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Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies
Laminin derived from the Engelbreth-Holm-Swarm (EHS) tumor and a lamininlike molecule synthesized by RN22 Schwannoma cells both stimulate rapid neurite outgrowth, consistent with a common neurite- promoting site. However, antilaminin antisera can only inhibit the activity of the EHS laminin. The blo...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1988
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114995/ https://www.ncbi.nlm.nih.gov/pubmed/2452171 |
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collection | PubMed |
description | Laminin derived from the Engelbreth-Holm-Swarm (EHS) tumor and a lamininlike molecule synthesized by RN22 Schwannoma cells both stimulate rapid neurite outgrowth, consistent with a common neurite- promoting site. However, antilaminin antisera can only inhibit the activity of the EHS laminin. The blocking antibodies in such sera are directed against the terminal heparin-binding domain of the laminin long arm (Edgar, D., R. Timpl, and H. Thoenen. 1984. EMBO [Eur. Mol. Biol. Organ.] J. 3: 1463-1468). These epitopes are demonstrated by immunoblotting to be part of the A chain and to be absent in RN22 laminin, showing (through metabolic labeling) that the cells synthesized little if any 440-kD A chain. This indicates that the antibody inhibition was probably due to steric hindrance, a common neurite-promoting site, apparently not being antigenic in native molecules. Antibodies raised against a 25-kD proteolytic fragment derived from the long arm of laminin were then used as probes to identify other potential neurite-promoting structures. Although these antibodies do not cross-react with native laminin, they recognized the B chains of denatured EHS and RN22 molecules on immunoblots. The antibodies also bound to the large proteolytic fragment, derived from the long arm of laminin that contains the neurite-promoting site, thus inhibiting its activity. Taken together, these results point to the localization of normally nonantigenic, defined, B chain sequences within or close to the neurite-promoting site of laminin. |
format | Text |
id | pubmed-2114995 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1988 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21149952008-05-01 Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies J Cell Biol Articles Laminin derived from the Engelbreth-Holm-Swarm (EHS) tumor and a lamininlike molecule synthesized by RN22 Schwannoma cells both stimulate rapid neurite outgrowth, consistent with a common neurite- promoting site. However, antilaminin antisera can only inhibit the activity of the EHS laminin. The blocking antibodies in such sera are directed against the terminal heparin-binding domain of the laminin long arm (Edgar, D., R. Timpl, and H. Thoenen. 1984. EMBO [Eur. Mol. Biol. Organ.] J. 3: 1463-1468). These epitopes are demonstrated by immunoblotting to be part of the A chain and to be absent in RN22 laminin, showing (through metabolic labeling) that the cells synthesized little if any 440-kD A chain. This indicates that the antibody inhibition was probably due to steric hindrance, a common neurite-promoting site, apparently not being antigenic in native molecules. Antibodies raised against a 25-kD proteolytic fragment derived from the long arm of laminin were then used as probes to identify other potential neurite-promoting structures. Although these antibodies do not cross-react with native laminin, they recognized the B chains of denatured EHS and RN22 molecules on immunoblots. The antibodies also bound to the large proteolytic fragment, derived from the long arm of laminin that contains the neurite-promoting site, thus inhibiting its activity. Taken together, these results point to the localization of normally nonantigenic, defined, B chain sequences within or close to the neurite-promoting site of laminin. The Rockefeller University Press 1988-04-01 /pmc/articles/PMC2114995/ /pubmed/2452171 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title | Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title_full | Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title_fullStr | Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title_full_unstemmed | Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title_short | Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
title_sort | structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114995/ https://www.ncbi.nlm.nih.gov/pubmed/2452171 |