Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
115
|
| pubmed:dateCreated |
1998-8-31
|
| pubmed:abstractText |
Using a monoclonal antibody (GHRP2-88) raised against the extracellular portion of human growth hormone receptor (hGHR), the mechanisms on modulations of cellular levels of hGHR were investigated in human IM-9 cells. Upon stimulation with human growth hormone (hGH), hGHRs on the cell surface are down-regulated through internalization and degradation of hGHR. For hGHR internalization, hGH-mediated dimerization of hGHRs, but not staurosporine-sensitive phosphorylation is required. For hGHR degradation, however, staurosporine-sensitive phosphorylation is necessary. In the absence of hGH, hGHRs on the cell surface are cleaved to release human growth hormone-binding proteins (hGH-BPs), probably by a metalloprotease. In the presence of hGH, the hGH-BP release was rather decreased based on the reduction in cell surface hGHRs. Thus, the cell surface level of hGHR may be regulated post-translationally by the two mechanisms depending on the external hGH levels.
|
| pubmed:language |
jpn
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1343-4292
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
27-39
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1997
|
| pubmed:articleTitle |
[Modulations of human growth hormone receptor level on the cell surface].
|
| pubmed:affiliation |
yoshiro@nihs.go.jp
|
| pubmed:publicationType |
Journal Article,
English Abstract,
Review
|