pubmed-article:8928790 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0085979 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0026727 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C1704242 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0439708 | lld:lifeskim |
pubmed-article:8928790 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
pubmed-article:8928790 | pubmed:issue | 4 Pt 1 | lld:pubmed |
pubmed-article:8928790 | pubmed:dateCreated | 1996-11-20 | lld:pubmed |
pubmed-article:8928790 | pubmed:abstractText | Binding and localization of transforming growth factor-alpha (TGF-alpha) and epidermal growth factor (EGF) were assessed using in vitro primary cultures of guinea pig gastric mucous epithelial cells (GMEC). GMEC were isolated and cultured in six-well plates with Dulbecco's modified Eagle's medium + 10% serum and then changed to serum-free medium for 24 h for binding studies. The binding time course of 125I-labeled EGF and 125I-TGF-alpha in GMEC cultures at 4 degrees C was saturable, reaching a plateau within 4-6 h. Competition-binding curves revealed that the amount of unlabeled EGF and TGF-alpha to reduce 125I-EGF binding by 50% was 0.35 and 0.23 nM, respectively. The amount of unlabeled EGF and TGF-alpha to decrease 125I-TGF-alpha binding by 50% was 0.30 and 0.21 nM, respectively. A Scatchard analysis of the data disclosed that a single class of high-affinity binding sites (dissociation constant = 0.24 nM) was present. The maximal binding capacity was approximately 20 fmol/10(6) cells or approximately 12,000 receptors per cell. The binding of 125I-EGF and 125I-TFG-alpha to GMEC cultures was maximal between pH 7.0 and 8.5. No specific binding of EGF or TGF-alpha could be detected below pH 5.0. The half-maximal pH dissociation value for EGF and TGF-alpha was pH 5.89 and pH 6.83, respectively. We found no difference in the final amounts of membrane-bound or internalized 125I-EGF and 125I-TGF-alpha. However, there was a significant difference (P < 0.05) at 5-30 min in the rate of dissociated and internalized 125I-EGF- and 125I-TGF-alpha. Immunofluorescence microscopy of GMEC cultures for EGF/TGF-alpha receptors showed increased fluorescence at the leading edges and around the perimeter of cells. Detection of an EGF/TGF-alpha receptor was also confirmed by Western blotting. Our findings demonstrate that guinea pig GMEC possess a specific EGF/TGF-alpha receptor, which further supports a physiological role for EFG and TFG-alpha as mitogens in these cells. | lld:pubmed |
pubmed-article:8928790 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8928790 | pubmed:language | eng | lld:pubmed |
pubmed-article:8928790 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8928790 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8928790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8928790 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8928790 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8928790 | pubmed:issn | 0002-9513 | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:DempseyP JPJ | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:DeveneyC WCW | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:CrassR ARA | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:CoffeyR JRJJr | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:SheppardB CBC | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:RuttenM JMJ | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:LuttroppC ACA | lld:pubmed |
pubmed-article:8928790 | pubmed:author | pubmed-author:HawkeyM AMA | lld:pubmed |
pubmed-article:8928790 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8928790 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:8928790 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8928790 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8928790 | pubmed:pagination | G604-12 | lld:pubmed |
pubmed-article:8928790 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:8928790 | pubmed:meshHeading | pubmed-meshheading:8928790-... | lld:pubmed |
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pubmed-article:8928790 | pubmed:meshHeading | pubmed-meshheading:8928790-... | lld:pubmed |
pubmed-article:8928790 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8928790 | pubmed:articleTitle | Identification of an EGF/TGF-alpha receptor in primary cultures of guinea pig gastric mucous epithelial cells. | lld:pubmed |
pubmed-article:8928790 | pubmed:affiliation | Department of Surgery, Oregon Health Sciences University, Portland, USA. | lld:pubmed |
pubmed-article:8928790 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8928790 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8928790 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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