General Information:

Id: 533
Diseases: Alzheimer disease - [OMIM]
Amyotrophic lateral sclerosis
Homo sapiens
BTO:0000007 HEK-293 cell
article
Reference: Rudrabhatla P et al.(2008) Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein J. Biol. Chem. 283 [PMID: 18635547]

Interaction Information:

Comment EGF stimulation of HEK293 cells transiently transfected with NF-H increased the p-NF-H (phosphorylated NF-H), suggesting that MAPKs phosphorylate NF-H in vivo. DN-Pin1 (dominant-negative) inhibited the EGF induced p-NF-H in transfected HEK293 cells.
Formal Description
Interaction-ID: 2666

gene/protein

PIN1

increases_quantity of

protein modification

NEFH-mod

Drugbank entries Show/Hide entries for PIN1
Comment In EGF-treated transfected cells, endogenous Pin1 colocalized with p-NF-H (phosphorylated NF-H).
Formal Description
Interaction-ID: 2668

gene/protein

PIN1

interacts (colocalizes) with

protein modification

NEFH-mod

Drugbank entries Show/Hide entries for PIN1
Comment Experimental motor neuron disease models are characterized by oxidative stress leading to the accumulation of phospho-NFs within perikarya. Treatment of transfected HEK293 cells with H(2)O(2) resulted in 6-fold increase of phosphorylated NF-H.
Formal Description
Interaction-ID: 2671

increases_quantity of

protein modification

NEFH-mod

Comment Knockdown of Pin1 by Pin1 siRNA as well as DN-Pin1 (dominant-negative) significantly inhibited the increase in p-NF-H by H2O2.
Formal Description
Interaction-ID: 2672

gene/protein

PIN1

increases_quantity of

protein modification

NEFH-mod

induced by oxidative stress
Drugbank entries Show/Hide entries for PIN1
Comment Heat shock treatment of transfected HEK293 cells resulted in 5-fold increase of phosphorylated NF-H.
Formal Description
Interaction-ID: 2675

increases_quantity of

protein modification

NEFH-mod

Comment The deregulation of NF-H tail domain phosphorylation is correlated with neurodegenerative disorders such as Alzheimer disease (AD) and amyotrophic lateral sclerosis (ALS) in which aberrant tail domain phosphorylation occurs in neuronal perikarya.
Formal Description
Interaction-ID: 10798

disease

Amyotrophic lateral sclerosis

increases_quantity of

protein modification

NEFH-mod

Comment The deregulation of NF-H tail domain phosphorylation is correlated with neurodegenerative disorders such as Alzheimer disease (AD) and amyotrophic lateral sclerosis (ALS) in which aberrant tail domain phosphorylation occurs in neuronal perikarya.
Formal Description
Interaction-ID: 13602

increases_quantity of

protein modification

NEFH-mod