NDLI: Evidence for participation of transglutaminase in receptor-mediated endocytosis.

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Evidence for participation of transglutaminase in receptor-mediated endocytosis.

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Evidence for participation of transglutaminase in receptor-mediated endocytosis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Willingham, M. Pastan, I. Levitzki, A.
Abstract	We report evidence that the enzyme transglutaminase (glutaminyl-peptide gamma-glutamyltransferase; R-glutaminyl-peptide:amine gamma-glutamyltransferase, EC2.3.2.13) participates in receptor-mediated endocytosis. Clustering and internalization of rhodamine-labeled alpha 2-macroglobulin (R alpha 2 M) in normal rat kidney (NRK) cells is inhibited by a wide spectrum of compounds that inhibit transglutaminases, including that from NRK cells. The pattern of clustering inhibition resembles the pattern of transglutaminase inhibition as follows: (i) The most potent transglutaminase inhibitors are dansylcadaverine and the transglutaminase-directed affinity label N-benzyloxy-carbonyl-5-diazo-4-oxonorvaline p-nitrophenyl ester; these were also the most potent inhibitors of clustering and internalization of R alpha 2M. (ii) The inhibition of clustering of R alpha 2M occurs in the same concentration range as that required for transglutaminase inhibition. (iii) Linear primary amines are more effective blockers than the iso-chain primary amines. (iv) The transglutaminase affinity label N-benzyloxycarbonyl-5-diazo-4-oxonorvaline p-nitrophenyl ester irreversibly inhibits a significant fraction of the NRK transglutaminase and the clustering and internalization of R alpha 2M. A closely related compound, N-trifluoroacetyl-6-diazo-5-oxonorleucine ethyl ester, does not significantly inhibit transglutaminase or clustering and internalization. (v) Clustering and internalization is inhibited 10-fold more effectively by the heptapeptide Ac-Gly2-LLeu-LLys-Gly3 than by the heptapeptides Ac-Gly2-LLeu-DLys-Gly3 or AcGly3-DLys-DLeu-Gly2. This is the pattern of stereospecificity for the inhibition of purified transglutaminases.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	77
Language	English
Publisher	National Academy of Sciences
Publisher Date	1980-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endocytosis Receptors, Drug Metabolism Gamma-Glutamyltransferase Affinity Labels Animals Cell Line Cell Membrane Permeability Dimethyl Sulfoxide Pharmacology Kinetics Membrane Fluidity Drug Effects Rhodanine Alpha-Macroglobulins Antagonists & Inhibitors Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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