Talk:Lecture - Integumentary Development: Difference between revisions

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* [http://embryology.med.unsw.edu.au/embryology/index.php?title=Lecture_-_Integumentary_Development&oldid=132743 2013]
* [http://embryology.med.unsw.edu.au/embryology/index.php?title=Lecture_-_Integumentary_Development&oldid=132743 2013]
** [http://lectopia.telt.unsw.edu.au/lectopia/lectopia.lasso?ut=153&id=140225 Lecture 18 - Integumentary Development]  Lecture Date: 2013-10-08  Lecture Time: 16:00 Venue: Biomedical Theatre E Speaker: Annemiek Beverdam
* [[2010_Lecture_22|2010]]
* [[2010_Lecture_22|2010]]



Revision as of 07:48, 13 September 2014

Lecture History

Keratins

  • Keratins are the major structural proteins of the vertebrate epidermis and its appendages, constituting up to 85% of a fully differentiated keratinocyte.
  • Together with actin microfilaments and microtubules, keratin filaments make up the cytoskeletons of vertebrate epithelial cells.
  • Traced as far back in the evolutionary kingdom as mollusks, keratins belong to the superfamily of intermediate filament (IF) proteins that form alpha-helical coiled-coil dimers which associate laterally and end-to-end to form 10-nm diameter filaments.
  • The evolutionary transition between organisms bearing an exoskeleton and those with an endoskeleton seemed to cause considerable change in keratin.
  • Keratins expanded from a single gene to a multigene family. Of the approximately 60 IF genes in the human genome, half encode keratins, and at least 18 of these are expressed in skin.
  • Vertebrate keratins are subdivided into two sequence types (I and II) that are typically coexpressed as specific pairs with complex expression patterns.
  • The filament-forming capacity of a pair is dependent upon its intrinsic ability to self-assemble into coiled-coil heterodimers, a feature not required of the invertebrate keratins (Weber et al 1988).
  • Approximately 20,000 heterodimers of type I and type II keratins assemble into an IF. Mutations that perturb keratin filament assembly in vitro can cause blistering human skin disorders in vivo.

(text from Review Article)