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In Vitro Cell Dev Biol. 1987 Nov;23(11):795-800.

Cellular transglutaminase has affinity for extracellular matrix.

Author information

1
Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73402.

Abstract

Cellular transglutaminase (TGase) was demonstrated as an intracellular enzyme by immunofluorescence in WI-38 cells. Following cell membrane perturbation by Triton X-100 treatment, TGase was bound to the extracellular matrix and was found to coexist with fibronectin as visualized by immunofluorescence microscopy. The binding of TGase to the cell matrix was blocked by anti-fibronectin antibody. Exogenous sources of soluble TGase were transferred to the extracellular matrix of an untreated or methanol fixed cell. The experimental data indicated that "particulate bound" TGase is a consequence of soluble TGase binding to the extracellular matrix following cell rupture.

PMID:
2890619
[Indexed for MEDLINE]

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