| pubmed-article:1646599 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0599282 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0062482 | lld:lifeskim |
| pubmed-article:1646599 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:1646599 | pubmed:dateCreated | 1991-7-17 | lld:pubmed |
| pubmed-article:1646599 | pubmed:abstractText | Haemopexin receptors from mouse hepatoma (Hepa) cells were affinity-labelled by cross-linking to haem-125I-haemopexin complexes using two homo-[disuccinimidyl suberate (DSS) and 3,3'-dithiobis(succinimidyl propionate) (DTSSP)] and one hetero-[sulphosuccinimidyl 4-(p-maleimidophenyl)butyrate (sulpho-SMPB)] bifunctional cross-linking agents. Analysis of the cross-linked products by SDS/PAGE in the absence of reducing agents revealed that 125I-haemopexin was cross-linked specifically to a protein of apparent molecular mass 85-90 kDa. Upon reduction, haemopexin remained cross-linked to a protein of 20 kDa, suggesting that the murine haemopexin receptor has a subunit structure. Two subunits were identified: alpha (p65) and beta (p20). Furthermore, because haemopexin was cross-linked by all three agents to p20, the shortest cross-linker arm being 1.1 nm (11 A), we propose that the haem-haemopexin-binding site resides on this subunit. In addition, a cysteine residue of p20 is located near the haemopexin-binding site, since haemopexin, which has no free thiol groups, is cross-linked to this subunit by the hetero-bifunctional agent sulpho-SMPB. Exposure of Hepa cells to the tumour-promoting phorbol ester 4 alpha-phorbol 12-myristate 13-acetate (PMA) causes a rapid redistribution of haemopexin receptors from the cell surface to the cell interior. Within 2-4 min of incubation with 100 nM-PMA, there was an approx. 50% decrease in cell-surface haemopexin receptors, as judged by ligand binding at 0 degrees C and affinity labelling of the receptor. This time- and dose-dependent down-regulation was fully reversible within 60-90 min after removal of PMA, and the affinity of the remaining receptors was unaltered by PMA. The specificity of PMA was demonstrated by comparison with the non-tumour-promoter 4 alpha-phorbol, which did not affect any of the parameters examined. The amine H-7, a specific inhibitor of protein kinase C, antagonised the receptor redistribution effect of PMA, suggesting that the down-regulation of haemopexin receptors on the cell surface was a consequence of protein kinase C activation. The PMA-induced decrease in surface haemopexin receptors was due to a 2-fold increase in the rate of internalization (from 0.73 min-1 to 1.32 min-1), whereas the rate of exocytosis (0.6 min-1) was unchanged. PMA treatment, like binding of the natural ligand, haem-haemopexin, results in a lower steady-state level of surface haemopexin receptors independent of receptor synthesis, and the receptors were not degraded but were recycled back to the cell surface. | lld:pubmed |
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| pubmed-article:1646599 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1646599 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1646599 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1646599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1646599 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1646599 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1646599 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1646599 | pubmed:author | pubmed-author:SmithAA | lld:pubmed |
| pubmed-article:1646599 | pubmed:author | pubmed-author:MorganW TWT | lld:pubmed |
| pubmed-article:1646599 | pubmed:author | pubmed-author:FarooquiS MSM | lld:pubmed |
| pubmed-article:1646599 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1646599 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1646599 | pubmed:volume | 276 ( Pt 2) | lld:pubmed |
| pubmed-article:1646599 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1646599 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1646599 | pubmed:pagination | 417-25 | lld:pubmed |
| pubmed-article:1646599 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1646599 | pubmed:meshHeading | pubmed-meshheading:1646599-... | lld:pubmed |
| pubmed-article:1646599 | pubmed:year | 1991 | lld:pubmed |
