Peptide hormone antibodies. Cross reactivity of vasopressin analogues with rabbit antibodies against [8-lysine]vasopressin

1977 ◽  
Vol 42 (12) ◽  
pp. 3510-3517
Author(s):  
J. Slaninovvá ◽  
T. Barth ◽  
I. Krejčí ◽  
I. Rychlík
Keyword(s):  
Peptide Hormone ◽  
Cross Reactivity ◽  
Lysine Vasopressin ◽  
Vasopressin Analogues

Polarographic study of hydrolysis of [8-lysine]vasopressin and its derivatives with blood serum of pregnant women

1980 ◽  
Vol 45 (4) ◽  
pp. 1099-1108 ◽  
Author(s):  
Mikuláš Chavko ◽  
Michal Bartík ◽  
Evžen Kasafírek
Keyword(s):  
Blood Serum ◽  
Pregnant Women ◽  
Degree Of Hydrolysis ◽  
Polarographic Study ◽  
Ph Optimum ◽  
Lysine Vasopressin ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Vasopressin Analogues

A polarographic study of the hydrolysis of [8-lysine]vasopressin and some hormonogens of the vasopressin series with the blood serum of women in the last week of pregnancy was studied. The dependence of hydrolysis on pH (pH optimum: 7.4-7.50, substrate concentration (Km 1.2 . 10-5M), pH stability and thermal stability were determined. The rate of hydrolysis of individual vasopressin analogues decreases in the order: [8-lysine]vasopressin > Nα-glycyl-prolyl[8-lysine]-vasopressin > Nα-leucyl-[8-lysine]vasopressin > Nα-alanyl-[8-lysine]vasopressin > Nα-phenyl alanyl-[8-lysine]vasopressin > Nα-diglycyl-[8-lysine]vasopressin > Nα-prolyl-[8-lysine]vasopressin > Nα-triglycyl-[8-lysine]vasopressin > Nα-sarcosyl-glycyl-[8-lysine]vasopressin. The degree of hydrolysis gradually increases to a multiple with the length of the pregnancy in consequence of the presence of oxytocine. However, vasopressin is also hydrolysed to a small extent with the enzymes from the blood sera of non-pregnant women. Under similar analytical conditions oxytocin was not hydrolysed with the sera of non-pregnant women and therefore oxytocin is a more suitable substrate than vasopressin for polarographic determination of serum oxytocinase.

Corticotropin Releasing Activity of Lysine Vasopressin Analogues

Endocrinology ◽  
1969 ◽  
Vol 84 (3) ◽  
pp. 579-583 ◽  
Author(s):  
A. ARIMURA ◽  
A. V. SCHALLY ◽  
C. Y. BOWERS
Keyword(s):  
Lysine Vasopressin ◽  
Vasopressin Analogues

A specific antibody to vasopressin in a man with concomitant resistance to treatment with Pitressin.

1986 ◽  
Vol 32 (1) ◽  
pp. 211-212 ◽  
Author(s):  
D G Bichet ◽  
C Kortas ◽  
C Manzini ◽  
J N Barjon
Keyword(s):  
Diabetes Insipidus ◽  
Arginine Vasopressin ◽  
Specific Antibody ◽  
Specific Binding ◽  
Cross Reactivity ◽  
Resistance To Treatment ◽  
Allergic Symptoms ◽  
Lysine Vasopressin ◽  
Concomitant Resistance ◽  
Neurogenic Diabetes Insipidus

Abstract A 26-year-old man with complete neurogenic diabetes insipidus since age nine was initially treated with vasopressin (Pitressin Tannate in oil). At age 13, its dosages were progressively increased to control the patient's polyuria; minor allergic symptoms occurred after every such treatment. We incubated serial dilutions of the patient's plasma with 125I-labeled arginine-vasopressin and obtained a 50% specific binding for the plasma at a final dilution of 625-fold. Cross-reactivity studies showed that lysine-vasopressin was better recognized by the antibody than arginine-vasopressin. These results were attributed to large concentrations of lysine-vasopressin (pork vasopressin) in the Pitressin.

