Specificity of insulin binding by plasma and nuclear membrane receptors in Tetrahymena: similarities and dissimilarities at the two levels.

Research output: Article

10 Citations (Scopus)

Abstract

The plasma membrane and nuclear envelope of Tetrahymena are equally able to bind insulin both specifically and otherwise. Primary interaction with exogenous insulin (imprinting) accounted for an increase in the specificity of binding which became even more pronounced in the distant offspring generations of the imprinted cells. Virgin Tetrahymena cells not imprinted with insulin showed a greater specificity of insulin binding at the nuclear than at the plasma membrane level. This difference became equalized under the influence of imprinting with exogenous insulin which increased the specificity of binding at the plasma membrane level.

Original languageEnglish
Pages (from-to)153-158
Number of pages6
JournalCytobios
Volume70
Issue number282-283
Publication statusPublished - 1992

Fingerprint

Tetrahymena
Nuclear Envelope
nuclear membrane
Cytoplasmic and Nuclear Receptors
imprinting
insulin
plasma membrane
Cell Membrane
Insulin
membrane
plasma
receptors
cells

ASJC Scopus subject areas

  • Aquatic Science
  • Cell Biology

Cite this

@article{6ce827847467479897ee808d01b3cbaa,
title = "Specificity of insulin binding by plasma and nuclear membrane receptors in Tetrahymena: similarities and dissimilarities at the two levels.",
abstract = "The plasma membrane and nuclear envelope of Tetrahymena are equally able to bind insulin both specifically and otherwise. Primary interaction with exogenous insulin (imprinting) accounted for an increase in the specificity of binding which became even more pronounced in the distant offspring generations of the imprinted cells. Virgin Tetrahymena cells not imprinted with insulin showed a greater specificity of insulin binding at the nuclear than at the plasma membrane level. This difference became equalized under the influence of imprinting with exogenous insulin which increased the specificity of binding at the plasma membrane level.",
author = "G. Csaba and H. Hegyesi",
year = "1992",
language = "English",
volume = "70",
pages = "153--158",
journal = "Cytobios",
issn = "0011-4529",
publisher = "University of Cambridge",
number = "282-283",

}

TY - JOUR

T1 - Specificity of insulin binding by plasma and nuclear membrane receptors in Tetrahymena

T2 - similarities and dissimilarities at the two levels.

AU - Csaba, G.

AU - Hegyesi, H.

PY - 1992

Y1 - 1992

N2 - The plasma membrane and nuclear envelope of Tetrahymena are equally able to bind insulin both specifically and otherwise. Primary interaction with exogenous insulin (imprinting) accounted for an increase in the specificity of binding which became even more pronounced in the distant offspring generations of the imprinted cells. Virgin Tetrahymena cells not imprinted with insulin showed a greater specificity of insulin binding at the nuclear than at the plasma membrane level. This difference became equalized under the influence of imprinting with exogenous insulin which increased the specificity of binding at the plasma membrane level.

AB - The plasma membrane and nuclear envelope of Tetrahymena are equally able to bind insulin both specifically and otherwise. Primary interaction with exogenous insulin (imprinting) accounted for an increase in the specificity of binding which became even more pronounced in the distant offspring generations of the imprinted cells. Virgin Tetrahymena cells not imprinted with insulin showed a greater specificity of insulin binding at the nuclear than at the plasma membrane level. This difference became equalized under the influence of imprinting with exogenous insulin which increased the specificity of binding at the plasma membrane level.

UR - http://www.scopus.com/inward/record.url?scp=0027022723&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027022723&partnerID=8YFLogxK

M3 - Article

C2 - 1486794

AN - SCOPUS:0027022723

VL - 70

SP - 153

EP - 158

JO - Cytobios

JF - Cytobios

SN - 0011-4529

IS - 282-283

ER -