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

Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

3.2K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
3.2K
Structural Protein Function01:56

Structural Protein Function

30.2K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
30.2K
Fibril-associated Collagen01:11

Fibril-associated Collagen

3.4K
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
3.4K
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

3.8K
Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl...
3.8K
Phases of Wound Repair01:28

Phases of Wound Repair

9.1K
Following injury, the integrity of the injured tissues must be reestablished. For example, in skin tissue, wound repair involves coordination among resident skin cells, blood mononuclear cells, extracellular matrix, growth factors, and cytokines to complete the healing cascade.
Formation of Blood Clot
In case of deep injuries, trauma to blood vessels results in blood loss. In the meantime, phospholipids released from the ruptured endothelial cellular membrane are converted into arachidonic...
9.1K
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

3.5K
Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
3.5K

You might also read

Related Articles

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

Sort by
Same author

Molecular mapping of a novel non-canonical gibberellin-sensitive dwarfing gene Rht29 in wheat (Triticum aestivum).

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2026
Same author

Haplotype-resolved methylomes reveal parent-of-origin DNA methylation imbalance in autism spectrum disorder.

Science advances·2026
Same author

CHST5 gene mutations contribute to high myopia by disrupting collagen fiber organization.

Journal of genetics and genomics = Yi chuan xue bao·2026
Same author

Programmable mRNA 3'UTR engineering restores MHC-I and overcomes immune evasion in prostate cancer.

Nature biomedical engineering·2026
Same author

Evidence supporting the role of GIGYF2 in synapse development and autism.

Molecular psychiatry·2026
Same author

OTULIN protects hyperoxia-induced neonatal lung injury and modulates mitochondrial protein OPA1 in association with the E3 ubiquitin ligase RNF31.

Cellular & molecular biology letters·2026

Related Experiment Video

Updated: Feb 28, 2026

Assessment and Characterization of Hyaloid Vessels in Mice
08:22

Assessment and Characterization of Hyaloid Vessels in Mice

Published on: May 15, 2019

9.8K

P4HA2 Participates in Pathogenesis of Refractive Error by Regulating Collagen Posttranslational Modification and

Yanling Liu1,2, Shanshan Dong3, Furong Huang4

  • 1Center for Medical Genetics & Hunan Key Laboratory of Medical Genetics, School of Life Sciences, Central South University, Changsha, Hunan, China, csu.edu.cn.

Human Mutation
|February 27, 2026
PubMed
Summary

The P4HA2 gene is crucial for maintaining eye structure. Its deficiency leads to collagen degeneration and vision impairment, contributing to high myopia progression.

Keywords:
collagen hydroxylationcollagen thermal stabilityextracellular matrix (ECM)high myopia (HM)prolyl 4-hydroxylase ii (P4HA2)refractive error

More Related Videos

Preparing Porcine Eyes for Confocal Reflectance Microscopy to Visualize the Vitreous Collagen Fiber Network
06:07

Preparing Porcine Eyes for Confocal Reflectance Microscopy to Visualize the Vitreous Collagen Fiber Network

Published on: October 17, 2025

398
Scleral Cross-linking Using Riboflavin and Ultraviolet-A Radiation for Prevention of Axial Myopia in a Rabbit Model
05:56

Scleral Cross-linking Using Riboflavin and Ultraviolet-A Radiation for Prevention of Axial Myopia in a Rabbit Model

Published on: April 3, 2016

9.4K

Related Experiment Videos

Last Updated: Feb 28, 2026

Assessment and Characterization of Hyaloid Vessels in Mice
08:22

Assessment and Characterization of Hyaloid Vessels in Mice

Published on: May 15, 2019

9.8K
Preparing Porcine Eyes for Confocal Reflectance Microscopy to Visualize the Vitreous Collagen Fiber Network
06:07

Preparing Porcine Eyes for Confocal Reflectance Microscopy to Visualize the Vitreous Collagen Fiber Network

Published on: October 17, 2025

398
Scleral Cross-linking Using Riboflavin and Ultraviolet-A Radiation for Prevention of Axial Myopia in a Rabbit Model
05:56

Scleral Cross-linking Using Riboflavin and Ultraviolet-A Radiation for Prevention of Axial Myopia in a Rabbit Model

Published on: April 3, 2016

9.4K

Area of Science:

  • Ophthalmology
  • Genetics
  • Biochemistry

Background:

  • High myopia (HM) pathogenesis is not fully understood, despite identified genetic links.
  • Previous research implicated a mutation in the P4HA2 gene in HM development.

Purpose of the Study:

  • To investigate the functional role of P4HA2 in high myopia.
  • To elucidate the molecular mechanisms by which P4HA2 influences refractive error.

Main Methods:

  • Generation of P4HA2-knockout mouse models (P4ha2-/-) and HEK293 cell lines.
  • Biometric assessments to evaluate visual acuity and light transmission.
  • Analysis of collagen fibril arrangement, hydroxylation, fibronectin, and Collagen I expression in ocular tissues and cells.

Main Results:

  • P4ha2-/- mice displayed impaired visual acuity and disrupted light transmission.
  • Reduced collagen hydroxylation in P4ha2-/- mice led to collagen fibril disorganization and decreased thermal stability.
  • Elevated fibronectin and reduced Collagen I levels were observed, indicating extracellular matrix imbalance.

Conclusions:

  • P4HA2 is essential for maintaining collagen integrity and ocular structure.
  • Reduced P4HA2 function accelerates collagen degeneration via decreased hydroxylation, contributing to high myopia pathogenesis.
  • P4HA2 deficiency disrupts extracellular matrix homeostasis, leading to refractive error progression.