Activation of proteinase-activated receptor 2 prevents apoptosis of lung cancer cells

Related Experiment Video

Updated: May 6, 2026

Protein Transfection of Mouse Lung
04:21

Protein Transfection of Mouse Lung

Published on: May 15, 2013

9.0K

Shao-hong Huang1, Yun Li, Hui-guo Chen

  • 1Departments of 1 Cardiothoracic Surgery,2Anesthesiology, and3Medical Oncology, The Third Affiliated Hospital, Sun Yat-Sen University, Guangzhou, China.

Cancer Investigation
|October 22, 2013
PubMed

Insights

Protease-activated receptor 2 (PAR2) activation by tryptase increases epidermal growth factor receptor (EGFR) expression and suppresses apoptosis in lung cancer cells. This suggests PAR2 plays a role in lung cancer progression.

Area of Science:

  • Oncology
  • Molecular Biology
  • Immunoregulation

Background:

  • Lung cancer therapeutics remain unsatisfactory, with unclear pathogenesis.
  • Protease-activated receptors (PARs) are implicated in immunoregulation.
  • Understanding novel regulatory pathways in lung cancer is crucial.

Purpose of the Study:

  • To investigate the role of PAR2 activation in regulating EGFR expression in lung cancer (LC) cells.
  • To determine the effect of PAR2 activation on apoptosis of LC cells.
  • To elucidate the molecular mechanisms underlying PAR2-mediated effects on LC cell apoptosis.

Main Methods:

  • Exposure of A549 lung cancer cells to tryptase.
  • Quantification of EGFR expression levels.
  • Assessment of apoptosis using relevant biomarkers (Bax, Bcl-xL).

Main Results:

  • Tryptase exposure significantly increased EGFR expression in A549 cells.
  • Tryptase suppressed A549 cell apoptosis.
  • Tryptase decreased Bax expression and increased Bcl-xL levels, altering the Bax/Bcl-xL ratio.

Conclusions:

  • Activation of PAR2 by tryptase promotes lung cancer cell survival by upregulating EGFR and inhibiting apoptosis.
  • The observed changes in Bax and Bcl-xL expression indicate PAR2's role in modulating apoptotic pathways.
  • Targeting PAR2 may represent a novel therapeutic strategy for lung cancer.

More Related Videos

Author Spotlight: Developing Parmodulins to Target Protease-Activated Receptors for Inflammation Control07:13

Author Spotlight: Developing Parmodulins to Target Protease-Activated Receptors for Inflammation Control

Published on: May 24, 2024

1.1K
Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death09:18

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Published on: December 27, 2016

7.9K

Related Concept Videos

The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
6.2K
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
6.2K
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
8.7K
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...
10.3K
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...
5.2K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
15.3K