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Desmopressin (1-deamino-8-D-arginine vasopressin) is a synthetic form of the normal human hormone arginine vasopressin (the antidiuretic hormone, or ADH), a peptide containing nine amino acids. Compared to vasopressin, desmopressin's first amino acid has been deaminated , and the arginine at the eighth position is in the dextro rather than the ...
An antidiuretic is a substance that helps to control fluid balance in an animal's body by reducing urination, [1] opposing diuresis. [2] Its effects are opposite that of a diuretic.
Vasopressin analogues are synthetic peptides structurally and functionally similar to arginine vasopressin (AVP), a naturally occurring hormone in mammals. These compounds have been developed to target specific vasopressin receptors (V1, V2, and V3) with varying affinities, allowing for more tailored therapeutic applications.
551 11998 Ensembl ENSG00000101200 ENSMUSG00000037727 UniProt P01185 P35455 RefSeq (mRNA) NM_000490 NM_009732 RefSeq (protein) NP_000481 NP_033862 Location (UCSC) Chr 20: 3.08 – 3.08 Mb Chr 2: 130.42 – 130.42 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Human vasopressin, also called antidiuretic hormone (ADH), arginine vasopressin (AVP) or argipressin, is a hormone synthesized ...
While taking desmopressin, a person should drink fluids or water only when thirsty and not at other times, as this can lead to sudden fluid accumulation in the central nervous system. If desmopressin reduces urine output and increases urine osmolarity, the hypothalamic production of ADH is deficient, and the kidney responds normally to ...
Vasopressin agonists are used therapeutically in various conditions, and its long-acting synthetic analogue desmopressin is used in conditions featuring low vasopressin secretion, as well as for control of bleeding (in some forms of von Willebrand disease and in mild haemophilia A) and in extreme cases of bedwetting by children.
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V 2 receptor (V 2 R) differs from V 1 R primarily in the number of sites susceptible to N-linked glycosylation; the V 1 R has sites at both the amino-terminus and at the extracellular loop, whereas the V 2 R has a single site at the extracellular amino-terminus.
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