Abstract
Upon vigorous extraction with ionic detergent under reducing conditions, the macroscopic structures of mammalian hair, bird feather and horny teeth of the hagfish became swollen and flexible but were substantially preserved. In each case, removal in this way of solubilizable constituents, such as disulfide-bonded keratins and associated matrix proteins, left a residue of ε-(γ-glutamyl)lysine cross-linked protein. Residual features in hair included cell envelopes in the cortex, cell envelopes and intracellular deposits in the medulla, and nearly the entire cuticle cells. In feather, extraction left largely intact the macroscopic barb structures but caused collapse of the rachis. In both rachis and barbs, considerable material resembling cell envelopes remained. In extracted hagfish teeth the cellular organization was clearly visible microscopically, including cell borders and remnant nuclei. Unlike the cornified envelopes of mature epidermal keratinocytes, which appear as doublets, reflecting their formation immediately beneath each plasma membrane of apposing cells, the borders of cells of hair cortex and hagfish teeth appeared single and continuous from one cell to the next. Thus the observed cross-linked features comprised four types: (i) condensation immediately beneath the plasma membrane (feather, hair medulla and cuticle) similar to cornified envelopes of epidermal keratinocytes; (ii) deposition between cells (hair cortex, horny teeth); (iii) cytoplasmic deposits (hair cuticle and medulla); and (iv) nuclear condensation (hair medulla, horny teeth). The results emphasize the importance of transglutaminases and their substrate proteins for the function of epidermal appendages and may provide a useful diagnostic test for perturbation of their normal structures.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1985-1992 |
| Number of pages | 8 |
| Journal | Journal of Cell Science |
| Volume | 107 |
| Issue number | 7 |
| State | Published - Jul 1994 |
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Keywords
- Feather
- Hagfish teeth
- Hair
- Isopeptide
- Transglutaminase
ASJC Scopus subject areas
- Cell Biology
Cite this
Ultrastructural visualization of cross-linked protein features in epidermal appendages. / Rice, Robert H.; Wong, Viviana J.; Pinkerton, Kent E.
In: Journal of Cell Science, Vol. 107, No. 7, 07.1994, p. 1985-1992.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ultrastructural visualization of cross-linked protein features in epidermal appendages
AU - Rice, Robert H.
AU - Wong, Viviana J.
AU - Pinkerton, Kent E
PY - 1994/7
Y1 - 1994/7
N2 - Upon vigorous extraction with ionic detergent under reducing conditions, the macroscopic structures of mammalian hair, bird feather and horny teeth of the hagfish became swollen and flexible but were substantially preserved. In each case, removal in this way of solubilizable constituents, such as disulfide-bonded keratins and associated matrix proteins, left a residue of ε-(γ-glutamyl)lysine cross-linked protein. Residual features in hair included cell envelopes in the cortex, cell envelopes and intracellular deposits in the medulla, and nearly the entire cuticle cells. In feather, extraction left largely intact the macroscopic barb structures but caused collapse of the rachis. In both rachis and barbs, considerable material resembling cell envelopes remained. In extracted hagfish teeth the cellular organization was clearly visible microscopically, including cell borders and remnant nuclei. Unlike the cornified envelopes of mature epidermal keratinocytes, which appear as doublets, reflecting their formation immediately beneath each plasma membrane of apposing cells, the borders of cells of hair cortex and hagfish teeth appeared single and continuous from one cell to the next. Thus the observed cross-linked features comprised four types: (i) condensation immediately beneath the plasma membrane (feather, hair medulla and cuticle) similar to cornified envelopes of epidermal keratinocytes; (ii) deposition between cells (hair cortex, horny teeth); (iii) cytoplasmic deposits (hair cuticle and medulla); and (iv) nuclear condensation (hair medulla, horny teeth). The results emphasize the importance of transglutaminases and their substrate proteins for the function of epidermal appendages and may provide a useful diagnostic test for perturbation of their normal structures.
AB - Upon vigorous extraction with ionic detergent under reducing conditions, the macroscopic structures of mammalian hair, bird feather and horny teeth of the hagfish became swollen and flexible but were substantially preserved. In each case, removal in this way of solubilizable constituents, such as disulfide-bonded keratins and associated matrix proteins, left a residue of ε-(γ-glutamyl)lysine cross-linked protein. Residual features in hair included cell envelopes in the cortex, cell envelopes and intracellular deposits in the medulla, and nearly the entire cuticle cells. In feather, extraction left largely intact the macroscopic barb structures but caused collapse of the rachis. In both rachis and barbs, considerable material resembling cell envelopes remained. In extracted hagfish teeth the cellular organization was clearly visible microscopically, including cell borders and remnant nuclei. Unlike the cornified envelopes of mature epidermal keratinocytes, which appear as doublets, reflecting their formation immediately beneath each plasma membrane of apposing cells, the borders of cells of hair cortex and hagfish teeth appeared single and continuous from one cell to the next. Thus the observed cross-linked features comprised four types: (i) condensation immediately beneath the plasma membrane (feather, hair medulla and cuticle) similar to cornified envelopes of epidermal keratinocytes; (ii) deposition between cells (hair cortex, horny teeth); (iii) cytoplasmic deposits (hair cuticle and medulla); and (iv) nuclear condensation (hair medulla, horny teeth). The results emphasize the importance of transglutaminases and their substrate proteins for the function of epidermal appendages and may provide a useful diagnostic test for perturbation of their normal structures.
KW - Feather
KW - Hagfish teeth
KW - Hair
KW - Isopeptide
KW - Transglutaminase
UR - http://www.scopus.com/inward/record.url?scp=0028236958&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028236958&partnerID=8YFLogxK
M3 - Article
C2 - 7983163
AN - SCOPUS:0028236958
VL - 107
SP - 1985
EP - 1992
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 7
ER -