Localization of the chemotactic domain in fibronectin

A. Albini, H. Richter, B. F. Pontz

Research output: Contribution to journalArticle

Abstract

Fragments derived from human plasma fibronectin by enzymatic degradation were tested in the Boyden chamber for chemotactic activity towards various fibroblast strains. The results provide clear evidence that the chemotactic activity is restricted to a defined region of the fibronectin molecule which is the same for various fibroblast strains. The active domain is localized between the collagen binding site and the major heparin binding site, about 170 kDa apart from the N-terminal and about 70 kDa from the C-terminal ends of the two subunit peptide chains.

Original languageEnglish
Pages (from-to)222-226
Number of pages5
JournalFEBS Letters
Volume156
Issue number2
DOIs
Publication statusPublished - Jun 13 1983

Fingerprint

Fibroblasts
Fibronectins
Binding Sites
Plasma (human)
Heparin
Collagen
Degradation
Peptides
Molecules

Keywords

  • Boyden chamber
  • Fibroblast chemotaxis
  • Fibronectin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Localization of the chemotactic domain in fibronectin. / Albini, A.; Richter, H.; Pontz, B. F.

In: FEBS Letters, Vol. 156, No. 2, 13.06.1983, p. 222-226.

Research output: Contribution to journalArticle

Albini, A. ; Richter, H. ; Pontz, B. F. / Localization of the chemotactic domain in fibronectin. In: FEBS Letters. 1983 ; Vol. 156, No. 2. pp. 222-226.
@article{07a6874595494d9a8ed40afccba393b1,
title = "Localization of the chemotactic domain in fibronectin",
abstract = "Fragments derived from human plasma fibronectin by enzymatic degradation were tested in the Boyden chamber for chemotactic activity towards various fibroblast strains. The results provide clear evidence that the chemotactic activity is restricted to a defined region of the fibronectin molecule which is the same for various fibroblast strains. The active domain is localized between the collagen binding site and the major heparin binding site, about 170 kDa apart from the N-terminal and about 70 kDa from the C-terminal ends of the two subunit peptide chains.",
keywords = "Boyden chamber, Fibroblast chemotaxis, Fibronectin",
author = "A. Albini and H. Richter and Pontz, {B. F.}",
year = "1983",
month = "6",
day = "13",
doi = "10.1016/0014-5793(83)80500-6",
language = "English",
volume = "156",
pages = "222--226",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Localization of the chemotactic domain in fibronectin

AU - Albini, A.

AU - Richter, H.

AU - Pontz, B. F.

PY - 1983/6/13

Y1 - 1983/6/13

N2 - Fragments derived from human plasma fibronectin by enzymatic degradation were tested in the Boyden chamber for chemotactic activity towards various fibroblast strains. The results provide clear evidence that the chemotactic activity is restricted to a defined region of the fibronectin molecule which is the same for various fibroblast strains. The active domain is localized between the collagen binding site and the major heparin binding site, about 170 kDa apart from the N-terminal and about 70 kDa from the C-terminal ends of the two subunit peptide chains.

AB - Fragments derived from human plasma fibronectin by enzymatic degradation were tested in the Boyden chamber for chemotactic activity towards various fibroblast strains. The results provide clear evidence that the chemotactic activity is restricted to a defined region of the fibronectin molecule which is the same for various fibroblast strains. The active domain is localized between the collagen binding site and the major heparin binding site, about 170 kDa apart from the N-terminal and about 70 kDa from the C-terminal ends of the two subunit peptide chains.

KW - Boyden chamber

KW - Fibroblast chemotaxis

KW - Fibronectin

UR - http://www.scopus.com/inward/record.url?scp=0020626774&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020626774&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(83)80500-6

DO - 10.1016/0014-5793(83)80500-6

M3 - Article

C2 - 6852256

AN - SCOPUS:0020626774

VL - 156

SP - 222

EP - 226

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -