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

Muscles of the Eye01:20

Muscles of the Eye

The muscles of the eye are sophisticated structures that control eye movement and focus, allowing for the precise and rapid adjustments necessary for vision. The human eye is controlled by ten muscles — six extraocular muscles, three intraocular muscles, and one primary eyelid retractor muscle.
Extraocular Muscles
The six extraocular muscles surround the eyeball and control its movements. They are responsible for a wide range of eye motions, including looking up, down, left, right, and rotating...
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
The Sarcomere01:08

The Sarcomere

A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each myosin...
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.
Accessory Structures of the Eye01:17

Accessory Structures of the Eye

Optical perception, or vision, is an extraordinary sense dependent on converting light signals received via the ocular organs. These organs, known as eyes, are securely positioned within the bony cavities of the skull, called orbits. The orbits serve a dual purpose: a protective shield for the ocular globes and a stable attachment point for the soft ocular tissues. The eye's external protective mechanisms include the eyelids, which are edged with lashes that act as a barrier against foreign...
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...

You might also read

Related Articles

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

Sort by
Same author

Examination of respiratory syncytial virus fusion protein proteolytic processing and roles of the P27 domain.

Journal of virology·2024
Same author

RIT1 regulation of CNS lipids RIT1 deficiency Alters cerebral lipid metabolism and reduces white matter tract oligodendrocytes and conduction velocities.

Heliyon·2023
Same author

Imaging analysis reveals budding of filamentous human metapneumovirus virions and direct transfer of inclusion bodies through intercellular extensions.

mBio·2023
Same author

Human Metapneumovirus Phosphoprotein Independently Drives Phase Separation and Recruits Nucleoprotein to Liquid-Like Bodies.

mBio·2022
Same author

Analysis of Hendra Virus Fusion Protein N-Terminal Transmembrane Residues.

Viruses·2021
Same author

Effect of clinical isolate or cleavage site mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell-cell fusion.

The Journal of biological chemistry·2021

Related Experiment Video

Updated: Jul 19, 2026

Ocular Kinematics Measured by In Vitro Stimulation of the Cranial Nerves in the Turtle
10:49

Ocular Kinematics Measured by In Vitro Stimulation of the Cranial Nerves in the Turtle

Published on: June 2, 2018

Nebulin isoforms of extraocular muscle.

Carole L Moncman1, Francisco H Andrade

  • 1Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA. cmonc2@uky.edu

Cell and Tissue Research
|October 21, 2006
PubMed
Summary

Extraocular muscles (EOMs) exhibit unique protein compositions, including cardiac myosin. Research shows EOMs express titin isoforms similar to other skeletal muscles and a nebulin isoform characteristic of fast-twitch muscles, not nebulette.

Area of Science:

  • Muscle physiology
  • Skeletal muscle biochemistry
  • Ocular biomechanics

Background:

  • Extraocular muscles (EOMs) possess unique biochemical and ultrastructural properties distinct from other skeletal muscles.
  • Rodent EOMs notably lack M-lines and express EOM-specific myosin heavy chain (MYH13) and alpha-cardiac myosin heavy chain.
  • Gene-expression profiling suggests the presence of other cardiac-specific proteins in adult EOMs.

Purpose of the Study:

  • To investigate the expression of nebulin and titin isoforms in EOMs.
  • To clarify the presence of nebulette versus nebulin in EOMs.
  • To characterize the titin isoforms within EOMs.

Main Methods:

  • Gel electrophoresis and immunological analyses were employed.
  • Protein isoforms of titin and nebulin in EOMs were identified.

More Related Videos

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
08:57

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

Published on: February 4, 2021

Related Experiment Videos

Last Updated: Jul 19, 2026

Ocular Kinematics Measured by In Vitro Stimulation of the Cranial Nerves in the Turtle
10:49

Ocular Kinematics Measured by In Vitro Stimulation of the Cranial Nerves in the Turtle

Published on: June 2, 2018

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
08:57

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

Published on: February 4, 2021

  • Comparative analysis with soleus and extensor digitorum longus (EDL) muscles was performed.

    • Main Results:

    • Titin isoforms in EOMs closely resemble those found in soleus and EDL skeletal muscles.
    • EOMs express cardiac myosin isoforms but do not express nebulette.
    • A nebulin isoform consistent with that of the fast hindlimb muscle EDL was identified in EOMs.

    Conclusions:

    • EOMs exhibit a unique protein profile, incorporating cardiac myosin but lacking nebulette.
    • The titin and nebulin isoform composition in EOMs aligns with characteristics of other skeletal muscles, particularly fast-twitch fibers.