Abstract |
Transglutaminases (TGase), a family of cross-linking enzymes present in most cell types, are important in events as diverse as cell-signaling and matrix stabilization. Transglutaminase 1 is crucial in developing the epidermal barrier, however the skin also contains other family members, in particular TGase 3. This isoform is highly expressed in the cornified layer, where it is believed to stabilize the epidermis and its reduction is implicated in psoriasis. To understand the importance of TGase 3 in vivo we have generated and analyzed mice lacking this protein. Surprisingly, these animals display no obvious defect in skin development, no overt changes in barrier function or ability to heal wounds. In contrast, hair lacking TGase 3 is thinner, has major alterations in the cuticle cells and hair protein cross-linking is markedly decreased. Apparently, while TGase 3 is of unique functional importance in hair, in the epidermis loss of TGase 3 can be compensated for by other family members.
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Authors | Susan John, Lars Thiebach, Christian Frie, Sharada Mokkapati, Manuela Bechtel, Roswitha Nischt, Sally Rosser-Davies, Mats Paulsson, Neil Smyth |
Journal | PloS one
(PLoS One)
Vol. 7
Issue 4
Pg. e34252
( 2012)
ISSN: 1932-6203 [Electronic] United States |
PMID | 22496784
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Tgm3 protein, mouse
- Transglutaminases
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Topics |
- Animals
- Cornea
(cytology, enzymology)
- Epidermal Cells
- Epidermis
(enzymology)
- Female
- Fluorescent Antibody Technique
- Hair Follicle
(enzymology, growth & development)
- Immunoblotting
- Male
- Mice
- Mice, Inbred C57BL
- Mice, Knockout
- Microscopy, Electron, Scanning
- Microscopy, Electron, Transmission
- Phenotype
- Skin
(cytology, enzymology)
- Transglutaminases
(physiology)
- Wound Healing
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