Endogenous substrates for epidermal transglutaminase |
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| Affiliation: | 1. Laboratory for Separation Processes and Product Design, Faculty of Chemistry and Chemical Engineering, University of Maribor, Smetanova ulica 17, SI-2000 Maribor, Slovenia;2. Kozmetika Afrodita d.o.o., Kidričeva 54, SI-3250, Rogaška Slatina, Slovenia;3. Faculty of Medicine, University of Maribor, Smetanova 17, SI-2000, Maribor, Slovenia;1. Embrapa Centro Nacional de Pesquisa de Soja, Caixa Postal: 231, CEP. 86001-970, Londrina, PR, Brazil;2. UNESP Universidade Estadual Paulista, FCAV, Via de Acesso Prof. Paulo Donato Castellane, s/n, CEP. 14884-900, Jaboticabal, SP, Brazil;3. IAC Instituto Agronômico de Campinas, Av. Barão de Itapura, 1481, Cx. Postal: 28, CEP. 13012-970, Campinas, SP, Brazil;4. UEL Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445 Km 380, Caixa Postal 6001, CEP. 86051-980, Londrina, PR, Brazil;5. UNAERP Universidade de Ribeirão Preto, Avenida Costábile Romano, Caixa Postal: 2201, CEP. 14096-900, Ribeirão Preto, SP, Brazil;6. Biological Chemistry and Crop Protection Department, Rothamsted Research, Harpenden, Herts. AL5 2JQ, United Kingdom;7. UEM Universidade Estadual de Maringá, Avenida Colombo, 5790, Jardim Universitario, CEP. 87020-900, Maringá, PR, Brazil;8. Computational and Systems Biology Department, Rothamsted Research, Harpenden, Herts. AL5 2JQ, United Kingdom;1. Department of Clinical Pharmacy, School of Basic Medicine and Clinical Pharmacy, China Pharmaceutical University, Nanjing 211198, China;2. Department of Bioengineering & Therapeutic Science, University of California, San Francisco, CA 94143-0912, USA |
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| Abstract: | Potential in vivo substrates for epidermal transglutaminase have been isolated and partially characterized in human stratum corneum and new born rat epidermis. [14C]Putrescine and dansylcadaverine were incorporated into epidermal protens in vitro. Two high molecular weight proteins incorporated the labels in both the rat and human homogenates. One of the proteins was too large to enter a 4% sodium dodecyl sulfate-polyacrylamide spacer gel; the other was seen at the interface between the spacer gel and a 10% sodium dodecyl sulphate-polyacrylamide running gel. These proteins were present in a buffer extract, sodium dodecyl sulphate-dithiothreitol extract and NaOH extract. The labels were also incorporated into protein in the insoluble pellet remaining after the afore-mentioned extractions. The incorporation of putrescine and dansylcadaverine was time dependent, and was inhibited by known inhibitors of epidermal transglutaminase. The two high molecular weight proteins had similar amino acid composition, characterized by high glycine, glutamic acid, serine and aspartic acid. Their amino acid composition was similar to, although not identical with, the amino acid composition of α-keratin proteins.Epidermal homogenates incubated in the presence of transglutaminase showed progressive insolubilization of the protein. This cross-linking was inhibited by putrescine.[14C]Glycine, [14C]histidine and [14C]proline were incorporated into epidermal proteins in newborn rats in vivo. The glycine-labelled protein became progressively more insoluble when incubated in vitro in the presence of transglutaminase. In vitro incubation with transglutaminase had no effect on the histidine- and proline-labelled proteins. |
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