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Related Concept Videos

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...
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...
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
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...
Introduction to Fibroblasts01:09

Introduction to Fibroblasts

Rudolph Virchow discovered spindle-shaped cells called fibroblasts in 1858. Inactive fibroblasts, called fibrocytes, become activated by various stimuli, such as growth factors and inflammatory cytokines. Activated fibroblasts play a crucial role in wound healing, inflammation, formation of new blood vessels, and cancer progression. Uncontrolled activation of fibroblasts results in fibrosis, the excess deposition of fibrous tissue, which can lead to scarring and affect normal organs. This...

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Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction
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Fibulins: multiple roles in matrix structures and tissue functions.

S de Vega1, T Iwamoto, Y Yamada

  • 1Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial Research, National Institutes of Health, DHHS, 30 Convent Drive MSC 4370, Bethesda, MD 20892-4370, USA.

Cellular and Molecular Life Sciences : CMLS
|February 4, 2009
PubMed
Summary

Fibulins are matrix glycoproteins crucial for tissue structure and remodeling. This review explores their structure, function, and roles in development and disease.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Fibulins are secreted glycoproteins integral to extracellular matrices, including basement membranes and elastic fibers.
  • They possess unique structural features, comprising epidermal growth factor-like modules and a C-terminal fibulin-type module.
  • Fibulins interact with diverse extracellular matrix components, mediating structural organization and cellular functions.

Purpose of the Study:

  • To review the structure and function of the fibulin protein family.
  • To discuss the implications of fibulins in biological processes, development, and diseases.
  • To consolidate current knowledge on fibulin's role as extracellular matrix organizers and mediators.

Main Methods:

  • Literature review of existing research on fibulins.
  • Analysis of data from in vitro studies.
  • Examination of findings from gene knockout mouse models.
  • Review of human genetic disorder studies involving fibulins.

Main Results:

  • Fibulins act as intermolecular bridges, forming supramolecular structures within the extracellular matrix.
  • They play significant roles in cellular processes and tissue remodeling.
  • Dysfunction or alterations in fibulin expression are linked to various human genetic disorders.

Conclusions:

  • Fibulins are essential multifunctional proteins with critical roles in maintaining tissue integrity and facilitating biological processes.
  • Their involvement in development and disease pathogenesis highlights their therapeutic potential.
  • Further research into fibulin biology is warranted to fully elucidate their complex functions and clinical relevance.