Related Experiment Video

Updated: Jun 30, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Protein kinase C regulates the expression of M1 receptors and BDNF in rat retinal cells

Aline Araujo dos Santos1, Simone Vidal Medina, Leandro de Araújo Martins

  • 1Departamento de Neurobiologia, Programa de Neuroimunologia, Instituto de Biologia, Centro de Estudos Gerais, Universidade Federal Fluminense, Niterói, Rio de Janeiro,Brazil.

Neurochemical Research
|September 20, 2008
PubMed

Insights

Protein kinase C (PKC) activation by PMA decreases retinal cell proliferation, mediated by M1 receptors and BDNF. This study reveals PKC

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Protein kinase C (PKC) is crucial for cell proliferation, survival, and differentiation.
  • Previous research indicated phorbol 12-myristate 13-acetate (PMA), a PKC activator, reduces retinal cell proliferation.
  • Muscarinic type 1 receptors (M1) and brain-derived neurotrophic factor (BDNF) were implicated in this proliferation decrease.

Purpose of the Study:

  • To investigate the impact of PMA on M1 receptor and BDNF expression in retinal cells.
  • To analyze the expression patterns of M1 receptors and BDNF during postnatal retinal development in vivo.
  • To elucidate the role of PKC in regulating M1 receptor expression within retinal cells.

Main Methods:

  • Retinal cell cultures were treated with PMA to assess M1 receptor and BDNF protein expression over time (45 min and 48 h).
  • In vivo studies examined M1 receptor and BDNF expression during postnatal retinal development.
  • Western blot or similar protein quantification techniques were likely employed.

Main Results:

  • PMA treatment led to a decrease in both M1 receptor and BDNF protein expression after 48 hours.
  • A transient increase in BDNF expression and a decrease in M1 receptor expression were observed at 45 minutes post-PMA treatment.
  • In vivo analysis showed a general decrease in M1 receptor and BDNF expression during postnatal development.

Conclusions:

  • PKC activation influences M1 receptor expression in retinal cells.
  • The findings suggest a complex regulatory relationship between PKC, M1 receptors, and BDNF in retinal cell function.
  • PKC may play a significant role in controlling M1 receptor levels in the developing and mature retina.

More Related Videos

Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis11:08

Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis

Published on: December 7, 2021

Developing a Rat Model for Bipolar Disorder04:42

Developing a Rat Model for Bipolar Disorder

Published on: May 2, 2025

Related Concept Videos

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...
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 rapamycin-insensitive companion...
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,...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...