Literature DB >> 3080804

Protein modification by amino acid addition is increased in crushed sciatic but not optic nerves.

S Shyne-Athwal, R V Riccio, G Chakraborty, N A Ingoglia.   

Abstract

Rat optic and sciatic nerves were crushed, and 10 minutes to 3 days later nerve segments between the crushed site and the cell body were removed and assayed for posttranslational protein modification by amino acid addition. Protein modification was comparable in intact optic and sciatic nerves, but in sciatic nerves increased to 1.6 times control levels 10 minutes after crushing and reached a maximum of ten times control levels by 2 hours. In optic nerves activity was decreased throughout the time course studied. The results indicate that, in a nerve which is capable of regeneration (sciatic), protein modification by the addition of amino acids increases immediately after injury, but a nerve incapable of regeneration (optic) is incapable of activating the modification reaction. These findings may be important in understanding the reasons for the lack of a regenerative response after injury to central mammalian nerves.

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Year:  1986        PMID: 3080804     DOI: 10.1126/science.3080804

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  12 in total

1.  What is the signal for the posttranslational arginylation of proteins?

Authors:  N A Ingoglia; M Ramanathan; N Zhang; B Tzeng; G Mathur; K Opuni; R Donnelly
Journal:  Neurochem Res       Date:  2000-01       Impact factor: 3.996

2.  Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway.

Authors:  L A Pasquini; M Besio Moreno; M Lopez Salon; E F Soto
Journal:  Neurochem Res       Date:  2002-11       Impact factor: 3.996

3.  Evidence that oxidized proteins are substrates for N-terminal arginylation.

Authors:  N Zhang; R Donnelly; N A Ingoglia
Journal:  Neurochem Res       Date:  1998-11       Impact factor: 3.996

Review 4.  Posttranslational arginylation of brain proteins.

Authors:  M E Hallak; G Bongiovanni
Journal:  Neurochem Res       Date:  1997-04       Impact factor: 3.996

5.  Post-translational arginylation of proteins in cultured cells.

Authors:  S Fissolo; G Bongiovanni; M B Decca; M E Hallak
Journal:  Neurochem Res       Date:  2000-01       Impact factor: 3.996

6.  Isolation of a peptide that inhibits the posttranslational arginylation of proteins in rat brain.

Authors:  M Yu; M Grabow; N A Ingoglia
Journal:  J Mol Neurosci       Date:  1993       Impact factor: 3.444

7.  N-terminal arginylation of sciatic nerve and brain proteins following injury.

Authors:  Y M Wang; N A Ingoglia
Journal:  Neurochem Res       Date:  1997-12       Impact factor: 3.996

Review 8.  The role of local protein synthesis and degradation in axon regeneration.

Authors:  Laura F Gumy; Chin Lik Tan; James W Fawcett
Journal:  Exp Neurol       Date:  2009-06-09       Impact factor: 5.330

9.  Re-examination of the post-translational arginylated protein of 125-kD initially identified as N-STOP.

Authors:  María Belén Decca; Mauricio R Galiano; Héctor S Barra; Marta E Hallak
Journal:  Neurochem Res       Date:  2004-02       Impact factor: 3.996

10.  N-terminal arginylation of proteins in explants of injured sciatic nerves and embryonic brains of rats.

Authors:  N S Xu; G Chakraborty; A Hassankhani; N A Ingoglia
Journal:  Neurochem Res       Date:  1993-11       Impact factor: 3.996

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