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

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

You might also read

Related Articles

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

Sort by
Same author

Gelatinous drop-like amyloid in FOXC2 distichiasis syndrome: a case report.

BMC ophthalmology·2026
Same author

Autophagy and mitophagy at the synapse and beyond: implications for learning, memory and neurological disorders.

Autophagy·2025
Same author

Epidrug screening identifies type I PRMT inhibitors as modulators of lysosomal exocytosis and drug sensitivity in cancers.

Cell death & disease·2025
Same author

Tectonic Corneal Transplant in the Management of Congenital Anterior Staphyloma.

Cornea·2025
Same author

Novel Kinesin Family Member 1A Variants Linked to Atypical Parkinsonism Elicit Altered Neuronal Transactive Response DNA Binding Protein 43 kDa Interactions and Dendritic Atrophy.

The American journal of pathology·2025
Same author

The Role of Autophagy in Excitotoxicity, Synaptic Mitochondrial Stress and Neurodegeneration.

Autophagy reports·2025

Related Experiment Video

Updated: Jul 19, 2026

Modeling Mitochondrial Disease Using Brain Organoids: A Focus on Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like Episodes
08:56

Modeling Mitochondrial Disease Using Brain Organoids: A Focus on Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like Episodes

Published on: October 10, 2025

Mitochondrial aberrations in mucolipidosis Type IV.

John J Jennings1, Jian-Hui Zhu, Youssef Rbaibi

  • 1Department of Biological Science, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.

The Journal of Biological Chemistry
|October 24, 2006
PubMed
Summary

Mucolipidosis type IV and other lysosomal storage diseases cause mitochondrial fragmentation due to impaired autophagolysosomal recycling. This leads to calcium dysregulation and increased apoptosis, suggesting a common cell death mechanism.

More Related Videos

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

Published on: November 23, 2011

Related Experiment Videos

Last Updated: Jul 19, 2026

Modeling Mitochondrial Disease Using Brain Organoids: A Focus on Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like Episodes
08:56

Modeling Mitochondrial Disease Using Brain Organoids: A Focus on Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like Episodes

Published on: October 10, 2025

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

Published on: November 23, 2011

Area of Science:

  • Cell Biology
  • Genetics
  • Neuroscience

Background:

  • Mucolipidosis type IV (MLIV) is a genetic lysosomal storage disease linked to MCOLN1 gene mutations, causing brain and eye degeneration.
  • The exact link between lysosomal dysfunction and MLIV's degenerative effects remains unclear.

Purpose of the Study:

  • To investigate the relationship between lysosomal dysfunction and mitochondrial alterations in MLIV and other lysosomal storage diseases.
  • To explore the role of mitochondrial calcium buffering and apoptosis in the pathogenesis of these diseases.

Main Methods:

  • Comparative analysis of mitochondrial structure and function in MLIV patient cells and control cells.
  • Experimental induction of lysosomal and autophagy inhibition in control cells to mimic disease phenotypes.
  • Assessment of mitochondrial calcium buffering capacity and apoptosis sensitivity.

Main Results:

  • MLIV and other lysosomal storage diseases exhibit significant mitochondrial fragmentation and reduced mitochondrial calcium buffering.
  • Mitochondrial defects are replicated by lysosomal and autophagy inhibition, suggesting impaired autophagolysosomal recycling.
  • Cells with decreased mitochondrial calcium buffering show heightened apoptosis sensitivity via a caspase-8 pathway.

Conclusions:

  • Inefficient autophagolysosomal recycling of mitochondria contributes to mitochondrial dysfunction in MLIV and related diseases.
  • Deficient mitochondrial calcium homeostasis is a potential common mechanism driving degenerative cell death in lysosomal storage diseases.