Forskning ved Københavns Universitet - Københavns Universitet

Forside

Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins. / Gibson, W T; Couchman, J R; Badley, R A; Saunders, H J; Smith, C G.

I: European Journal of Cell Biology, Bind 30, Nr. 2, 1983, s. 205-13.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Gibson, WT, Couchman, JR, Badley, RA, Saunders, HJ & Smith, CG 1983, 'Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins.', European Journal of Cell Biology, bind 30, nr. 2, s. 205-13.

APA

Gibson, W. T., Couchman, J. R., Badley, R. A., Saunders, H. J., & Smith, C. G. (1983). Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins. European Journal of Cell Biology, 30(2), 205-13.

Vancouver

Gibson WT, Couchman JR, Badley RA, Saunders HJ, Smith CG. Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins. European Journal of Cell Biology. 1983;30(2):205-13.

Author

Gibson, W T ; Couchman, J R ; Badley, R A ; Saunders, H J ; Smith, C G. / Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins. I: European Journal of Cell Biology. 1983 ; Bind 30, Nr. 2. s. 205-13.

Bibtex

@article{3cf18700598f11dd8d9f000ea68e967b,
title = "Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins.",
abstract = "The aim of this study was to investigate whether epidermal cells can synthesise fibronectin and whether the distribution of this glycoprotein is related to the adhesion and cytoskeletal organisation of these cells. The production of fibronectin by newborn rat epidermal cells was shown by indirect immunofluorescence staining of cultures grown in the absence of a feeder layer using an antiserum which had been cross-adsorbed with foetal calf serum proteins to remove antibodies which recognised serum fibronectin. The distribution of fibronectin in areas of cell-cell and cell-substratum contact, characteristically in the form of short radial stitches, was examined in more detail using immunoelectron microscopy with colloidal gold as marker. This showed the close proximity of fibronectin to the cell membrane, with the ventral surface and fine cellular processes showing the heaviest labelling, and also revealed evidence of a relationship between external fibronectin and internal structure in epidermal cells. Immunofluorescence showed that tonofilaments (keratin) and microtubules were present as fibrillar arrays but were not related to fibronectin distribution. Vimentin and desmin were absent. Actin was distributed as a circumferential bundle of filaments, with finer stands running radially to the edge. The latter were reminiscent of the radial fibronectin stitches and a spatial correspondence between fibronectin and actin was confirmed by double-label immunofluorescence which revealed many instances of overlap and colinearity of actin and fibronectin filaments. The ability of keratinocytes to produce fibronectin suggests that these cells can contribute to the formation of the basement membrane in skin. The localisation of fibronectin and its close association with actin also suggests that it is involved in keratinocyte adhesion and is related to the internal organisation of these cells.",
author = "Gibson, {W T} and Couchman, {J R} and Badley, {R A} and Saunders, {H J} and Smith, {C G}",
note = "Keywords: Actins; Animals; Animals, Newborn; Cytoskeleton; Desmin; Fibronectins; Keratinocytes; Keratins; Microscopy, Fluorescence; Microscopy, Immunoelectron; Microscopy, Phase-Contrast; Microtubules; Rabbits; Rats; Vimentin",
year = "1983",
language = "English",
volume = "30",
pages = "205--13",
journal = "European Journal of Cell Biology",
issn = "0171-9335",
publisher = "Elsevier GmbH - Urban und Fischer",
number = "2",

}

RIS

TY - JOUR

T1 - Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins.

AU - Gibson, W T

AU - Couchman, J R

AU - Badley, R A

AU - Saunders, H J

AU - Smith, C G

N1 - Keywords: Actins; Animals; Animals, Newborn; Cytoskeleton; Desmin; Fibronectins; Keratinocytes; Keratins; Microscopy, Fluorescence; Microscopy, Immunoelectron; Microscopy, Phase-Contrast; Microtubules; Rabbits; Rats; Vimentin

PY - 1983

Y1 - 1983

N2 - The aim of this study was to investigate whether epidermal cells can synthesise fibronectin and whether the distribution of this glycoprotein is related to the adhesion and cytoskeletal organisation of these cells. The production of fibronectin by newborn rat epidermal cells was shown by indirect immunofluorescence staining of cultures grown in the absence of a feeder layer using an antiserum which had been cross-adsorbed with foetal calf serum proteins to remove antibodies which recognised serum fibronectin. The distribution of fibronectin in areas of cell-cell and cell-substratum contact, characteristically in the form of short radial stitches, was examined in more detail using immunoelectron microscopy with colloidal gold as marker. This showed the close proximity of fibronectin to the cell membrane, with the ventral surface and fine cellular processes showing the heaviest labelling, and also revealed evidence of a relationship between external fibronectin and internal structure in epidermal cells. Immunofluorescence showed that tonofilaments (keratin) and microtubules were present as fibrillar arrays but were not related to fibronectin distribution. Vimentin and desmin were absent. Actin was distributed as a circumferential bundle of filaments, with finer stands running radially to the edge. The latter were reminiscent of the radial fibronectin stitches and a spatial correspondence between fibronectin and actin was confirmed by double-label immunofluorescence which revealed many instances of overlap and colinearity of actin and fibronectin filaments. The ability of keratinocytes to produce fibronectin suggests that these cells can contribute to the formation of the basement membrane in skin. The localisation of fibronectin and its close association with actin also suggests that it is involved in keratinocyte adhesion and is related to the internal organisation of these cells.

AB - The aim of this study was to investigate whether epidermal cells can synthesise fibronectin and whether the distribution of this glycoprotein is related to the adhesion and cytoskeletal organisation of these cells. The production of fibronectin by newborn rat epidermal cells was shown by indirect immunofluorescence staining of cultures grown in the absence of a feeder layer using an antiserum which had been cross-adsorbed with foetal calf serum proteins to remove antibodies which recognised serum fibronectin. The distribution of fibronectin in areas of cell-cell and cell-substratum contact, characteristically in the form of short radial stitches, was examined in more detail using immunoelectron microscopy with colloidal gold as marker. This showed the close proximity of fibronectin to the cell membrane, with the ventral surface and fine cellular processes showing the heaviest labelling, and also revealed evidence of a relationship between external fibronectin and internal structure in epidermal cells. Immunofluorescence showed that tonofilaments (keratin) and microtubules were present as fibrillar arrays but were not related to fibronectin distribution. Vimentin and desmin were absent. Actin was distributed as a circumferential bundle of filaments, with finer stands running radially to the edge. The latter were reminiscent of the radial fibronectin stitches and a spatial correspondence between fibronectin and actin was confirmed by double-label immunofluorescence which revealed many instances of overlap and colinearity of actin and fibronectin filaments. The ability of keratinocytes to produce fibronectin suggests that these cells can contribute to the formation of the basement membrane in skin. The localisation of fibronectin and its close association with actin also suggests that it is involved in keratinocyte adhesion and is related to the internal organisation of these cells.

M3 - Journal article

C2 - 11596494

VL - 30

SP - 205

EP - 213

JO - European Journal of Cell Biology

JF - European Journal of Cell Biology

SN - 0171-9335

IS - 2

ER -

ID: 5167819