Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.6K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
3.6K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.9K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.9K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

6.2K
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
6.2K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

3.4K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.4K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.6K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.6K
Cell Motility through Blebbing01:16

Cell Motility through Blebbing

2.3K
Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
In multicellular...
2.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Protocol for isolation of lipid-laden hepatocytes from high-fat diet-fed and metabolically challenged mice.

STAR protocols·2026
Same author

Molecularly imprinted polymers as next-generation weapons against the AMR crisis.

Journal of materials chemistry. B·2026
Same author

Lipid metabolism and neurodegeneration: Mechanistic insights and therapeutic targets.

Ageing research reviews·2026
Same author

Mass Spectrometry Profiling of Therapeutic Antibodies in Multiple Myeloma: <i>m</i>/<i>z</i> Features and Concordance with Immunofixation Electrophoresis.

Biomedicines·2025
Same author

Drug Development.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025
Same author

Correction: Cholesterol depletion inhibits Na+,K+-ATPase activity in a near-native membrane environment.

The Journal of biological chemistry·2025

Related Experiment Video

Updated: Dec 13, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.3K

Inflammation-induced PINCH expression leads to actin depolymerization and mitochondrial mislocalization in neurons.

Kalimuthusamy Natarajaseenivasan1,2, Santhanam Shanmughapriya3, Prema Velusamy3

  • 1Department of Neurosciences and Center for Neurovirology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA, 19140, USA.

Translational Neurodegeneration
|August 5, 2020
PubMed
Summary

Neuroinflammation increases the Particularly Interesting New Cysteine Histidine-Rich Protein (PINCH) in neurons, disrupting mitochondrial function and metabolism. Maintaining normal PINCH levels may offer a new therapeutic strategy for neurodegenerative diseases.

Keywords:
ActinMitochondriaNeuroinflammationNeuronPINCH

More Related Videos

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

4.5K
Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
10:13

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

Published on: February 10, 2016

12.6K

Related Experiment Videos

Last Updated: Dec 13, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.3K
A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

4.5K
Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
10:13

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

Published on: February 10, 2016

12.6K

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Chronic neuroinflammation is linked to metabolic changes in the central nervous system (CNS).
  • Human immunodeficiency virus (HIV) and Alzheimer's disease (AD) patients exhibit metabolic disturbances, but the mechanisms connecting inflammation, neurodegeneration, and energy deficits are unclear.
  • The protein PINCH (particularly interesting new cysteine histidine-rich-protein) is highly expressed in neurodegenerative diseases like HIV and AD, but its role is poorly understood.

Purpose of the Study:

  • To investigate the regulatory mechanisms of PINCH-mediated changes in neuronal bioenergetics and mitochondrial localization.
  • To identify factors involved in actin depolymerization and mitochondrial mislocalization due to PINCH.
  • To confirm PINCH specificity and restore protein complex communication using inhibition experiments.

Main Methods:

  • Investigated PINCH protein-mediated effects on bioenergetics and mitochondrial localization in neurons exposed to TNFα or HIV Tat protein.
  • Assessed changes in the PINCH-ILK-Parvin (PIP) complex association with cofilin and TESK1.
  • Utilized lentiviral and pharmacological inhibition to confirm PINCH specificity and restore protein complex function.

Main Results:

  • Identified MEF2A as the transcription factor for PINCH in neuroinflammation.
  • Demonstrated that TNFα-induced MEF2A activation increases PINCH, disrupting the PIP complex, inactivating TESK1, and causing actin depolymerization.
  • Showed that actin disruption leads to perinuclear mitochondrial mislocalization, impairing neuronal metabolism; blocking PINCH expression preserved mitochondrial localization and metabolism.

Conclusions:

  • This study elucidates the mechanistic and biological consequences of PINCH expression in CNS neurons during chronic neuroinflammation.
  • Findings highlight the potential of maintaining physiological PINCH levels as a therapeutic target for neurodegenerative diseases with metabolic dysfunction.