Regulation of fibronectin and laminin receptor expression, fibronectin and laminin secretion in human colon cancer cells by transforming growth factor‐β1

Shuang Huang, Subhas Chakrabarty

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Transforming growth factor (TGF)‐β1, modulates the expression of extracellular matrix (ECM) glycoproteins, fibronectin and laminin and the adhesion of Moser colon cancer cells to these glycoproteins. Since adhesion can be altered through expression of cell‐surface receptors, binding affinities of adhesion molecules for receptors, or both, we investigated the effect of TGF‐β1, on the binding properties of fibronectin and laminin to their cell‐surface receptors by saturation binding and Scatchard analyses using radiolabeled fibronectin and laminin. Fibronectin bound to its cell‐surface receptor with high affinity (Kd = 1.25 × 10−9 M), Moser cells had approximately 7.1 × 104 fibronectin‐binding sites per cell. TGF‐β1 treatment rapidly up‐modulated the number of cell‐surface fibronectin‐binding sites by 1.9‐fold. The binding affinity of fibronectin for the receptor, however, was not altered. Laminin was found to bind to a higher‐affinity and a lower‐affinity receptor. Moser cells expressed approximately 1.1 × 103 higher‐affinity laminin‐binding sites and approximately 3.1 × 10 lower‐affinity‐binding sites per cell. TGF‐β1 rapidly increased the expression of the higher‐affinity sites 3‐fold and the lower‐affinity sites 5‐fold. The binding affinity of both the higher‐affinity and lower‐affinity laminin receptors increased 3‐fold after 2 and 6 hr of TGF‐β1 treatment respectively. Concurrent with receptor modulation, TGF‐β1 induced the secretion of fibronectin and laminin from Moser cells. Northern hybridization analyses showed a concurrent stimulation of the expression of the mRNAs for ligands (fibronectin and laminin) and the mRNAs for the integrin species of the fibronectin and laminin receptors (α5 and α6 subunits). Thus the production of fibronectin and laminin and the expression of their receptors were tightly co‐regulated by TGF‐β1.

Original languageEnglish (US)
Pages (from-to)742-746
Number of pages5
JournalInternational Journal of Cancer
Volume57
Issue number5
DOIs
StatePublished - Jan 1 1994

Fingerprint

Integrin alpha5beta1
Laminin
Fibronectins
Colonic Neoplasms
Growth
Glycoproteins
Fibronectin Receptors
Laminin Receptors
Messenger RNA
Transforming Growth Factors
Integrins
Extracellular Matrix
Ligands

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Regulation of fibronectin and laminin receptor expression, fibronectin and laminin secretion in human colon cancer cells by transforming growth factor‐β1. / Huang, Shuang; Chakrabarty, Subhas.

In: International Journal of Cancer, Vol. 57, No. 5, 01.01.1994, p. 742-746.

Research output: Contribution to journalArticle

@article{b3344cfa1c2c447699d9962fccd61a06,
title = "Regulation of fibronectin and laminin receptor expression, fibronectin and laminin secretion in human colon cancer cells by transforming growth factor‐β1",
abstract = "Transforming growth factor (TGF)‐β1, modulates the expression of extracellular matrix (ECM) glycoproteins, fibronectin and laminin and the adhesion of Moser colon cancer cells to these glycoproteins. Since adhesion can be altered through expression of cell‐surface receptors, binding affinities of adhesion molecules for receptors, or both, we investigated the effect of TGF‐β1, on the binding properties of fibronectin and laminin to their cell‐surface receptors by saturation binding and Scatchard analyses using radiolabeled fibronectin and laminin. Fibronectin bound to its cell‐surface receptor with high affinity (Kd = 1.25 × 10−9 M), Moser cells had approximately 7.1 × 104 fibronectin‐binding sites per cell. TGF‐β1 treatment rapidly up‐modulated the number of cell‐surface fibronectin‐binding sites by 1.9‐fold. The binding affinity of fibronectin for the receptor, however, was not altered. Laminin was found to bind to a higher‐affinity and a lower‐affinity receptor. Moser cells expressed approximately 1.1 × 103 higher‐affinity laminin‐binding sites and approximately 3.1 × 10 lower‐affinity‐binding sites per cell. TGF‐β1 rapidly increased the expression of the higher‐affinity sites 3‐fold and the lower‐affinity sites 5‐fold. The binding affinity of both the higher‐affinity and lower‐affinity laminin receptors increased 3‐fold after 2 and 6 hr of TGF‐β1 treatment respectively. Concurrent with receptor modulation, TGF‐β1 induced the secretion of fibronectin and laminin from Moser cells. Northern hybridization analyses showed a concurrent stimulation of the expression of the mRNAs for ligands (fibronectin and laminin) and the mRNAs for the integrin species of the fibronectin and laminin receptors (α5 and α6 subunits). Thus the production of fibronectin and laminin and the expression of their receptors were tightly co‐regulated by TGF‐β1.",
author = "Shuang Huang and Subhas Chakrabarty",
year = "1994",
month = "1",
day = "1",
doi = "10.1002/ijc.2910570522",
language = "English (US)",
volume = "57",
pages = "742--746",
journal = "International Journal of Cancer",
issn = "0020-7136",
publisher = "Wiley-Liss Inc.",
number = "5",

