ChloroquineV1, Main, Merge, bibRecord, 003206

Decreased adenylate cyclase activation by helodermin and PGE1 in the lectin-resistant variant Wa4 of the mouse melanoma cell line B16

Identifieur interne : 003206 ( Main/Merge ); précédent : 003205; suivant : 003207

Decreased adenylate cyclase activation by helodermin and PGE1 in the lectin-resistant variant Wa4 of the mouse melanoma cell line B16

Auteurs : Catherine Damien [Belgique] ; Patrick Robberecht ; Robert Hooghe [Belgique] ; Philippe De Neef [Belgique] ; Jean Christophe [Belgique]

Source :

Peptides [ 0196-9781 ] ; 1989.

RBID : ISTEX:DA95B6813B99D583FE43603232D1898B3A18E72F

English descriptors

Teeft :
- Adenylate, Adenylate cyclase, Adenylate cyclase activation, Adenylate cyclase activity, Adenylate cyclase system, Cell line, Cell lines, Cell membranes, Cholera, Cholera toxin, Christophe, Clone, Cyclase, Cyclic, Febs lett, Helodermin, Higher potency, Melanoma, Melanoma cells, Melanoma clones, Membrane, Mouse melanoma, Mouse melanoma cell line, Neef, Peptide, Pmol cyclic, Prostaglandin, Receptor, Robberecht, Toxin.

Abstract

Abstract: We examined the cultured mouse melanoma cell line B16 (clone F1) and its wheat germ agglutinin-resistant variant Wa4 that suffers from abnormal protein glycosylation (a high fucose:sialic acid ratio in glycoproteins). In both cell lines the adenylate cyclase system was endowed with a functional guanine nucleotide binding protein Gs and was efficiently coupled to α-MSH receptors. In the B16 cell line F1 studied we also observed an efficient stimulation of adenylate cyclase activity by helodermin, VIP and the VIP analogue [acetyl-His1]VIP, and also by PGE1. In membranes from the lectin-resistant variant Wa4, the stimulations by VIP-like peptides and by PGE1 were reduced by 60% and 50%, respectively, while the stimulation by α-MSH remained normal. As other components of the adenylate cyclase system (Gs site, catalytical unit) appeared unchanged in the Wa4 variant, we conclude that impaired glycosylation essentially affected the number of both VIP-like peptide receptors and PGE1 receptors.

Url:

https://api.istex.fr/ark:/67375/6H6-202G12D1-V/fulltext.pdf

DOI: 10.1016/0196-9781(89)90192-7

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ISTEX:DA95B6813B99D583FE43603232D1898B3A18E72F

Le document en format XML

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<term>Cell line</term>
<term>Cell lines</term>
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<term>Cholera</term>
<term>Cholera toxin</term>
<term>Christophe</term>
<term>Clone</term>
<term>Cyclase</term>
<term>Cyclic</term>
<term>Febs lett</term>
<term>Helodermin</term>
<term>Higher potency</term>
<term>Melanoma</term>
<term>Melanoma cells</term>
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<term>Membrane</term>
<term>Mouse melanoma</term>
<term>Mouse melanoma cell line</term>
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<term>Peptide</term>
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<front><div type="abstract" xml:lang="en">Abstract: We examined the cultured mouse melanoma cell line B16 (clone F1) and its wheat germ agglutinin-resistant variant Wa4 that suffers from abnormal protein glycosylation (a high fucose:sialic acid ratio in glycoproteins). In both cell lines the adenylate cyclase system was endowed with a functional guanine nucleotide binding protein Gs and was efficiently coupled to α-MSH receptors. In the B16 cell line F1 studied we also observed an efficient stimulation of adenylate cyclase activity by helodermin, VIP and the VIP analogue [acetyl-His1]VIP, and also by PGE1. In membranes from the lectin-resistant variant Wa4, the stimulations by VIP-like peptides and by PGE1 were reduced by 60% and 50%, respectively, while the stimulation by α-MSH remained normal. As other components of the adenylate cyclase system (Gs site, catalytical unit) appeared unchanged in the Wa4 variant, we conclude that impaired glycosylation essentially affected the number of both VIP-like peptide receptors and PGE1 receptors.</div>
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Decreased adenylate cyclase activation by helodermin and PGE1 in the lectin-resistant variant Wa4 of the mouse melanoma cell line B16

Decreased adenylate cyclase activation by helodermin and PGE1 in the lectin-resistant variant Wa4 of the mouse melanoma cell line B16

Source :

English descriptors

Abstract

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Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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