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PMID: 2890619 Published · ppublish English Journal Article

Cellular transglutaminase has affinity for extracellular matrix.

In vitro cellular & developmental biology : journal of the Tissue Culture Association ·Vol. 23 ·No. 11 ·1987-11-00 ·Pages 795-800

Upchurch HF, Conway E, Patterson MK, Birckbichler PJ, Maxwell MD

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.

MeSH Terms
Extracellular Matrix/metabolism Fibroblasts/enzymology,ultrastructure Fibronectins/analysis Fluorescent Antibody Technique Humans Transglutaminases/metabolism
Chemicals
Fibronectins Transglutaminases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Upchurch H F
Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73402.
Conway E
Patterson M K
Birckbichler P J
Maxwell M D
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Article Info
Journal
In vitro cellular & developmental biology : journal of the Tissue Culture Association
Abbr.
In Vitro Cell Dev Biol
ISSN
0883-8364
DOI
10.1007/BF02623682
Published
1987-11-00
Pages
795-800
Language
English
Region
United States
NLM ID
8506951
Subset
IM
External Links
PubMed source DOI: 10.1007/BF02623682
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