5 Citations (Scopus)

Abstract

Laminin, a complex glycoprotein of the extracellular matrix, contains a number of biologically active sites. These sites are involved in cell growth, attachment, differentiation, and gene expression. Our previous studies have shown that chronic ethanol consumption by rats impairs hepatocyte attachment to various components of the extracellular matrix including laminin. In this study, three synthetic peptides (PA22‐2, YIGSR, and RGD) that correspond to three distinct functional sites on the laminin molecule were used to investigate the effect of ethanol consumption on their cognate receptors. Initially, varying concentrations of each peptide were incubated with isolated hepatocytes from ethanol‐fed and pair‐fed control rats. These hepatocytes were then assayed for the ability to attach to laminin. The results Indicated that all three peptides effectively inhibited laminin‐mediated cell adhesion: the degree of inhibition appeared similar between pair‐fed controls and ethanol‐fed animals. Of the three peptides, PA22‐2 showed the most dramatic inhibition of attachment. Therefore, we investigated the ability of hepatocytes to attach directly to PA22‐2 itself. Attachment of hepatocytes from ethanol‐fed animals to PA22‐2 was impaired by 30% after 4 days and 90% by 14 days. Conversely, no significant difference in attachment to the entire laminin molecule was observed in ethanol‐fed animals at these early time points. These results indicated that the ethanol‐induced impairment of hepatocyte attachment to laminin may be caused by the decreased interaction of hepatocytes with specific functional sites on the laminin molecule and that specific receptors on the hepatocyte may be affected differently. Because laminin has been shown to influence cell proliferation, differentiation, and gene expression, this defect could potentially result in structural and functional changes of the hepatocytes.

Original languageEnglish (US)
Pages (from-to)1215-1219
Number of pages5
JournalAlcoholism: Clinical and Experimental Research
Volume18
Issue number5
DOIs
StatePublished - Oct 1994

Fingerprint

Laminin
Rats
Hepatocytes
Ethanol
Peptides
Animals
Gene expression
tyrosyl-isoleucyl-glycyl-seryl-arginine
Molecules
Extracellular Matrix
Rat control
Gene Expression
Cell adhesion
Cell proliferation
Cell growth
Cell Adhesion
Cell Differentiation
Catalytic Domain
Glycoproteins
Cell Proliferation

Keywords

  • Ethanol
  • Hepatocyte Attachment
  • Laminin Peptide

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Toxicology
  • Psychiatry and Mental health

Cite this

@article{95b806876e0346b08a3c063b2f9464a0,
title = "Effects of Ethanol Feeding on the Interaction of Rat Hepatocytes with Laminin Peptides",
abstract = "Laminin, a complex glycoprotein of the extracellular matrix, contains a number of biologically active sites. These sites are involved in cell growth, attachment, differentiation, and gene expression. Our previous studies have shown that chronic ethanol consumption by rats impairs hepatocyte attachment to various components of the extracellular matrix including laminin. In this study, three synthetic peptides (PA22‐2, YIGSR, and RGD) that correspond to three distinct functional sites on the laminin molecule were used to investigate the effect of ethanol consumption on their cognate receptors. Initially, varying concentrations of each peptide were incubated with isolated hepatocytes from ethanol‐fed and pair‐fed control rats. These hepatocytes were then assayed for the ability to attach to laminin. The results Indicated that all three peptides effectively inhibited laminin‐mediated cell adhesion: the degree of inhibition appeared similar between pair‐fed controls and ethanol‐fed animals. Of the three peptides, PA22‐2 showed the most dramatic inhibition of attachment. Therefore, we investigated the ability of hepatocytes to attach directly to PA22‐2 itself. Attachment of hepatocytes from ethanol‐fed animals to PA22‐2 was impaired by 30{\%} after 4 days and 90{\%} by 14 days. Conversely, no significant difference in attachment to the entire laminin molecule was observed in ethanol‐fed animals at these early time points. These results indicated that the ethanol‐induced impairment of hepatocyte attachment to laminin may be caused by the decreased interaction of hepatocytes with specific functional sites on the laminin molecule and that specific receptors on the hepatocyte may be affected differently. Because laminin has been shown to influence cell proliferation, differentiation, and gene expression, this defect could potentially result in structural and functional changes of the hepatocytes.",
keywords = "Ethanol, Hepatocyte Attachment, Laminin Peptide",
author = "D. Xu and Sorrell, {Michael Floyd} and Clemens, {Dahn L} and Casey, {Carol A} and Tuma, {D. J.}",
year = "1994",
month = "10",
doi = "10.1111/j.1530-0277.1994.tb00107.x",
language = "English (US)",
volume = "18",
pages = "1215--1219",
journal = "Alcoholism: Clinical and Experimental Research",
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}

TY - JOUR

T1 - Effects of Ethanol Feeding on the Interaction of Rat Hepatocytes with Laminin Peptides

AU - Xu, D.

