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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

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...
Structural Protein Function01:56

Structural Protein Function

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 form...
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...

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Updated: Jun 13, 2026

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart
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Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart

Published on: March 26, 2015

Microfibril structure masks fibrillin-2 in postnatal tissues.

Noe L Charbonneau1, C Diana Jordan, Douglas R Keene

  • 1Shriners Hospital for Children, 3101 SW Sam Jackson Park Rd., Portland, OR 97239, USA.

The Journal of Biological Chemistry
|April 21, 2010
PubMed
Summary

Fibrillin-2

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Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart
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Isolation and Characterization of Adult Cardiac Fibroblasts and Myofibroblasts
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Area of Science:

  • Connective tissue biology
  • Molecular and cellular biology
  • Biochemistry

Background:

  • Fibrillin microfibrils are essential for connective tissue integrity.
  • Genetic defects in fibrillins cause connective tissue disorders.
  • Microfibril insolubility limits structural studies.

Purpose of the Study:

  • To investigate the role of fibrillin-2 in postnatal microfibril structure.
  • To understand microfibril structural evolution during development.

Main Methods:

  • Immunochemical approaches using monoclonal and polyclonal antibodies.
  • Studies on wild-type and fibrillin-1 null tissues.
  • Enzymatic digestion and genetic ablation techniques.

Main Results:

  • N-terminal fibrillin-2 epitopes are masked in postnatal microfibrils.
  • Masked epitopes are revealed by enzymatic digestion or Fbn1 ablation.
  • Fibrillin-2 forms an inner core in postnatal microfibrils.

Conclusions:

  • Microfibril structure evolves postnatally.
  • Fibrillin-2 plays a crucial role in the core structure of postnatal microfibrils.
  • Novel cryptic sites in fibrillin-1 highlight molecular complexity.