-
CD36 is a major mediator of FA-induced release of CCK and secretin. These peptides contribute to the role of CD36 in fat absorption and to its pleiotropic metabolic effects.
-
Data suggest that the interaction between secretin peptide residue H1 and secretin receptor residue W274 is most compatible with a hydrophobic interaction.
-
a lineage of mature enteroendocrine cells have the ability to coexpress members of a group of functionally related peptides: CCK, secretin, GIP, GLP-1, PYY, and neurotensin
-
Secretin effect on increase in transcription of the tyrosine hydroxylase (Th) gene and modulate catecholamine secretion, was tested.
-
binding and activity of a series of 11 truncated and lactam-constrained secretin(5-27) analogues at the prototypic member of this family, the secretin receptor
-
secretin significantly inhibited the tumor size and more than doubled tumor latency, which was associated with a decrease in proliferating cell nuclear antigen and an increase in cleaved-caspase 3 expression levels
-
The purpose of this study was to investigate whether secretin exhibits similar properties in vitro by forming micelles in aqueous solution and interacting with phospholipids
-
Human VPAC1 receptor selectivity filter; Identification of a critical domain for restricting binding
-
fine structure in 11p15.5 and sequence variation in patients with autism
-
human secretin gene is controlled by the Sp1/Sp3 transcription factors ratio and the methylation status of the promoter
-
Transgenic mouse study suggests a trophic role for secretin on neurons known to be involved in multiple superior functions in the normal brain, and lost in neurodegenerative disorders.
-
Secretin mRNAs are found in Purkinje cells and secretin-immunoreactivities are localized in both the soma and dendrites of Purkinje cells of human cerebellum.
-
small heterodimer partner and secretin are potentially co-expressed and lead us to propose a novel regulatory pathway
-
first pathway is by changing the expression levels of nuclear factor-I C(NFI-C) and secretin proteins while the second pathway is by modifying the phosphorylation status of both NFI-C and secretin proteins via cyclin-dependent kinase 1
-
Peptic ulceration may be a hormonal (secfretin) deficiency disease.
-
These results collectively suggest that variable of tandem repeats could potentially be a functional regulator to control the expression of the human secretin gene in different individuals.
-
secretin acts through stimulation of presynaptic cholinergic neurons in a vagally mediated pathway.
-
Bile acids inhibit duodenal secretin expression via orphan nuclear receptor small heterodimer partner (SHP).