Recombinant murine and human IL 1α bind to human endothelial cells with an equal affinity, but have an unequal ability to induce endothelial cell adherence of lymphocytes

T. R. Thieme, Steven Hefeneider, C. R. Wagner, D. R. Burger

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Consistent with the reports of others, we have demonstrated that human peripheral blood lymphocytes adhere to cultured human umbilical vein-derived endothelial cells (EC) in vitro. In our studies adherence was increased twofold to threefold by a 6-hr preincubation of the EC with IL 1. Recombinant human IL 1α induced a maximal adherence response at less than 1 U per 2 x 104 EC. In contrast, recombinant murine IL 1α was found to be 250- to 1250-fold less active in the adherence assay, based on units of IL 1 activity defined by the murine thymocyte proliferation assay. Moreover, when EC were preincubated with excess murine IL 1, no inhibition of the adherence-inducing effect of human IL 1 was noted. To characterize further this dichotomy of biological potency of murine and human IL 1 on the adherence assay, IL 1 binding studies were initiated. Recombinant human and murine IL 1α were equally effective in inhibiting the binding of 125I-labeled human and murine IL 1, based on both micrograms of protein and units of IL 1 activity. The results of this study demonstrate that although human and murine IL 1 bind with equal affinity to receptors on human EC, human IL 1 is significantly more potent at inducing the increased EC adhesiveness for lymphocytes. The implications of these results for endothelial cell IL 1 receptor function are discussed.

Original languageEnglish (US)
Pages (from-to)1173-1178
Number of pages6
JournalJournal of Immunology
Volume139
Issue number4
StatePublished - 1987
Externally publishedYes

Fingerprint

Interleukin-1
Endothelial Cells
Lymphocytes
Adhesiveness
Interleukin-1 Receptors
Human Umbilical Vein Endothelial Cells
Thymocytes

ASJC Scopus subject areas

  • Immunology

Cite this

@article{95554f0d2e5c411fbd200e3a4dc75305,
title = "Recombinant murine and human IL 1α bind to human endothelial cells with an equal affinity, but have an unequal ability to induce endothelial cell adherence of lymphocytes",
abstract = "Consistent with the reports of others, we have demonstrated that human peripheral blood lymphocytes adhere to cultured human umbilical vein-derived endothelial cells (EC) in vitro. In our studies adherence was increased twofold to threefold by a 6-hr preincubation of the EC with IL 1. Recombinant human IL 1α induced a maximal adherence response at less than 1 U per 2 x 104 EC. In contrast, recombinant murine IL 1α was found to be 250- to 1250-fold less active in the adherence assay, based on units of IL 1 activity defined by the murine thymocyte proliferation assay. Moreover, when EC were preincubated with excess murine IL 1, no inhibition of the adherence-inducing effect of human IL 1 was noted. To characterize further this dichotomy of biological potency of murine and human IL 1 on the adherence assay, IL 1 binding studies were initiated. Recombinant human and murine IL 1α were equally effective in inhibiting the binding of 125I-labeled human and murine IL 1, based on both micrograms of protein and units of IL 1 activity. The results of this study demonstrate that although human and murine IL 1 bind with equal affinity to receptors on human EC, human IL 1 is significantly more potent at inducing the increased EC adhesiveness for lymphocytes. The implications of these results for endothelial cell IL 1 receptor function are discussed.",
author = "Thieme, {T. R.} and Steven Hefeneider and Wagner, {C. R.} and Burger, {D. R.}",
year = "1987",
language = "English (US)",
volume = "139",
pages = "1173--1178",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "4",

}

TY - JOUR

T1 - Recombinant murine and human IL 1α bind to human endothelial cells with an equal affinity, but have an unequal ability to induce endothelial cell adherence of lymphocytes

AU - Thieme, T. R.

AU - Hefeneider, Steven

AU - Wagner, C. R.

AU - Burger, D. R.

PY - 1987

Y1 - 1987

N2 - Consistent with the reports of others, we have demonstrated that human peripheral blood lymphocytes adhere to cultured human umbilical vein-derived endothelial cells (EC) in vitro. In our studies adherence was increased twofold to threefold by a 6-hr preincubation of the EC with IL 1. Recombinant human IL 1α induced a maximal adherence response at less than 1 U per 2 x 104 EC. In contrast, recombinant murine IL 1α was found to be 250- to 1250-fold less active in the adherence assay, based on units of IL 1 activity defined by the murine thymocyte proliferation assay. Moreover, when EC were preincubated with excess murine IL 1, no inhibition of the adherence-inducing effect of human IL 1 was noted. To characterize further this dichotomy of biological potency of murine and human IL 1 on the adherence assay, IL 1 binding studies were initiated. Recombinant human and murine IL 1α were equally effective in inhibiting the binding of 125I-labeled human and murine IL 1, based on both micrograms of protein and units of IL 1 activity. The results of this study demonstrate that although human and murine IL 1 bind with equal affinity to receptors on human EC, human IL 1 is significantly more potent at inducing the increased EC adhesiveness for lymphocytes. The implications of these results for endothelial cell IL 1 receptor function are discussed.

AB - Consistent with the reports of others, we have demonstrated that human peripheral blood lymphocytes adhere to cultured human umbilical vein-derived endothelial cells (EC) in vitro. In our studies adherence was increased twofold to threefold by a 6-hr preincubation of the EC with IL 1. Recombinant human IL 1α induced a maximal adherence response at less than 1 U per 2 x 104 EC. In contrast, recombinant murine IL 1α was found to be 250- to 1250-fold less active in the adherence assay, based on units of IL 1 activity defined by the murine thymocyte proliferation assay. Moreover, when EC were preincubated with excess murine IL 1, no inhibition of the adherence-inducing effect of human IL 1 was noted. To characterize further this dichotomy of biological potency of murine and human IL 1 on the adherence assay, IL 1 binding studies were initiated. Recombinant human and murine IL 1α were equally effective in inhibiting the binding of 125I-labeled human and murine IL 1, based on both micrograms of protein and units of IL 1 activity. The results of this study demonstrate that although human and murine IL 1 bind with equal affinity to receptors on human EC, human IL 1 is significantly more potent at inducing the increased EC adhesiveness for lymphocytes. The implications of these results for endothelial cell IL 1 receptor function are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0023189899&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023189899&partnerID=8YFLogxK

M3 - Article

C2 - 2956325

AN - SCOPUS:0023189899

VL - 139

SP - 1173

EP - 1178

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 4

ER -