Abstract
Among the adaptations of aquatic species during evolution of terrestrial tetrapods was the development of an epidermis preventing desiccation. In present day mammals, keratinocytes of the epidermis, using a membrane-bound transglutaminase (Tgm1), accomplish this function by synthesizing a scaffold of cross-linked protein to which a lipid envelope is attached. This study characterizes the abilities of two homologous transglutaminase isozymes in the teleost fish tilapia to form cross-linked protein structures and their expression in certain tissues. Results indicate they are capable of membrane localization and of generating cellular structures resistant to detergent solubilization. They are both expressed in epithelial cells of the lip, buccal cavity and tips of gill filaments. Adaptation of transglutaminase use in evolution of terrestrial keratinocytes evidently involved refinements in tissue expression, access to suitable substrate proteins and activation of cross-linking during terminal differentiation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | e0177016 |
| Journal | PLoS One |
| Volume | 12 |
| Issue number | 5 |
| DOIs | |
| State | Published - 2017 |
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ASJC Scopus subject areas
- Medicine(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
Cite this
Tgm1-like transglutaminases in tilapia (Oreochromis mossambicus). / Rodriguez Cruz, Sandra I.; Phillips, Marjorie A.; Kültz, Dietmar; Rice, Robert H.
In: PLoS One, Vol. 12, No. 5, 2017, p. e0177016.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Tgm1-like transglutaminases in tilapia (Oreochromis mossambicus)
AU - Rodriguez Cruz, Sandra I.
AU - Phillips, Marjorie A.
AU - Kültz, Dietmar
AU - Rice, Robert H.
PY - 2017
Y1 - 2017
N2 - Among the adaptations of aquatic species during evolution of terrestrial tetrapods was the development of an epidermis preventing desiccation. In present day mammals, keratinocytes of the epidermis, using a membrane-bound transglutaminase (Tgm1), accomplish this function by synthesizing a scaffold of cross-linked protein to which a lipid envelope is attached. This study characterizes the abilities of two homologous transglutaminase isozymes in the teleost fish tilapia to form cross-linked protein structures and their expression in certain tissues. Results indicate they are capable of membrane localization and of generating cellular structures resistant to detergent solubilization. They are both expressed in epithelial cells of the lip, buccal cavity and tips of gill filaments. Adaptation of transglutaminase use in evolution of terrestrial keratinocytes evidently involved refinements in tissue expression, access to suitable substrate proteins and activation of cross-linking during terminal differentiation.
AB - Among the adaptations of aquatic species during evolution of terrestrial tetrapods was the development of an epidermis preventing desiccation. In present day mammals, keratinocytes of the epidermis, using a membrane-bound transglutaminase (Tgm1), accomplish this function by synthesizing a scaffold of cross-linked protein to which a lipid envelope is attached. This study characterizes the abilities of two homologous transglutaminase isozymes in the teleost fish tilapia to form cross-linked protein structures and their expression in certain tissues. Results indicate they are capable of membrane localization and of generating cellular structures resistant to detergent solubilization. They are both expressed in epithelial cells of the lip, buccal cavity and tips of gill filaments. Adaptation of transglutaminase use in evolution of terrestrial keratinocytes evidently involved refinements in tissue expression, access to suitable substrate proteins and activation of cross-linking during terminal differentiation.
UR - http://www.scopus.com/inward/record.url?scp=85029668331&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85029668331&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0177016
DO - 10.1371/journal.pone.0177016
M3 - Article
C2 - 28472103
AN - SCOPUS:85029668331
VL - 12
SP - e0177016
JO - PLoS One
JF - PLoS One
SN - 1932-6203
IS - 5
ER -