J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth

A. Lochter, L. Vaughan, A. Kaplony, A. Prochiantz, Melitta Camartin, A. Faissner

Research output: Contribution to journalArticle

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Abstract

The influence of J1/tenascin adsorbed to polyornithine-conditioned plastic (substrate-bound J1/tenascin) and J1/tenascin present in the culture medium (soluble J1/tenascin) on neurite outgrowth was studied with cultured single cells from hippocampus and mesencephalon of embryonic rats. Neurons at low density grew well on J1/tenascin substrates and extended neurites that were ~40% longer than on the polyornithine control substrate after 24 h in vitro. The neurite outgrowth promoting effect of substrate bound J1/tenascin was largely abolished in the presence of mAb J1/tn2, but not by mAb J1/tn1. In contrast to the neurite growth-promoting effects of substrate bound J1/tenascin, neurite outgrowth on polyornithine, laminin, fibronectin, or J1/tenascin as substrates was inhibited by addition of soluble J1/tenascin to the cultures. Neither of the two mAbs neutralized the neurite outgrowth-inhibitory properties of soluble J1/tenascin. In contrast to their opposite effects on neurite outgrowth, both substrate-bound and soluble J1/tenascin reduced spreading of the neuronal cell bodies, suggesting that the neurite outgrowth-promoting and antispreading effects are mediated by two different sites on the molecule. This was further supported by the inability of the mAb J1/tn2 to neutralize the antispreading effect. The J1/tn2 epitope localizes to a fibronectin type III homology domain that is presumably distinct from the putative Tn68 cell-binding domain of chicken tenascin for fibroblasts, as shown by electronmicroscopic localization of antibody binding sites. We infer from these experiments that J1/tenascin contains a neurite outgrowth promoting domain that is distinguishable from the cell-binding site and presumably not involved in the inhibition of neurite outgrowth or cell spreading. Our observations support the notion that J1/tenascin is a multifunctional extracellular matrix molecule.

Original languageEnglish (US)
Pages (from-to)1159-1171
Number of pages13
JournalJournal of Cell Biology
Volume113
Issue number5
DOIs
StatePublished - Jan 1 1991

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Tenascin
Neurites
Neuronal Outgrowth
Antibody Binding Sites
Laminin
Mesencephalon
Fibronectins

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Lochter, A. ; Vaughan, L. ; Kaplony, A. ; Prochiantz, A. ; Camartin, Melitta ; Faissner, A. / J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. In: Journal of Cell Biology. 1991 ; Vol. 113, No. 5. pp. 1159-1171.
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abstract = "The influence of J1/tenascin adsorbed to polyornithine-conditioned plastic (substrate-bound J1/tenascin) and J1/tenascin present in the culture medium (soluble J1/tenascin) on neurite outgrowth was studied with cultured single cells from hippocampus and mesencephalon of embryonic rats. Neurons at low density grew well on J1/tenascin substrates and extended neurites that were ~40{\%} longer than on the polyornithine control substrate after 24 h in vitro. The neurite outgrowth promoting effect of substrate bound J1/tenascin was largely abolished in the presence of mAb J1/tn2, but not by mAb J1/tn1. In contrast to the neurite growth-promoting effects of substrate bound J1/tenascin, neurite outgrowth on polyornithine, laminin, fibronectin, or J1/tenascin as substrates was inhibited by addition of soluble J1/tenascin to the cultures. Neither of the two mAbs neutralized the neurite outgrowth-inhibitory properties of soluble J1/tenascin. In contrast to their opposite effects on neurite outgrowth, both substrate-bound and soluble J1/tenascin reduced spreading of the neuronal cell bodies, suggesting that the neurite outgrowth-promoting and antispreading effects are mediated by two different sites on the molecule. This was further supported by the inability of the mAb J1/tn2 to neutralize the antispreading effect. The J1/tn2 epitope localizes to a fibronectin type III homology domain that is presumably distinct from the putative Tn68 cell-binding domain of chicken tenascin for fibroblasts, as shown by electronmicroscopic localization of antibody binding sites. We infer from these experiments that J1/tenascin contains a neurite outgrowth promoting domain that is distinguishable from the cell-binding site and presumably not involved in the inhibition of neurite outgrowth or cell spreading. Our observations support the notion that J1/tenascin is a multifunctional extracellular matrix molecule.",
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J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. / Lochter, A.; Vaughan, L.; Kaplony, A.; Prochiantz, A.; Camartin, Melitta; Faissner, A.

In: Journal of Cell Biology, Vol. 113, No. 5, 01.01.1991, p. 1159-1171.

Research output: Contribution to journalArticle

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T1 - J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth

AU - Lochter, A.

AU - Vaughan, L.

AU - Kaplony, A.

AU - Prochiantz, A.

AU - Camartin, Melitta

AU - Faissner, A.

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