|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for AVP(NM_000490.5) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a precursor protein consisting of arginine vasopressin and two associated proteins, neurophysin II and a glycopeptide, copeptin. Arginine vasopressin is a posterior pituitary hormone which is synthesized in the supraoptic nucleus and paraventricular nucleus of the hypothalamus. Along with its carrier protein, neurophysin II, it is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis where it is either stored or secreted into the bloodstream. The precursor is thought to be activated while it is being transported along the axon to the posterior pituitary.
Gene References into function
- autosomal dominant neurohypophyseal diabetes insipidus associated with a novel and recurrent mutations in the vasopressin-neurophysin II gene.
- identification of a missense mutation of the AVP-NPII gene and a novel mutation predicting a truncated protein in the gene in familial central diabetes insipidus
- Autosomal dominant neurohypophyseal diabetes insipidus due to substitution of histidine for tyrosine(2) in the vasopressin moiety of the hormone precursor.
- novel mutation substituting cysteine with phenylalanine in one AVP-NPII gene allele in autosomal dominant neurohypophyseal diabetes insipidus
- AVP responses to hypotension in adipsic diabetes insipidus are heterogeneous and reflect the site of the lesion causing the diabetes insipidus
- demonstrated a novel mechanism for upstream stimulatory factor activation, which contributes to differential vasopressin expression in lung cancer.
- Non-suppressible release of AVP is crucially involved in the impaired water excretion and hyponatremia seen in elderly patients with secondary adrenal insufficiency.
- As a result of this mutation cysteine residue is exchanged, which is involved in disulfide bond with cysteine 44 of NPII moiety. Resulting misfolded protein may lead to chronic neurotoxicity by accumulation of these products in endoplasmatic reticulum.
- wild-type vasopressin precursor and pathogenic mutants are degraded by the proteasome
- Plasma arginine vasopressin (AVP) was determined before the stressor, at the time of maximum ACTH secretion, and 75 min after stress onset. Activation of the HPA system by psychosocial stress is accompanied by an increase in peripheral plasma AVP levels.
- In the present study we found decreased vasopressin in several hypothalamic nuclei in vascular dementia indicating diminished production of certain hormones and neurotransmitters.
- molecular dynamics analysis of mechanism of desmopressin binding in vasopressin V2 receptor versus vasopressin V1a and oxytocin receptors
- These results suggest that the elevation of plasma vasopressin in the acute phase of Meniere's disease is related to the pathogenesis of Meniere's attacks.
- Data show AVP was significantly increased in multiple trauma patients and seems to be an integral part of the neuroendocrine response to severe injury. In ICU patients, AVP decreased to moderately elevated levels within 24 h after ED admission.
- Study suggests that symptomatic intradialytic hypotension patients are unable to mount an appropriate increase in AVP secretion in the setting of hypotension.
- there is a relationship between plasma osmolality, plasma apelin and plasma AVP in various states of hydration
- Presence of this mutation suggests that the portion of the neurophysin peptide encoded by this sequence is important for the appropriate expression of vasopressin.
- Data demonstrate need for autophagy-mediated degradation of toxic, mutated arginine vasopressin C98X peptides, and suggest that, in the presence of mis-folded proteins, the stimulation of Akt signalling counteracts autophagy and precipitates cell death.
- This article reviews mutations of the arginine vasopressin neurophysin-II gene in familial neurohypophyseal diabetes insipidus patients.