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Related Concept Videos

Translation01:31

Translation

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Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
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Translation01:31

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Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
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Bone Disorders01:29

Bone Disorders

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Aging and its effect on bone remodeling is the most common cause of bone disorders. In young and healthy people, bone deposition and resorption happen at an equal rate to maintain optimal bone health.
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Bone Formation by Intramembranous Ossification01:29

Bone Formation by Intramembranous Ossification

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Intramembranous ossification is one of the two processes involved in the development of bones within an embryo. The flat bones of the face, most of the cranial bones, and the clavicles are formed via this process. During intramembranous ossification, the bones develop directly from sheets of undifferentiated mesenchymal connective tissue.
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Fractures: Bone Repair01:27

Fractures: Bone Repair

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Treatment for a fracture is based on the type of break, the bone affected, and the patient's age.
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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...
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Related Experiment Video

Updated: Apr 11, 2026

Laser Capture Microdissection of Mouse Embryonic Cartilage and Bone for Gene Expression Analysis
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IFITM5 mutations and osteogenesis imperfecta.

Nobutaka Hanagata1,2

  • 1Nanotechnology Innovation Station, National Institute for Materials Science, 1-2-1 Sengen, Tsukuba, Ibaraki, 305-0047, Japan. Hanagata.Nobutaka@nims.go.jp.

Journal of Bone and Mineral Metabolism
|June 3, 2015
PubMed
Summary

Interferon-induced transmembrane protein 5 (IFITM5) mutations are linked to osteogenesis imperfecta (OI). This review explores how IFITM5 mutations cause OI, despite its unclear in vivo function.

Keywords:
Heterozygous mutationIFITM5Osteogenesis imperfecta type V

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Area of Science:

  • Bone biology
  • Genetics
  • Molecular mechanisms of disease

Background:

  • Interferon-induced transmembrane protein 5 (IFITM5) is an osteoblast-specific protein regulating mineralization in vitro.
  • IFITM5 knockout mice show no significant bone abnormalities, indicating its in vivo function is not fully understood.
  • Mutations in IFITM5 have been associated with osteogenesis imperfecta (OI), a bone fragility disorder.

Purpose of the Study:

  • To review the current understanding of osteogenesis imperfecta pathological mechanisms.
  • To investigate the role of IFITM5 mutations in OI pathogenesis.
  • To elucidate the mystery behind IFITM5's involvement in OI despite its unclear in vivo bone formation role.

Main Methods:

  • Literature review of studies on IFITM5 and osteogenesis imperfecta.
  • Analysis of genetic data linking IFITM5 mutations to OI phenotypes.
  • Synthesis of existing knowledge on bone mineralization and IFITM5 function.

Main Results:

  • IFITM5 mutations, including in the 5' untranslated and coding regions, are identified in OI patients.
  • Specific IFITM5 mutations correlate with varying severity of OI symptoms.
  • The precise mechanism by which IFITM5 mutations lead to OI remains under investigation.

Conclusions:

  • IFITM5 plays a critical role in OI pathogenesis, likely through mechanisms beyond direct bone formation.
  • Further research is needed to fully understand the molecular pathways linking IFITM5 mutations to bone fragility in OI.
  • Targeting IFITM5 pathways may offer therapeutic potential for osteogenesis imperfecta.