}

TY - JOUR

T1 - Regulation of fibronectin and laminin receptor expression, fibronectin and laminin secretion in human colon cancer cells by transforming growth factor‐β1

AU - Huang, Shuang

AU - Chakrabarty, Subhas

PY - 1994/1/1

Y1 - 1994/1/1

N2 - Transforming growth factor (TGF)‐β1, modulates the expression of extracellular matrix (ECM) glycoproteins, fibronectin and laminin and the adhesion of Moser colon cancer cells to these glycoproteins. Since adhesion can be altered through expression of cell‐surface receptors, binding affinities of adhesion molecules for receptors, or both, we investigated the effect of TGF‐β1, on the binding properties of fibronectin and laminin to their cell‐surface receptors by saturation binding and Scatchard analyses using radiolabeled fibronectin and laminin. Fibronectin bound to its cell‐surface receptor with high affinity (Kd = 1.25 × 10−9 M), Moser cells had approximately 7.1 × 104 fibronectin‐binding sites per cell. TGF‐β1 treatment rapidly up‐modulated the number of cell‐surface fibronectin‐binding sites by 1.9‐fold. The binding affinity of fibronectin for the receptor, however, was not altered. Laminin was found to bind to a higher‐affinity and a lower‐affinity receptor. Moser cells expressed approximately 1.1 × 103 higher‐affinity laminin‐binding sites and approximately 3.1 × 10 lower‐affinity‐binding sites per cell. TGF‐β1 rapidly increased the expression of the higher‐affinity sites 3‐fold and the lower‐affinity sites 5‐fold. The binding affinity of both the higher‐affinity and lower‐affinity laminin receptors increased 3‐fold after 2 and 6 hr of TGF‐β1 treatment respectively. Concurrent with receptor modulation, TGF‐β1 induced the secretion of fibronectin and laminin from Moser cells. Northern hybridization analyses showed a concurrent stimulation of the expression of the mRNAs for ligands (fibronectin and laminin) and the mRNAs for the integrin species of the fibronectin and laminin receptors (α5 and α6 subunits). Thus the production of fibronectin and laminin and the expression of their receptors were tightly co‐regulated by TGF‐β1.

AB - Transforming growth factor (TGF)‐β1, modulates the expression of extracellular matrix (ECM) glycoproteins, fibronectin and laminin and the adhesion of Moser colon cancer cells to these glycoproteins. Since adhesion can be altered through expression of cell‐surface receptors, binding affinities of adhesion molecules for receptors, or both, we investigated the effect of TGF‐β1, on the binding properties of fibronectin and laminin to their cell‐surface receptors by saturation binding and Scatchard analyses using radiolabeled fibronectin and laminin. Fibronectin bound to its cell‐surface receptor with high affinity (Kd = 1.25 × 10−9 M), Moser cells had approximately 7.1 × 104 fibronectin‐binding sites per cell. TGF‐β1 treatment rapidly up‐modulated the number of cell‐surface fibronectin‐binding sites by 1.9‐fold. The binding affinity of fibronectin for the receptor, however, was not altered. Laminin was found to bind to a higher‐affinity and a lower‐affinity receptor. Moser cells expressed approximately 1.1 × 103 higher‐affinity laminin‐binding sites and approximately 3.1 × 10 lower‐affinity‐binding sites per cell. TGF‐β1 rapidly increased the expression of the higher‐affinity sites 3‐fold and the lower‐affinity sites 5‐fold. The binding affinity of both the higher‐affinity and lower‐affinity laminin receptors increased 3‐fold after 2 and 6 hr of TGF‐β1 treatment respectively. Concurrent with receptor modulation, TGF‐β1 induced the secretion of fibronectin and laminin from Moser cells. Northern hybridization analyses showed a concurrent stimulation of the expression of the mRNAs for ligands (fibronectin and laminin) and the mRNAs for the integrin species of the fibronectin and laminin receptors (α5 and α6 subunits). Thus the production of fibronectin and laminin and the expression of their receptors were tightly co‐regulated by TGF‐β1.

UR - http://www.scopus.com/inward/record.url?scp=0028232024&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028232024&partnerID=8YFLogxK

U2 - 10.1002/ijc.2910570522

DO - 10.1002/ijc.2910570522

M3 - Article

C2 - 8194884

AN - SCOPUS:0028232024

VL - 57

SP - 742

EP - 746

JO - International Journal of Cancer

JF - International Journal of Cancer

SN - 0020-7136

IS - 5

ER -