Rabbit corneal epithelial cells adhere to two distinct heparin-binding synthetic peptides derived from fibronectin

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Abstract

Fibronectin plays an important role in corneal reepithelialization during corneal wound healing. In this study, rabbit corneal epithelial (RCE) cell adhesion to fibronectin was further defined using proteolytic fragments of fibronectin and chemically synthesized peptides derived from the amino acid sequence of fibronectin. RCE cells adhere to intact fibronectin, the 75 kD fragment containing the RGDS (Arg-Gly-Asp-Ser) cell adhesion-promoting sequence, and the 33/66 kD cell adhesion promoting/heparin-binding fragments of fibronectin. The 75 kD fragment and the 33/66 kD fragments partially inhibited RCE cell adhesion to intact fibronectin, suggesting that these fragments represent distinct sites used by RCE cells to adhere to intact fibronectin. Two chemically synthesized peptides derived from the amino acid sequence of the 33/66 kD fragments of fibronectin, FN-C/H-I (YEKPGSPPREVVPRPRPGV) and FN-C/H-III (YRVRVTPKEKTGPMKE), directly promoted the adhesion of RCE cells. As further evidence that FN-C/H-I and FN-C/H-III play a role in the adhesion of RCE cells to the 33/66 kD fragments of fibronectin, we have shown that soluble FN-C/H-I and FN-C/H-III inhibited RCE cell adhesion on surfaces coated with the 33/66 kD fragments. In addition, polyclonal IgG against FN-C/H-I and FN-C/H-III partially blocked RCE cell adhesion to the 33/66 kD fragments, confirming that these sequences represent adhesion-promoting sites within these fragments. In contrast, two previously described peptides from the 33/66 kD fragments of fibronectin, which promoted the adhesion of a variety of cell types, FN-C/H-II (KNNQKSEPLIGRKKT) and CS-1 (DELPQLVTLPHPNLHGPEILDVPST), did not support RCE cell adhesion. These data suggest that RCE cell adhesion to fibronectin has a complex molecular basis and is mediated by multiple domains, at least two of which are located within the carboxyl-terminal heparin-binding/cell adhesion-promoting domains of fibronectin.

Original languageEnglish (US)
Pages (from-to)3034-3040
Number of pages7
JournalInvestigative Ophthalmology and Visual Science
Volume33
Issue number11
StatePublished - Jan 1 1992

Fingerprint

Fibronectins
Heparin
Epithelial Cells
Rabbits
Cell Adhesion
Peptides
Amino Acid Sequence
arginyl-glycyl-aspartyl-serine
Wound Healing
Immunoglobulin G

Keywords

  • adhesion
  • cornea
  • epithelium
  • fibronectin
  • motility

Cite this

@article{49a31871b4eb4e8daa9657353bba279f,
title = "Rabbit corneal epithelial cells adhere to two distinct heparin-binding synthetic peptides derived from fibronectin",
abstract = "Fibronectin plays an important role in corneal reepithelialization during corneal wound healing. In this study, rabbit corneal epithelial (RCE) cell adhesion to fibronectin was further defined using proteolytic fragments of fibronectin and chemically synthesized peptides derived from the amino acid sequence of fibronectin. RCE cells adhere to intact fibronectin, the 75 kD fragment containing the RGDS (Arg-Gly-Asp-Ser) cell adhesion-promoting sequence, and the 33/66 kD cell adhesion promoting/heparin-binding fragments of fibronectin. The 75 kD fragment and the 33/66 kD fragments partially inhibited RCE cell adhesion to intact fibronectin, suggesting that these fragments represent distinct sites used by RCE cells to adhere to intact fibronectin. Two chemically synthesized peptides derived from the amino acid sequence of the 33/66 kD fragments of fibronectin, FN-C/H-I (YEKPGSPPREVVPRPRPGV) and FN-C/H-III (YRVRVTPKEKTGPMKE), directly promoted the adhesion of RCE cells. As further evidence that FN-C/H-I and FN-C/H-III play a role in the adhesion of RCE cells to the 33/66 kD fragments of fibronectin, we have shown that soluble FN-C/H-I and FN-C/H-III inhibited RCE cell adhesion on surfaces coated with the 33/66 kD fragments. In addition, polyclonal IgG against FN-C/H-I and FN-C/H-III partially blocked RCE cell adhesion to the 33/66 kD fragments, confirming that these sequences represent adhesion-promoting sites within these fragments. In contrast, two previously described peptides from the 33/66 kD fragments of fibronectin, which promoted the adhesion of a variety of cell types, FN-C/H-II (KNNQKSEPLIGRKKT) and CS-1 (DELPQLVTLPHPNLHGPEILDVPST), did not support RCE cell adhesion. These data suggest that RCE cell adhesion to fibronectin has a complex molecular basis and is mediated by multiple domains, at least two of which are located within the carboxyl-terminal heparin-binding/cell adhesion-promoting domains of fibronectin.",
keywords = "adhesion, cornea, epithelium, fibronectin, motility",
author = "Mooradian, {Daniel L} and {Mc Carthy}, {James B} and Cameron, {John D} and Skubitz, {Amy P} and Furcht, {Leo T}",
year = "1992",
month = "1",
day = "1",
language = "English (US)",
volume = "33",
pages = "3034--3040",
journal = "Investigative Ophthalmology and Visual Science",
issn = "0146-0404",
publisher = "Association for Research in Vision and Ophthalmology Inc.",
number = "11",

