Related Experiment Video

Updated: Aug 13, 2025

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
08:04

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method

Published on: October 23, 2018

19.1K

P-21 Activated Kinases in Liver Disorders

Xun Qiu1,2, Hanzhi Xu1,2, Kai Wang1,3

  • 1Key Laboratory of Integrated Oncology and Intelligent Medicine of Zhejiang Province, Department of Hepatobiliary and Pancreatic Surgery, Affiliated Hangzhou First People's Hospital, Zhejiang University School of Medicine, Hangzhou 310006, China.

Cancers
|January 21, 2023
PubMed

Insights

p21 Activated Kinases (PAKs) are crucial in liver disorders like cancer and fibrosis. Inhibiting PAKs may offer new therapeutic strategies for these conditions.

Area of Science:

  • Molecular Biology
  • Hepatology
  • Oncology

Background:

  • p21 Activated Kinases (PAKs) are serine/threonine kinases regulating cell growth, survival, and migration.
  • PAKs are increasingly implicated in various liver pathologies, including cancer, fibrosis, and ischemia-reperfusion injury.

Purpose of the Study:

  • To review the role of PAKs in liver disorders.
  • To explore the mechanisms underlying PAK involvement in liver diseases.
  • To discuss the therapeutic potential of PAK inhibitors in liver conditions.

Main Methods:

  • Literature review of studies on PAKs in liver disorders.
  • Analysis of signaling pathways affected by PAKs in liver cells.
  • Evaluation of preclinical and clinical data on PAK inhibitors.

Main Results:

  • PAKs promote liver cancer growth, metastasis, and resistance to therapy.
  • PAKs are involved in the pathogenesis of hepatitis, liver fibrosis, and ischemia-reperfusion injury.
  • PAK activation influences multiple signaling pathways in diverse liver cell types.

Conclusions:

  • PAKs are significant contributors to liver disease progression.
  • Targeting PAKs with inhibitors presents a promising therapeutic avenue for liver disorders.
  • Further research is warranted to fully elucidate PAK functions and optimize inhibitor strategies.
Keywords:
hepatic ischemia-reperfusion injuryhepatitisliver cancerliver fibrosisp21 Activated Kinasesmall molecular inhibitors

More Related Videos

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.3K
Murine Precision-Cut Liver Slices as an Ex Vivo Model of Liver Biology12:36

Murine Precision-Cut Liver Slices as an Ex Vivo Model of Liver Biology

Published on: March 14, 2020

16.1K

Related Concept Videos

cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
6.5K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.8K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
6.4K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.3K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
5.8K
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
9.1K