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Query: UNIPROT:P61278 (
somatostatin
)
22,083
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Using a functioning rat thyroid cell line (FRTL-5), we examined the effects of some cytokines, particularly interleukin-1 (IL-1) on the growth of thyroid cells. In 5H medium, namely Coon's modified Ham's F-12 medium supplemented with 5% calf serum and a five-hormone preparation consisting of insulin, hydrocortisone, transferrin, glycyl-L-histidyl-L-lysine acetate and
somatostatin
, IL-1 enhanced the growth of FRTL-5 cells detected by [3H]TdR incorporation. However, in 6H medium (5H medium plus bovine TSH), IL-1 inhibited the growth of FRTL-5 cells. Both effects were neutralized by the addition of anti-IL-1 antibody. Furthermore, IL-1 inhibited the growth of FRTL-5 cells induced by forskolin which is known as an adenylate cyclase activator. FRTL-5 cells have specific IL-1 receptors detected by the binding of 125I-labeled IL-1 alpha. By Scatchard plot analysis, the numbers and the dissociation constants of IL-1 receptors on FRTL-5 cells were shown to be 5225/cell and 8.69 x 10(-10) M.
Interleukin-2
, interleukin-6 and interferon-gamma (IFN-gamma) had no significant effects on the cell growth in 6H medium, while IFN-gamma and insulin-like growth factor I stimulated cell growth somewhat in 5H medium. These results suggest that IL-1 plays a regulatory role in the growth of thyroid cells through binding to the IL-1 receptors.
...
PMID:Inhibitory effect of IL-1 on the TSH dependent growth of rat thyroid cells (FRTL-5). 212 71
Interleukin-2
(
IL-2
), which plays a major role in the bidirectional intercellular communication between the neuroendocrine and immune systems, suppressed the release of GH from anterior pituitary halves at femtomolar concentrations. It is well established that the release of GH from the anterior pituitary is regulated by growth hormone releasing hormone (GRH) and growth hormone release-inhibiting hormone (
somatostatin
). Consequently, we studied the possible effect of
IL-2
on the release of
somatostatin
and GRH from the mediobasal hypothalamus (MBH) in vitro. Single MBHs were incubated with fresh Krebs-Ringer bicarbonate (KRB) buffer alone or KRB containing different concentrations of
IL-2
(10(-15)-10(-10) M) for 30 min. After collection of the media, the MBHs were incubated with KRB containing high potassium (high K+ = 56 mM) without
IL-2
for a period of 30 min to study the effect of pretreatment with
IL-2
on depolarization-induced
somatostatin
and GRH release. Experiments were also undertaken to study the effect of
IL-2
in the presence of high K+ or
IL-2
in the presence of DA (60 microM), a potent stimulator of
somatostatin
and GRH release. The minimal effective dose of
IL-2
which significantly stimulated the release of
somatostatin
was 10(-14) M. Depolarization-induced release of
somatostatin
was reduced significantly by prior treatment with all the concentrations of
IL-2
tested (10(-13)-10(-10) M).(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:The influence of interleukin-2 on the release of somatostatin and growth hormone-releasing hormone by mediobasal hypothalamus. 790 32
The targeting of tumor cells by peptides for drug delivery is a promising strategy for cancer therapy.
Interleukin-2
(
IL-2
), which mediates anti-tumor cellular immune responses, has been approved as a therapy for cancer. However, the serious side effects and short half-life of recombinant
IL-2
(rIL-2) has limited its use clinically.
Somatostatin
receptors (SSTRs), which are expressed in a large number of human tumors, are the targets for in vivo tumor targeting. In this study, we have constructed and expressed a novel chimeric recombinant protein containing octreotide analogs and
IL-2
in order to target the SSTR binding with tumor cells. The fusion protein somatostatin receptor targeted interleukin-2 (SIL), which was purified from bacterial inclusion bodies and refolded with high purity, was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. Tryptophan emission fluorescence was used to measure the structural changes in SIL after renaturation. Cell proliferation experiments showed that this chimeric protein retained the biological activities of hIL-2. Furthermore, the tumor binding capacity of SIL acting through SSTRs was shown through co-immunoprecipitation. Competition binding with octreotide of tumor cells also confirmed that SIL binds to tumor cells through the target peptide octreotide. Moreover, the performance of SIL in stimulating the proliferation of lymphocyte cell lines after binding to tumor cells showed that the immunocytokine, SIL, retained its bioactivity at the tumor site. These results suggest that SIL is a recombinant fusion protein that may be used for tumor-targeted drug delivery.
...
PMID:Expression, purification, refolding, and characterization of octreotide-interleukin-2: a chimeric tumor-targeting protein. 2168 29
