| pubmed-article:391 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:391 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:391 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:391 | pubmed:dateCreated | 1976-2-9 | lld:pubmed |
| pubmed-article:391 | pubmed:abstractText | NSILA-s (nonsuppressible insulin-like activity, soluble in acid ethanol) is a serum peptide that has insulin-like and growth-promoting activities. We have demonstrated previously that liver plasma membranes possess separate receptors for NSILA-s and insulin and have characterized the insulin receptor in detail. In the present study we have characterized the properties and specificity of the NSILA-s receptor and compared them to those of the insulin receptor in the same tissue. Both 125I-NSILA-s and 125I-insulin bind rapidly and reversibly to their receptors in liver membranes; maximal NSILA-s binding occurs at 20 degrees while maximal insulin binding is seen at 1-4 degrees. The pH optimum for NSILA-s binding is broad (6.0 to 8.0), in contrast to the very sharp pH optimum (7.5 to 8.0) for insulin binding. Both receptors exhibit a high degree of specificity. With the insulin receptor, NSILA-s and insulin analogues compete for binding in proportion to their insulin-like potency: insulin greater than proinsulin greater than NSILA-s. With the NSILA-s receptor, NSILA-s is most potent and the order is reversed: NSILA-s greater than proinsulin greater than insulin. Furthermore, six preparations of NSILA-s which varied 70-fold in biological activity competed for 125I-NSILA-s binding in order of their potencies. NSILA-s which had been inactivated biologically by reduction and aminoethylation and growth hormone were less than 1/100,000 as potent as the most purified NSILA-s preparation. Purified preparations of fibroblast growth factor, epidermal growth factor, nerve growth factor, and somatomedins B and C were less than 1% as effective as NSILA-s in competing for the 125I-NSILA-s suggesting that these factors act through other receptors. In contrast, somatomedin A was 10% as active as NSILA-s and multiplication-stimulating activity was fully as active as NSILA-s in competing for the NSILA-s receptor. Analysis of the data suggests that there are approximately 50 times more insulin receptors than NSILA-s receptors per liver cell, while the apparent affinity of NSILA-s receptors is somewhat higher than that of the insulin receptor. | lld:pubmed |
| pubmed-article:391 | pubmed:language | eng | lld:pubmed |
| pubmed-article:391 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:391 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:391 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:391 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:391 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:FroeschE RER | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:HumbelR ERE | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:RothJJ | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:NevilleD... | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:NissleyS PSP | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:KahnC RCR | lld:pubmed |
| pubmed-article:391 | pubmed:author | pubmed-author:MegyesiKK | lld:pubmed |
| pubmed-article:391 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:391 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:391 | pubmed:volume | 250 | lld:pubmed |
| pubmed-article:391 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:391 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:391 | pubmed:pagination | 8990-6 | lld:pubmed |
| pubmed-article:391 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Anim... | lld:pubmed |
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| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Cell... | lld:pubmed |
| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Prot... | lld:pubmed |
| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Solu... | lld:pubmed |
| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Bind... | lld:pubmed |
| pubmed-article:391 | pubmed:meshHeading | pubmed-meshheading:391-Rece... | lld:pubmed |
| pubmed-article:391 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:391 | pubmed:articleTitle | The NSILA-s receptor in liver plasma membranes. Characterization and comparison with the insulin receptor. | lld:pubmed |
| pubmed-article:391 | pubmed:publicationType | Journal Article | lld:pubmed |
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