Potential correlation between carbohydrate‐active enzyme family 48 expressed by gut microbiota and the expression of intestinal epithelial AMP‐activated protein kinase β

2019 ◽  
Vol 44 (2) ◽  
Author(s):  
Qian Li ◽  
Min Zhang ◽  
Tao Wu ◽  
Rui Liu
Keyword(s):  
Protein Kinase ◽  
Gut Microbiota ◽  
Active Enzyme ◽  
Intestinal Epithelial ◽  
Carbohydrate Active Enzyme ◽  
Enzyme Family ◽  
Amp Activated Protein Kinase

scholarly journals Deletion of intestinal epithelial AMP-activated protein kinase alters distal colon permeability but not glucose homeostasis

2021 ◽  
Vol 47 ◽  
pp. 101183
Author(s):  
Séverine Olivier ◽  
Camille Pochard ◽  
Hanna Diounou ◽  
Vanessa Castillo ◽  
Jordane Divoux ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Glucose Homeostasis ◽  
Distal Colon ◽  
Intestinal Epithelial ◽  
Amp Activated Protein Kinase

scholarly journals A carbohydrate-active enzyme (CAZy) profile links successful metabolic specialization of Prevotella to its abundance in gut microbiota

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Juhani Aakko ◽  
Sami Pietilä ◽  
Raine Toivonen ◽  
Anne Rokka ◽  
Kati Mokkala ◽  
...  
Keyword(s):  
Gut Microbiota ◽  
Active Enzyme ◽  
Carbohydrate Active Enzyme

scholarly journals Activation of AMP-Activated Protein Kinase by a Plant-Derived Dihydroisosteviol in Human Intestinal Epithelial Cell

2013 ◽  
Vol 36 (4) ◽  
pp. 522-528 ◽  
Author(s):  
Chatchai Muanprasat ◽  
Lalida Sirianant ◽  
Sutthipong Sawasvirojwong ◽  
Sureeporn Homvisasevongsa ◽  
Apichart Suksamrarn ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Intestinal Epithelial ◽  
Human Intestinal Epithelial Cell ◽  
Amp Activated Protein Kinase

scholarly journals Polyamines modulate the subcellular localization of RNA-binding protein HuR through AMP-activated protein kinase-regulated phosphorylation and acetylation of importin α1

2007 ◽  
Vol 409 (2) ◽  
pp. 389-398 ◽  
Author(s):  
Tongtong Zou ◽  
Lan Liu ◽  
Jaladanki N. Rao ◽  
Bernard S. Marasa ◽  
Jie Chen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Subcellular Localization ◽  
Nuclear Import ◽  
Rna Binding ◽  
Binding Protein ◽  
Phosphorylation Site ◽  
Rna Binding Protein ◽  
Intestinal Epithelial ◽  
Ampk Activation ◽  
Amp Activated Protein Kinase

Polyamines are required for maintenance of intestinal epithelial integrity, and a decrease in cellular polyamines increases the cytoplasmic levels of RNA-binding protein HuR stabilizing p53 and nucleophosmin mRNAs, thus inhibiting IEC (intestinal epithelial cell) proliferation. The AMPK (AMP-activated protein kinase), an enzyme involved in responding to metabolic stress, was recently found to be implicated in regulating the nuclear import of HuR. Here, we provide evidence showing that polyamines modulate subcellular localization of HuR through AMPK-regulated phosphorylation and acetylation of Impα1 (importin α1) in IECs. Decreased levels of cellular polyamines as a result of inhibiting ODC (ornithine decarboxylase) with DFMO (D,L-α-difluoromethylornithine) repressed AMPK activity and reduced Impα1 levels, whereas increased levels of polyamines as a result of ODC overexpression induced both AMPK and Impα1 levels. AMPK activation by overexpression of the AMPK gene increased Impα1 but reduced the cytoplasmic levels of HuR in control and polyamine-deficient cells. IECs overexpressing wild-type Impα1 exhibited a decrease in cytoplasmic HuR abundance, while cells overexpressing Impα1 proteins bearing K22R (lacking acetylation site), S105A (lacking phosphorylation site) or K22R/S105A (lacking both sites) mutations displayed increased levels of cytoplasmic HuR. Ectopic expression of these Impα1 mutants also prevented the increased levels of cytoplasmic HuR following polyamine depletion. These results indicate that polyamine-mediated AMPK activation triggers HuR nuclear import through phosphorylation and acetylation of Impα1 in IECs and that polyamine depletion increases cytoplasmic levels of HuR as a result of inactivation of the AMPK-driven Impα1 pathway.

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