AU - Sorrell, Michael Floyd

AU - Clemens, Dahn L

AU - Casey, Carol A

AU - Tuma, D. J.

PY - 1994/10

Y1 - 1994/10

N2 - Laminin, a complex glycoprotein of the extracellular matrix, contains a number of biologically active sites. These sites are involved in cell growth, attachment, differentiation, and gene expression. Our previous studies have shown that chronic ethanol consumption by rats impairs hepatocyte attachment to various components of the extracellular matrix including laminin. In this study, three synthetic peptides (PA22‐2, YIGSR, and RGD) that correspond to three distinct functional sites on the laminin molecule were used to investigate the effect of ethanol consumption on their cognate receptors. Initially, varying concentrations of each peptide were incubated with isolated hepatocytes from ethanol‐fed and pair‐fed control rats. These hepatocytes were then assayed for the ability to attach to laminin. The results Indicated that all three peptides effectively inhibited laminin‐mediated cell adhesion: the degree of inhibition appeared similar between pair‐fed controls and ethanol‐fed animals. Of the three peptides, PA22‐2 showed the most dramatic inhibition of attachment. Therefore, we investigated the ability of hepatocytes to attach directly to PA22‐2 itself. Attachment of hepatocytes from ethanol‐fed animals to PA22‐2 was impaired by 30% after 4 days and 90% by 14 days. Conversely, no significant difference in attachment to the entire laminin molecule was observed in ethanol‐fed animals at these early time points. These results indicated that the ethanol‐induced impairment of hepatocyte attachment to laminin may be caused by the decreased interaction of hepatocytes with specific functional sites on the laminin molecule and that specific receptors on the hepatocyte may be affected differently. Because laminin has been shown to influence cell proliferation, differentiation, and gene expression, this defect could potentially result in structural and functional changes of the hepatocytes.

AB - Laminin, a complex glycoprotein of the extracellular matrix, contains a number of biologically active sites. These sites are involved in cell growth, attachment, differentiation, and gene expression. Our previous studies have shown that chronic ethanol consumption by rats impairs hepatocyte attachment to various components of the extracellular matrix including laminin. In this study, three synthetic peptides (PA22‐2, YIGSR, and RGD) that correspond to three distinct functional sites on the laminin molecule were used to investigate the effect of ethanol consumption on their cognate receptors. Initially, varying concentrations of each peptide were incubated with isolated hepatocytes from ethanol‐fed and pair‐fed control rats. These hepatocytes were then assayed for the ability to attach to laminin. The results Indicated that all three peptides effectively inhibited laminin‐mediated cell adhesion: the degree of inhibition appeared similar between pair‐fed controls and ethanol‐fed animals. Of the three peptides, PA22‐2 showed the most dramatic inhibition of attachment. Therefore, we investigated the ability of hepatocytes to attach directly to PA22‐2 itself. Attachment of hepatocytes from ethanol‐fed animals to PA22‐2 was impaired by 30% after 4 days and 90% by 14 days. Conversely, no significant difference in attachment to the entire laminin molecule was observed in ethanol‐fed animals at these early time points. These results indicated that the ethanol‐induced impairment of hepatocyte attachment to laminin may be caused by the decreased interaction of hepatocytes with specific functional sites on the laminin molecule and that specific receptors on the hepatocyte may be affected differently. Because laminin has been shown to influence cell proliferation, differentiation, and gene expression, this defect could potentially result in structural and functional changes of the hepatocytes.

KW - Ethanol

KW - Hepatocyte Attachment

KW - Laminin Peptide

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U2 - 10.1111/j.1530-0277.1994.tb00107.x

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VL - 18

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JO - Alcoholism: Clinical and Experimental Research

JF - Alcoholism: Clinical and Experimental Research

SN - 0145-6008

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