Cellular transglutaminase has affinity for extracellular matrix |
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Authors: | Herbert F Upchurch Eugene Conway M K Patterson Jr Paul J Birckbichler Merle D Maxwell |
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Institution: | (1) The Samuel Roberts Noble Foundation, Inc., 2510 Highway 199 East, P. O. Box 2180, 73402 Ardmore, Oklahoma |
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Abstract: | Summary 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.
Editor's statement This report suggest that “particulate bound” transglutaminase may be a consequence of affinity of soluble
enzyme for specific molecules in extracellular matrix and opens up a means to characterize transglutaminase binding sites
in the matrix. |
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Keywords: | transglutaminase fibronectin extracellular matrix immunofluorescence |
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