Glycine methylester, an inhibitor of transglutaminase, decreased glucose-stimulated insulin release and delayed proinsulin conversion in rat pancreatic islets pulselabelle with L-[4-[3H]phenylalanine. Sarcosine methylester, which does not inhibit transglutaminase activity, failed to affect insulin release and proinsulin conversion. The incorporation of L-[4-3H]phenylalanine into islet peptides, the ratio of hormonal to total tritiated peptides and the insulin content of the islets failed to be affected by either of these methylesters. It is proposed that transglutaminase participates in the control of motile events involved in both the transfer of proinsulin from its site of synthesis to its site of conversion, and the translocation of insulin from its site of storage to its site of release.
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July 01 1985
Transglutaminase and cellular motile events: Retardation of proinsulin conversion by glycine methylester
C. Alarcon;
C. Alarcon
1Fundacion Jimenez Diaz, Universidad Autonoma de Madrid, Madrid, Spain
2Laboratory of Experimental Medicine, Brussels Free University, Brussels, Belgium
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I. Valverde;
I. Valverde
1Fundacion Jimenez Diaz, Universidad Autonoma de Madrid, Madrid, Spain
2Laboratory of Experimental Medicine, Brussels Free University, Brussels, Belgium
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W. J. Malaisse
W. J. Malaisse
1Fundacion Jimenez Diaz, Universidad Autonoma de Madrid, Madrid, Spain
2Laboratory of Experimental Medicine, Brussels Free University, Brussels, Belgium
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Publisher: Portland Press Ltd
Received:
May 20 1985
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1985 The Biochemical Society
1985
Biosci Rep (1985) 5 (7): 581–587.
Article history
Received:
May 20 1985
Citation
C. Alarcon, I. Valverde, W. J. Malaisse; Transglutaminase and cellular motile events: Retardation of proinsulin conversion by glycine methylester. Biosci Rep 1 July 1985; 5 (7): 581–587. doi: https://doi.org/10.1007/BF01117071
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