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IHC of SSTR (show SSTR3 Proteins) subtypes in the different cohorts showed SSTR2 (show SSTR2 Proteins) staining intensity scores higher than SSTR5 in TSHoma, acromegaly and prolactinoma, whereas the expression of SSTR5 was stronger than SSTR2 (show SSTR2 Proteins) in corticotropinoma and NFPA.
Somatostatin receptor 5 variant (sst5TMD4) was expressed in a subset of breast cancers, where it correlated with angiogenic markers, lymphatic metastasis, and reduced disease-free survival.
sst5TMD4 is overexpressed in PCa (show FLVCR1 Proteins), especially in those patients with a worse prognosis, and plays an important pathophysiologic role in PCa (show FLVCR1 Proteins), which suggesting its potential as a biomarker and/or therapeutic target
In cotransfected HEK (show EPHA3 Proteins)-293 cells, SSTR5 and CB1R (show CNR1 Proteins) existed in a constitutive heteromeric complex under basal condition, which was disrupted upon agonist treatments. Furthermore, concurrent receptor activation led to preferential formation of SSTR5 homodimer and dissociation of CB1R (show CNR1 Proteins) homodimer.
Combination treatment increased both SSTR2 (show SSTR2 Proteins) and SSTR5 mRNA and protein levels in DU-145 cells. The data suggest that this combination therapy may be a good candidate for patients with advanced metastatic Prostate cancer (PCa (show FLVCR1 Proteins)) do not respond to androgen deprivation.
A truncated splice variant of the somatostatin receptor subtype 5, is associated to features of increased aggressiveness in pancreatic neuroendocrine tumors.
SSTR5 was the predominantly expressed receptor subtype in the cytoplasm of all GH-secreting adenomas tested, regardless of whether they came from octreotide-naive, octreotide-responsive, or octreotide-resistant patients. SSTR5 mRNA predominance was significant only in octreotide treated patients. Its expression was not correlated with baseline or post-octreotide GH or IGF-1 (show IGF1 Proteins) levels or tumor volume.
Data showed that the distribution of somatostatin (show SST Proteins) receptor (SSTR (show SSTR3 Proteins)) subtypes among the 199 pancreatic neuroendocrine tumors (PNETs) was: SSTR2 (show SSTR2 Proteins) (54.8%), SSTR1 (show SSTR1 Proteins) (53.3%), SSTR4 (51.8%), SSTR5 (33.7%), and SSTR3 (show SSTR3 Proteins) (28.6%).
Data indicate that somatostatin (show SST Proteins) receptor scintigraphy (SRS (show SMS Proteins)) and immunohistochemical results for somatostatin (show SST Proteins) and dopamine receptors sstr2 (show SSTR2 Proteins), sstr3 (show SSTR3 Proteins), sstr5 and D2R (show DRD2 Proteins) were compared in neuroendocrine neoplasms tissues.
Somatostatin (show SST Proteins) receptors were expressed in a high proportion of merkel cell carcinomas, although expression was heterogeneous between tumours and was not associated with disease severity.
The expression and localization of the three receptors (SSTR3 (show SSTR3 Proteins)-SSTR5) in wild-type (WT), single-knockout (SSTR1 (show SSTR1 Proteins) KO) and double-knockout SSTR1 (show SSTR1 Proteins)/SSTR2 (show SSTR2 Proteins) (DKO) mice, are reported.
mouse somatostatin receptor 5 is sorted by a network of PDZ-domain containing proteins
Findings suggest that somatostatin (show SST Proteins) and its receptors (SSTR2 (show SSTR2 Proteins) and SSTR5) are important markers in the regulation and development of Sertoli cell.
In comparison to wt, ApoD (show APOD Proteins)(-/-) mice exhibit increased SSTR5-like immunoreactivity in paraventricular nuclei and decreased receptor expression in ventromedial hypothalamus and arcuate nucleus.
Somatostatin (show SST Proteins) inhibited GIP (show GIP Proteins) and glucagon-like peptide-1 (GLP-1 (show GCG Proteins)) secretion from primary small intestinal cultures, in part through SSTR5.
SSTR5 is a negative regulator for PDX-1 (show PDX1 Proteins) expression and SSTR5 may mediate the inhibitory effects of somatostatin (show SST Proteins) and its analogs on insulin (show INS Proteins) expression/secretion and cell proliferation via down-regulating PDX-1 (show PDX1 Proteins)
SST (show SST Proteins) and SSTRs might play an important role in regulation of neurodegeneration
The existence of new truncated sst5-variants with unique ligand-selective signaling properties, which could contribute to further understanding the complex, distinct pathophysiological roles of somatostatin (show SST Proteins) and cortistatin (show CORT Proteins).
Extraovarian somatostatin (show SST Proteins), acting through its receptors 2 and 5 present on granulosa cells, may be involved in mouse folliculogenesis by reducing recruitment of resting follicles.
The effect of sst2 (show SSTR2 Proteins) receptor knockout on sst5 receptor mRNA localization and binding sites throughout the brain has been determined.
This study describes the cloning and characterization of procine sst5 and identifies two spliced variants with six and three transmembrane domains (TMD (show TTN Proteins)): psst5TMD6 and psst5TMD3; psst5TMD6 and psst5TMD3 are functional (e.g., activate calcium signaling.
Data demonstrate that urotensin II (show UTS2 Proteins) and urotensin II-related peptide directly activate somatostatin (show SST Proteins) receptors 2 and 5 and thus mimic the effect of somatostatin (show SST Proteins) on its cognate receptors.
Somatostatin and its related peptide cortistatin exert multiple biological actions on normal and tumoral tissue targets by interacting with somatostatin receptors (SSTRs). The protein encoded by this gene is one of the SSTRs, which is a multi-pass membrane protein and belongs to the G-protein coupled receptor 1 family. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase, and different regions of this receptor molecule are required for the activation of different signaling pathways. A mutation in this gene results in somatostatin analog resistance. Alternatively spliced transcript variants have been identified in this gene.
somatostatin receptor type 5
, somatostatin receptor 5
, somatostatin receptor subtype 5
, Somatostatin receptor subtype 5