| dc.contributor.author |
Schmid, C |
en |
| dc.contributor.author |
Ghirlanda-Keller, C |
en |
| dc.contributor.author |
Zwimpfer, C |
en |
| dc.contributor.author |
Zoidis, E |
en |
| dc.date.accessioned |
2014-06-06T06:52:11Z |
|
| dc.date.available |
2014-06-06T06:52:11Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
0006291X |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.bbrc.2012.02.040 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5887 |
|
| dc.subject |
Cystatin C |
en |
| dc.subject |
Dexamethasone |
en |
| dc.subject |
Osteoblast |
en |
| dc.subject |
Triiodothyronine |
en |
| dc.subject.other |
cystatin C |
en |
| dc.subject.other |
dexamethasone |
en |
| dc.subject.other |
glucose |
en |
| dc.subject.other |
liothyronine |
en |
| dc.subject.other |
messenger RNA |
en |
| dc.subject.other |
animal cell |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
bone cell |
en |
| dc.subject.other |
calvaria |
en |
| dc.subject.other |
cell line |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
culture medium |
en |
| dc.subject.other |
dose response |
en |
| dc.subject.other |
drug potency |
en |
| dc.subject.other |
enzyme linked immunosorbent assay |
en |
| dc.subject.other |
glucose transport |
en |
| dc.subject.other |
hormonal regulation |
en |
| dc.subject.other |
in vitro study |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
nucleotide sequence |
en |
| dc.subject.other |
osteoblast |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein degradation |
en |
| dc.subject.other |
protein expression |
en |
| dc.subject.other |
protein folding |
en |
| dc.subject.other |
protein synthesis |
en |
| dc.subject.other |
Western blotting |
en |
| dc.subject.other |
Alkaline Phosphatase |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Cells, Cultured |
en |
| dc.subject.other |
Cystatin C |
en |
| dc.subject.other |
Deoxyglucose |
en |
| dc.subject.other |
Dexamethasone |
en |
| dc.subject.other |
Glucose Transporter Type 3 |
en |
| dc.subject.other |
Osteoblasts |
en |
| dc.subject.other |
Rats |
en |
| dc.subject.other |
RNA, Messenger |
en |
| dc.subject.other |
Triiodothyronine |
en |
| dc.title |
Triiodothyronine stimulates cystatin C production in bone cells |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.bbrc.2012.02.040 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
Thyroid hormones increase cystatin C levels in vivo. To study whether 3,3',5-triiodo-l-thyronine (T3) stimulates the production of cystatin C in vitro, we used a T3-responsive osteoblastic cell line (PyMS) which can be kept in serum-free culture. We compared the effects of T3 on cystatin C mRNA expression (by Northern) and on protein release (by Western and ELISA) with those of dexamethasone (dex). Triiodothyronine increased cystatin C mRNA expression and cystatin C accumulation in culture media in a dose- and time-dependent manner, 1.5-fold at 1nmol/l after 4d; dex (100nmol/l) was more potent and increased cystatin C accumulation 3-fold after 4d. Triiodothyronine but not dex stimulated glucose uptake. Our in vitro findings explain in vivo observations. Triiodothyronine-induced increase in the production of cystatin C may be related to an increased cell metabolism and proteolysis control demand. © 2012 Elsevier Inc.. |
en |
| heal.journalName |
Biochemical and Biophysical Research Communications |
en |
| dc.identifier.issue |
2 |
en |
| dc.identifier.volume |
419 |
en |
| dc.identifier.doi |
10.1016/j.bbrc.2012.02.040 |
en |
| dc.identifier.spage |
425 |
en |
| dc.identifier.epage |
430 |
en |