Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes

The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >...

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Veröffentlicht in:Biochemical and biophysical research communications 1996-04, Vol.221 (1), p.101-106
Hauptverfasser: Steinert, Peter M., Chung, Soo-Il, Kim, Soo-Youl
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creator Steinert, Peter M.
Chung, Soo-Il
Kim, Soo-Youl
description The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >95% is attached to membranes. In terminally differentiating keratinocytes, there is a ≥100-fold induction of mRNA and protein. In addition to some cytosolic protein, most of the newly expressed protein is attached to membranes, of which about half exists in the zymogen form. Other protein consists of a 67/33/10 kDa complex formed by proteolytic processing at specific sites, and is anchored by way of the 10 kDa fragment. This processed form is very highly active and thus accounts for almost all transglutaminase 1 activity in keratinocytes.
doi_str_mv 10.1006/bbrc.1996.0552
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subjects Base Sequence
Cell Membrane - metabolism
Cells, Cultured
Cytosol - metabolism
DNA Primers
Enzyme Precursors - metabolism
Epidermis - enzymology
Humans
Hydrolysis
Keratinocytes - enzymology
Molecular Sequence Data
Protein Processing, Post-Translational
Transglutaminases - metabolism
title Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes
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