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Transglutaminase Cross‐Linking of the τ Protein by Michael L. Miller; Gail V. W. Johnson is a Neuroscience article available to read on EtoBox.

What is Transglutaminase Cross‐Linking of the τ Protein about?

Abstract: Tissue transglutaminase (EC 2.3.2.13) is a calcium‐activated enzyme that cross‐links specific substrate proteins into insoluble, protease‐resistant, high molecular weight complexes. Because the neurofibrillary tangles in Alzheimer disease have similar biochemical characteristics, and because the microtubule‐associated protein τ is the predominant component of these structures, the substrate properties of τ with respect to transglutaminase were investigated. Bovine τ and recombinant human τ isoforms rapidly form high molecular weight, cross‐linked polymers on incubation with transglutaminase. Polyamine incorporation assays indicate that bovine τ is an excellent substrate of transglutaminase, with a __K__~m~ of 10.4 ± 2.2 μ__M__ and a __V__~max~ of 40.9 ± 4.5 nmol/mg of enzyme/min. Individual recombinant human τ isoforms are not equivalent with respect to transglutaminase, as the smallest isoform T3 (352 amino acids) is not as good a substrate as the larger isoforms T4 (383 amino acids) and T4L (441 amino acids). To determine which segments of the τ protein are susceptible to modification by transglutaminase, τ was labeled with [^3^H]putrescine by transglutaminase and prote

Who reads Transglutaminase Cross‐Linking of the τ Protein?

It is typically read by researchers, students, and practitioners in Neuroscience.

Author
Michael L. Miller; Gail V. W. Johnson
Publisher
John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)
Published
1995
Language
EN
Field
Neuroscience (Life Sciences)

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