BIOMAT Database Logo BIOMAT Database Logo

Khusimol, a non-peptide ligand for vasopressin V1a receptors. 1994

R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Sanofi Recherche, Toulouse, France.

In the course of a random screen of various plant extracts, khusimol [1], a non-peptide molecule isolated from the root of Vetiveria zizanioides, was found to competitively inhibit the binding of vasopressin to rat liver V1a receptors (Ki = 50 microM). The 1H- and 13C-nmr spectra of this sesquiterpene alcohol were assigned unambiguously.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D000081223 Polycyclic Sesquiterpenes Sesquiterpenes that contain two or more ring structures Caryophyllane,Caryophyllane Derivative,Caryophyllane Derivatives,Caryophyllanes,Eremophilane,Eremophilane Derivative,Eremophilane Derivatives,Eremophilanes,Polycyclic Sesquiterpene,Valerane,Valerane Derivative,Valerane Derivatives,Valeranes,Derivative, Caryophyllane,Derivative, Eremophilane,Derivative, Valerane,Derivatives, Caryophyllane,Derivatives, Eremophilane,Derivatives, Valerane,Sesquiterpene, Polycyclic,Sesquiterpenes, Polycyclic
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001127 Arginine Vasopressin The predominant form of mammalian antidiuretic hormone. It is a nonapeptide containing an ARGININE at residue 8 and two disulfide-linked cysteines at residues of 1 and 6. Arg-vasopressin is used to treat DIABETES INSIPIDUS or to improve vasomotor tone and BLOOD PRESSURE. Argipressin,Vasopressin, Arginine,Arg-Vasopressin,Argipressin Tannate,Arg Vasopressin
D012717 Sesquiterpenes Fifteen-carbon compounds formed from three isoprenoid units with general formula C15H24. Farnesanes,Farnesene,Farnesenes,Sesquiterpene,Sesquiterpene Derivatives,Sesquiterpenoid,Sesquiterpenoids,Derivatives, Sesquiterpene
D017483 Receptors, Vasopressin Specific molecular sites or proteins on or in cells to which VASOPRESSINS bind or interact in order to modify the function of the cells. Two types of vasopressin receptor exist, the V1 receptor in the vascular smooth muscle and the V2 receptor in the kidneys. The V1 receptor can be subdivided into V1a and V1b (formerly V3) receptors. Antidiuretic Hormone Receptors,Receptors, V1,Receptors, V2,V1 Receptors,V2 Receptors,Vasopressin Receptors,8-Arg-Vasopressin Receptor,Antidiuretic Hormone Receptor,Antidiuretic Hormone Receptor 1a,Antidiuretic Hormone Receptor 1b,Arginine Vasopressin Receptor,Argipressin Receptor,Argipressin Receptors,Receptor, Arginine(8)-Vasopressin,Renal-Type Arginine Vasopressin Receptor,V1 Receptor,V1a Vasopressin Receptor,V1b Vasopressin Receptor,V2 Receptor,Vascular-Hepatic Type Arginine Vasopressin Receptor,Vasopressin Receptor,Vasopressin Receptor 1,Vasopressin Type 1A Receptor,Vasopressin V1a Receptor,Vasopressin V1b Receptor,Vasopressin V2 Receptor,Vasopressin V3 Receptor,8 Arg Vasopressin Receptor,Hormone Receptor, Antidiuretic,Hormone Receptors, Antidiuretic,Receptor, Antidiuretic Hormone,Receptor, Arginine Vasopressin,Receptor, Argipressin,Receptor, V1,Receptor, V2,Receptor, Vasopressin,Receptor, Vasopressin V1b,Receptor, Vasopressin V3,Receptors, Antidiuretic Hormone,Receptors, Argipressin,Renal Type Arginine Vasopressin Receptor,V1b Receptor, Vasopressin,Vascular Hepatic Type Arginine Vasopressin Receptor,Vasopressin Receptor, V1b
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
A selective biotinylated probe for V1a vasopressin receptors.
May 1991, Molecular and cellular endocrinology,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
A radioiodinated linear vasopressin antagonist: a ligand with high affinity and specificity for V1a receptors.
April 1991, FEBS letters,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Effects of SR 49059, a non-peptide antagonist of vasopressin V1a receptors, on vasopressin-induced coronary vasoconstriction in conscious rabbits.
January 1995, Fundamental & clinical pharmacology,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Molecular pharmacology of V1a vasopressin receptors.
October 1995, General pharmacology,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Are there sex differences in oxytocin and vasopressin V1a receptors ligand binding affinities?
April 2024, Pharmacological reports : PR,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Upregulation of V1a vasopressin receptors by glucocorticoids.
December 1992, The American journal of physiology,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Mapping peptide antagonist binding sites of the human V1a and V2 vasopressin receptors.
January 1998, Advances in experimental medicine and biology,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Development of a radioligand for imaging V1a vasopressin receptors with PET.
October 2017, European journal of medicinal chemistry,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Molecular modeling of interactions of the non-peptide antagonist YM087 with the human vasopressin V1a, V2 receptors and with oxytocin receptors.
December 2001, Journal of computer-aided molecular design,
R C Rao, and C Serradeil-Le Gal, and I Granger, and J Gleye, and J M Augereau, and C Bessibes
Intramedullary blood vessels of the spinal cord express V1a vasopressin receptors: visualization by a biotinylated ligand.
December 1995, Neuroendocrinology,
Copied contents to your clipboard!