosphatase 1 complexes in ischemia-reperfusion and ischemic tolerance.

Authors: Cid, C  Garcia-Bonilla, L  Camafeita, E  Burda, J  Salinas, M  Alcazar, A 
Citation: Cid C, etal., Proteomics. 2007 Sep;7(17):3207-18.
RGD ID: 2293745
Pubmed: PMID:17683050   (View Abstract at PubMed)
DOI: DOI:10.1002/pmic.200700214   (Journal Full-text)

Serine/threonine protein phosphatase 1 (PP1) regulates multiple cellular processes. Protein phosphorylation-dephosphorylation is largely altered during ischemia and subsequent reperfusion. The brain is particularly vulnerable to stress resulting from ischemia-reperfusion (IR), however, the acquisition of ischemic tolerance (IT) protects against IR stress. We studied PP1 complexes in response to IR stress and IT in brain using proteomic characterization of PP1 complexes in animal models of IR and IT. PP1alpha and PP1gamma were immunoprecipitated and resolved by 2-D. DIGE analysis detected 14 different PP1-interacting proteins that exhibited significant changes in their association with PP1alpha or PP1gamma. These proteins were identified by MALDI-TOF MS. Seven had the PP1-binding RVxF motif. IR altered the interaction of heat shock cognate 71 kDa-protein, creatine kinase B, and dopamine- and cAMP-regulated phosphoprotein 32 kDa (DARPP32) with both PP1alpha and PP1gamma, and the interaction of phosphodiesterase-6B, transitional ER ATPase, lamin-A, glucose-regulated 78 kDa-protein, dihydropyrimidinase-related protein-2, gamma-enolase, neurofilament-L, and ubiquitin ligase SIAH2 with PP1gamma. IT prevented most of the IR-induced effects. This study identifies novel PP1alpha- and PP1gamma-interacting proteins and reveals an in vivo modularity of PP1 holoenzymes in response to physiological ischemic stress. It supports a potential role of PP1 in IR stress and as a target of the endogenous protective mechanisms induced by IT.



RGD Manual Disease Annotations    Click to see Annotation Detail View

  

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Ppp1ccRatlamin binding  IPILmna (Rattus norvegicus) RGD 
LmnaRatprotein phosphatase 1 binding  IPIPpp1cc (Rattus norvegicus) RGD 

Objects Annotated

Genes (Rattus norvegicus)
Eno2  (enolase 2)
Lmna  (lamin A/C)
Ppp1cc  (protein phosphatase 1 catalytic subunit gamma)

Genes (Mus musculus)
Eno2  (enolase 2, gamma neuronal)
Lmna  (lamin A)

Genes (Homo sapiens)
ENO2  (enolase 2)
LMNA  (lamin A/C)


Additional Information