Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization.

Aeschlimann, Daniel ORCID: https://orcid.org/0000-0003-0930-7706 and Paulsson, Mats 1991. Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization. Journal of Biological Chemistry 266 (23) , pp. 15308-15317.

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Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Subjects:	Q Science > Q Science (General) R Medicine > RK Dentistry
Publisher:	American Society for Biochemistry and Molecular Biology
ISSN:	0021-9258
Last Modified:	19 Oct 2022 10:17
URI:	https://orca.cardiff.ac.uk/id/eprint/23877

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