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TY - JOUR

T1 - Rabbit corneal epithelial cells adhere to two distinct heparin-binding synthetic peptides derived from fibronectin

AU - Mooradian, Daniel L

AU - Mc Carthy, James B

AU - Cameron, John D

AU - Skubitz, Amy P

AU - Furcht, Leo T

PY - 1992/1/1

Y1 - 1992/1/1

N2 - Fibronectin plays an important role in corneal reepithelialization during corneal wound healing. In this study, rabbit corneal epithelial (RCE) cell adhesion to fibronectin was further defined using proteolytic fragments of fibronectin and chemically synthesized peptides derived from the amino acid sequence of fibronectin. RCE cells adhere to intact fibronectin, the 75 kD fragment containing the RGDS (Arg-Gly-Asp-Ser) cell adhesion-promoting sequence, and the 33/66 kD cell adhesion promoting/heparin-binding fragments of fibronectin. The 75 kD fragment and the 33/66 kD fragments partially inhibited RCE cell adhesion to intact fibronectin, suggesting that these fragments represent distinct sites used by RCE cells to adhere to intact fibronectin. Two chemically synthesized peptides derived from the amino acid sequence of the 33/66 kD fragments of fibronectin, FN-C/H-I (YEKPGSPPREVVPRPRPGV) and FN-C/H-III (YRVRVTPKEKTGPMKE), directly promoted the adhesion of RCE cells. As further evidence that FN-C/H-I and FN-C/H-III play a role in the adhesion of RCE cells to the 33/66 kD fragments of fibronectin, we have shown that soluble FN-C/H-I and FN-C/H-III inhibited RCE cell adhesion on surfaces coated with the 33/66 kD fragments. In addition, polyclonal IgG against FN-C/H-I and FN-C/H-III partially blocked RCE cell adhesion to the 33/66 kD fragments, confirming that these sequences represent adhesion-promoting sites within these fragments. In contrast, two previously described peptides from the 33/66 kD fragments of fibronectin, which promoted the adhesion of a variety of cell types, FN-C/H-II (KNNQKSEPLIGRKKT) and CS-1 (DELPQLVTLPHPNLHGPEILDVPST), did not support RCE cell adhesion. These data suggest that RCE cell adhesion to fibronectin has a complex molecular basis and is mediated by multiple domains, at least two of which are located within the carboxyl-terminal heparin-binding/cell adhesion-promoting domains of fibronectin.

AB - Fibronectin plays an important role in corneal reepithelialization during corneal wound healing. In this study, rabbit corneal epithelial (RCE) cell adhesion to fibronectin was further defined using proteolytic fragments of fibronectin and chemically synthesized peptides derived from the amino acid sequence of fibronectin. RCE cells adhere to intact fibronectin, the 75 kD fragment containing the RGDS (Arg-Gly-Asp-Ser) cell adhesion-promoting sequence, and the 33/66 kD cell adhesion promoting/heparin-binding fragments of fibronectin. The 75 kD fragment and the 33/66 kD fragments partially inhibited RCE cell adhesion to intact fibronectin, suggesting that these fragments represent distinct sites used by RCE cells to adhere to intact fibronectin. Two chemically synthesized peptides derived from the amino acid sequence of the 33/66 kD fragments of fibronectin, FN-C/H-I (YEKPGSPPREVVPRPRPGV) and FN-C/H-III (YRVRVTPKEKTGPMKE), directly promoted the adhesion of RCE cells. As further evidence that FN-C/H-I and FN-C/H-III play a role in the adhesion of RCE cells to the 33/66 kD fragments of fibronectin, we have shown that soluble FN-C/H-I and FN-C/H-III inhibited RCE cell adhesion on surfaces coated with the 33/66 kD fragments. In addition, polyclonal IgG against FN-C/H-I and FN-C/H-III partially blocked RCE cell adhesion to the 33/66 kD fragments, confirming that these sequences represent adhesion-promoting sites within these fragments. In contrast, two previously described peptides from the 33/66 kD fragments of fibronectin, which promoted the adhesion of a variety of cell types, FN-C/H-II (KNNQKSEPLIGRKKT) and CS-1 (DELPQLVTLPHPNLHGPEILDVPST), did not support RCE cell adhesion. These data suggest that RCE cell adhesion to fibronectin has a complex molecular basis and is mediated by multiple domains, at least two of which are located within the carboxyl-terminal heparin-binding/cell adhesion-promoting domains of fibronectin.

KW - adhesion

KW - cornea

KW - epithelium

KW - fibronectin

KW - motility

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