Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is considered that the physiology of the human fallopian tube may be dependent on endocrine factors, especially their changes during the menstrual cycle in the fractionated fallopian tissues. In the present study, the dynamics of sex steroids (estradiol, E and progesterone, P), prostaglandins (PGs) and oxytocin (OT) binding to each receptor (R) in the ampullary and isthmic regions were analyzed simultaneously throughout the menstrual cycle. The number of binding sites (NBS) for nuclear ER (ERN) levels was always greater in the ampulla than in the isthmus, while that for nuclear PR (PRN) was almost the same. The NBS of both E-, and PRN reached the highest levels during the late proliferative to ovulatory phase. The NBS of both PGE2-, and PGF2 alpha-R in the isthmus was greater than that in the ampulla and highest during the secretory phase. Conversely, the tissue concentration of 6-keto-PGF1 alpha in the ampulla changed to that in the isthmus around the ovulatory phase. The OT-R showed the highest levels during the secretory phase in the isthmus, but showed little change in the ampulla throughout the menstrual cycle. It increased markedly in the isthmus but decreased in the ampulla. The present data suggest that the receptor concentrations in the human fallopian tube fluctuate in correlation with its physiological and histological status. It may, therefore, be concluded that the hormone-receptor interaction in this anatomical unit is closely involved in the reproductive functions of the human fallopian tube.
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PMID:[Cyclic changes in sex steroids, prostaglandins and oxytocin receptors of normal fallopian tube throughout the menstrual cycle]. 284 28

Oxytocin (OT) and its receptor (OT-R) are implicated in the etiology of autism spectrum disorders (ASD), and OT-R is a potential target for therapeutic intervention. Very few nonpeptide oxytocin agonists have currently been reported. Their molecular and in vivo pharmacology remain to be clarified, and none of them has been shown to be efficient in improving social interaction in animal models relevant to ASD. In an attempt to rationalize the design of centrally active nonpeptide full agonists, we studied in a systematic way the structural determinants of the affinity and efficacy of representative ligands of the V1a and V2 vasopressin receptor subtypes (V1a-R and V2-R) and of the oxytocin receptor. Our results confirm the subtlety of the structure-affinity and structure-efficacy relationships around vasopressin/oxytocin receptor ligands and lead however to the first nonpeptide OT receptor agonist active in a mouse model of ASD after peripheral ip administration.
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PMID:LIT-001, the First Nonpeptide Oxytocin Receptor Agonist that Improves Social Interaction in a Mouse Model of Autism. 3019 37