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J. Biol. Chem., Vol. 266, Issue 23, 15308-15317, 08, 1991
D Aeschlimann and M Paulsson
The laminin-nidogen complex, a major component of basement membranes,
incorporates [3H]putrescine and monodansylcadaverine in the presence of
guinea pig liver transglutaminase. Label was detected in nidogen in the
isolated, as well as in the complexed form, but not in laminin. The
incorporation proceeds in a time-dependent manner at a rate similar to that
achieved with N,N-dimethylcasein, a well characterized transglutaminase
substrate. Saturation of incorporation site(s), as well as comparison with
the incorporation level in reference proteins, indicated the presence of
one high affinity amine acceptor site in nidogen. Electron microscopy of
the reaction products showed that the laminin-nidogen complexes become
stabilized in a head-to-head arrangement, characteristic of Ca(2+)-induced
self-aggregation. Indirect immunofluorescence and detection of
transglutaminase activity on unfixed cryosections revealed an extracellular
distribution of tissue transglutaminase. Intensive staining was observed in
collagen- rich connective tissue. Codistribution with nidogen was not a
ubiquitous feature, but was observed in many locations.
Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization
M. E. Muller-Institute for Biomechanics, University of Bern, Switzerland.
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