Enzymatic cross-linking of involucrin and other proteins by keratinocyte particulates in vitro.

Abstract:

:A transglutaminase-catalyzed cross-linking process characteristic of keratinocytes leads to the formation of the insoluble corneocyte envelope. The essentials of this process take place in vitro in a reconstituted system derived from subcellular fractions. A particulate fraction containing membrane-bound envelope precursor proteins and the enzyme transglutaminase is combined with cytosolic proteins; when the enzyme is activated by Ca++, cytosolic proteins are removed from solution and cross-linked to particulate proteins. This interaction is cell-type-specific, since particulates derived from fibroblasts and also containing transglutaminase activity cannot substitute for those of keratinocytes. Involucrin, a cytosolic protein known to be a precursor of the envelope, is more efficiently cross-linked than other cytosolic proteins. The cross-linking of proteins of the particulate fraction (membrane proteins) is promoted by the presence of involucrin.

journal_name

Cell

journal_title

Cell

authors

Simon M,Green H

doi

10.1016/0092-8674(85)90216-8

subject

Has Abstract

pub_date

1985-03-01 00:00:00

pages

677-83

issue

3

eissn

0092-8674

issn

1097-4172

pii

0092-8674(85)90216-8

journal_volume

40

pub_type

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