RADIOIMMUNOASSAY FOR PLASMA ANTIDIURETIC HORMONE

1972 ◽  
Vol 52 (1) ◽  
pp. 69-78 ◽  
Author(s):  
C. I. JOHNSTON
Keyword(s):  
Antidiuretic Hormone ◽  
Blood Volume ◽  
Plasma Levels ◽  
Extraction Procedure ◽  
Cross Reactivity ◽  
Arterial Blood ◽  
Harvesting Technique ◽  
Lysine Vasopressin ◽  
Simple Extraction ◽  
The Mean

SUMMARY Antibodies to [8-lysine]-vasopressin (LVP) were produced in rabbits by a macrophage harvesting technique. Using these antibodies a radioimmunoassay for vasopressin was established using LVP as standard and for labelling with 125I. The antibody demonstrated complete cross-reactivity to [8-arginine]- and [8-ornithine]-vasopressin but concentrations of oxytocin 1000 times greater caused no displacement. A simple extraction procedure for antidiuretic hormone (ADH) in plasma is described. Employing this extraction procedure followed by radioimmunoassay, plasma levels of ADH were measured in sheep. The mean level of plasma ADH in nine sheep was found to be 5·28 ± 1·18 in arterial blood and this rose to 21·04 ± 7·29 μu./ml after haemorrhage of 10 to 20% of their blood volume.

Synthesis of two lysine-vasopressin analogues with protracted hormonal activity

1963 ◽  
Vol 28 (3) ◽  
pp. 747-749 ◽  
Author(s):  
M. Zaoral ◽  
V. Pliška ◽  
K. Řežábek ◽  
F. Šorm
Keyword(s):  
Hormonal Activity ◽  
Lysine Vasopressin ◽  
Vasopressin Analogues

Preparation of antibodies to [8-D-arginine]deamino-vasopressin and study of their cross-reactivity with vasopressin analogues

1978 ◽  
Vol 43 (4) ◽  
pp. 1167-1174 ◽  
Author(s):  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Jana Škopková ◽  
Ivo Bláha ◽  
František Franěk
Keyword(s):  
Cross Reactivity ◽  
Vasopressin Analogues

Vasopressin receptor-mediated endocytosis: current view

1991 ◽  
Vol 261 (1) ◽  
pp. F1-F13
Author(s):  
W. Lutz ◽  
J. L. Salisbury ◽  
R. Kumar
Keyword(s):  
Peptide Hormone ◽  
Current View ◽  
Target Cells ◽  
Receptor Ligand ◽  
Receptor Mediated Endocytosis ◽  
Vasopressin Receptors ◽  
Vascular Physiology ◽  
Precise Role ◽  
Vasopressin Analogues

A number of peptide hormones have been shown to undergo receptor-mediated endocytosis (RME). RME involves the internalization of receptor-ligand complexes followed by delivery to an intracellular compartment, the endosome, from which ligands or receptors can be delivered to lysosomes or other cellular destinations. Vasopressin, a peptide hormone that plays a role in kidney and vascular physiology, has recently been demonstrated to undergo RME in LLC-PK1 and A10 cells, which express V2- and V1-type vasopressin receptors, respectively. Fluorescent vasopressin analogues are internalized by RME from the basolateral surface of polarized LLC-PK1 cells. The precise role of RME in vasopressin action is uncertain, but it is likely that it is involved in the desensitization of target cells by altering the number of cell surface vasopressin receptors. Alterations in the rate of RME may alter the response of the cell to vasopressin. Fluorescent and biotinylated vasopressins are useful tools for the study of this process.

Tryptic splitting of vasopressin analogues containing homologues of lysine or arginine in position 8

1979 ◽  
Vol 44 (8) ◽  
pp. 2451-2454
Author(s):  
Anastasia Dimeli ◽  
Tomislav Barth
Keyword(s):  
Amino Acid ◽  
Arginine Vasopressin ◽  
Basic Amino Acid ◽  
Peptide Bond ◽  
Peptide Chain ◽  
Side Chain ◽  
Lysine Vasopressin ◽  
Vasopressin Analogues

Vasopressin analogues containing an amino acid with a shorter side chain in position 8 of the peptide chain were more resistant to tryptic splitting of the peptide bond formed by the basic amino acid and terminal glycine amide. In the lysine vasopressin series, analogues with ornithine or lower homologues of lysine in position 8 were not hydrolyzed. In the arginine vasopressin series, the analogue containing 3-guanidino-2-aminopropionic acid in position 8 was completely resistant to the action of trypsin. The vasopressin analogue with norarginine in position 8 was split at a lower rate than natural arginine vasopressin.

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