Effect of triethyllead on post-translational processing of myelin proteins

G. Konat, Halina Offner

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The effect of triethyllead (PbEt3) on entry of newly synthesized proteins into myelin was studied in an in vitro system of brain stem slices prepared from actively myelinating young rats. The slices were incubated 30 min with [3H]leucine then the labeling of proteins was halted by a chase with cold amino acid and the slices were incubated an additional 30 min with different concentrations of PbEt3. Proteins continued to appear in myelin after the chase and this process was inhibited by PbEt3; however, distinct differences among individual proteins were observed. Inhibition curves for proteolipid, intermediate, and Wolfgram proteins were of a decrementally increasing type and displayed highest inhibition values in the case of proteolipid proteins. On the other hand, deposition of basic proteins was unaffected by the toxin to the concentration of about 5 μm, resulting in a sigmoidal curve of inhibition. The present results indicate specificity of PbEt3 toward post-translational metabolism of integral myelin proteins.

Original languageEnglish (US)
Pages (from-to)89-94
Number of pages6
JournalExperimental Neurology
Volume75
Issue number1
DOIs
StatePublished - 1982
Externally publishedYes

Fingerprint

Myelin Proteins
Proteolipids
Proteins
Myelin Sheath
Individuality
Leucine
Brain Stem
triethyllead
Amino Acids
Inhibition (Psychology)

ASJC Scopus subject areas

  • Neuroscience(all)
  • Neurology

Cite this

Effect of triethyllead on post-translational processing of myelin proteins. / Konat, G.; Offner, Halina.

In: Experimental Neurology, Vol. 75, No. 1, 1982, p. 89-94.

Research output: Contribution to journalArticle

@article{18a9fcdc765d4e1497ab71ae1ace7c7f,
title = "Effect of triethyllead on post-translational processing of myelin proteins",
abstract = "The effect of triethyllead (PbEt3) on entry of newly synthesized proteins into myelin was studied in an in vitro system of brain stem slices prepared from actively myelinating young rats. The slices were incubated 30 min with [3H]leucine then the labeling of proteins was halted by a chase with cold amino acid and the slices were incubated an additional 30 min with different concentrations of PbEt3. Proteins continued to appear in myelin after the chase and this process was inhibited by PbEt3; however, distinct differences among individual proteins were observed. Inhibition curves for proteolipid, intermediate, and Wolfgram proteins were of a decrementally increasing type and displayed highest inhibition values in the case of proteolipid proteins. On the other hand, deposition of basic proteins was unaffected by the toxin to the concentration of about 5 μm, resulting in a sigmoidal curve of inhibition. The present results indicate specificity of PbEt3 toward post-translational metabolism of integral myelin proteins.",
author = "G. Konat and Halina Offner",
year = "1982",
doi = "10.1016/0014-4886(82)90008-5",
language = "English (US)",
volume = "75",
pages = "89--94",
journal = "Experimental Neurology",
issn = "0014-4886",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Effect of triethyllead on post-translational processing of myelin proteins

AU - Konat, G.

AU - Offner, Halina

PY - 1982

Y1 - 1982

N2 - The effect of triethyllead (PbEt3) on entry of newly synthesized proteins into myelin was studied in an in vitro system of brain stem slices prepared from actively myelinating young rats. The slices were incubated 30 min with [3H]leucine then the labeling of proteins was halted by a chase with cold amino acid and the slices were incubated an additional 30 min with different concentrations of PbEt3. Proteins continued to appear in myelin after the chase and this process was inhibited by PbEt3; however, distinct differences among individual proteins were observed. Inhibition curves for proteolipid, intermediate, and Wolfgram proteins were of a decrementally increasing type and displayed highest inhibition values in the case of proteolipid proteins. On the other hand, deposition of basic proteins was unaffected by the toxin to the concentration of about 5 μm, resulting in a sigmoidal curve of inhibition. The present results indicate specificity of PbEt3 toward post-translational metabolism of integral myelin proteins.

AB - The effect of triethyllead (PbEt3) on entry of newly synthesized proteins into myelin was studied in an in vitro system of brain stem slices prepared from actively myelinating young rats. The slices were incubated 30 min with [3H]leucine then the labeling of proteins was halted by a chase with cold amino acid and the slices were incubated an additional 30 min with different concentrations of PbEt3. Proteins continued to appear in myelin after the chase and this process was inhibited by PbEt3; however, distinct differences among individual proteins were observed. Inhibition curves for proteolipid, intermediate, and Wolfgram proteins were of a decrementally increasing type and displayed highest inhibition values in the case of proteolipid proteins. On the other hand, deposition of basic proteins was unaffected by the toxin to the concentration of about 5 μm, resulting in a sigmoidal curve of inhibition. The present results indicate specificity of PbEt3 toward post-translational metabolism of integral myelin proteins.

UR - http://www.scopus.com/inward/record.url?scp=0020042604&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020042604&partnerID=8YFLogxK

U2 - 10.1016/0014-4886(82)90008-5

DO - 10.1016/0014-4886(82)90008-5

M3 - Article

C2 - 7060684

AN - SCOPUS:0020042604

VL - 75

SP - 89

EP - 94

JO - Experimental Neurology

JF - Experimental Neurology

SN - 0014-4886

IS - 1

ER -