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
- 2013
- Lecture 18 - Integumentary Development Lecture Date: 2013-10-08 Lecture Time: 16:00 Venue: Biomedical Theatre E Speaker: Annemiek Beverdam
- 2010
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)