Epidermal and hair follicle trans glutaminases and crosslinking in skin
β Scribed by Larry L. Peterson; Kirk D. Wuepper
- Book ID
- 104678566
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 870 KB
- Volume
- 58
- Category
- Article
- ISSN
- 0300-8177
No coin nor oath required. For personal study only.
β¦ Synopsis
Epidermal and hair follicle transglutaminases crosslink structural proteins in the skin by epsilon-(gamma-glutamyl)-lysine bonds. This crosslinking produces protein polymers that are extremely insoluble and, until recently, difficult to characterize. Epidermal transglutaminase is localized to the granular layer of the epidermis. It catalyzes the crosslinking of a soluble cytoplasmic precursor to form the cornified envelope that lines the inner membrane of the mature keratinocyte in the stratum corneum. Hair follicle transglutaminase is localized to the inner root sheath and medulla of the hair follicle. It crosslinks a poorly characterized citrulline-rich protein. The enzymes and their substrates have been shown to be important markers of normal differentiation. Regulation of these processes is currently under investigation.
π SIMILAR VOLUMES
The innervation of normal, mature mammalian skin is widely thought to be constant. However, the extensive skin remodeling accompanying the transformation of hair follicles from resting stage through growth and regression back to resting (telogen-anagen-catagentelogen) may also be associated with alt