anti-Guanylate Cyclase Activator 2B (Uroguanylin) (GUCA2B) Antibodies

Mouse (Murine) Guanylate Cyclase Activator 2B (Uroguanylin) (GUCA2B) interaction partners

1. Guanylin and uroguanylin, as well as their prohormones, do not seem to play a significant role in body weight regulation and glycemic control, suggesting that guanylin-family peptides do not show promise as targets for the treatment of obesity or diabetes.

2. guanylin and uroguanylin are produced by mouse intestinal epithelial cells of columnar and secretory lineage

3. In obese mice UGN expression was decreased, whereas leptin treatment up-regulated UGN levels in duodenum in these genetically modified mice compared to WT.

4. UGN exerts its inhibitory activity on the prendrin gene promoter likely via heat shock factor 1 action at a defined heat shock element site.

5. findings establish a role for uroguanylin in an enteric-renal communication axis as well as a fundamental principle of this axis in the maintenance of salt homeostasis in vivo

6. act on the mouse kidney, in part, through a cGMP-dependent, GC-C-independent mechanism, causing significant natriuresis by renal tubular processes.

7. existence of two signaling pathways for guanylin peptides in principal cells of mouse cortical collecting duct of kidney

8. Role for uroguanylin in fluid homeostasis and as an integral component of a signaling mechanism that mediates changes in Na excretion in response to an enteral salt loading.

Human Guanylate Cyclase Activator 2B (Uroguanylin) (GUCA2B) interaction partners

1. The intestinal expression of uroguanylin, a key satiety hormone, appears to be diminished in female pediatric patients in the setting of obesity.

2. In female adolescents without obesity, levels of pro-uroguanylin are higher than in those with obesity. Pro-uroguanylin secretion patterns differ from other circulating gastrointestinal peptides. In female adolescents with obesity, inflammation correlates with decreased pro-uroguanylin levels.

3. Guanylin and uroguanylin, as well as their prohormones, do not seem to play a significant role in body weight regulation and glycemic control, suggesting that guanylin-family peptides do not show promise as targets for the treatment of obesity or diabetes.

4. Both guanylin and uroguanylin trigger lipolysis in human visceral adipocytes. Given the lipolytic action of the guanylin system on visceral adipocytes, the herein reported decrease of circulating prouroguanylin concentrations in obese patients may have a role in excessive fat accumulation in obesity.

5. Results demonstrate that GC-C and its ligands, guanylin and uroguanylin are downregulated in ulcerative colitis (UC), and this downregulation is more significant with aggravation of the clinical condition. Therefore, the GC-C signaling pathway may be implicated in the progression of UC.

6. The simulations suggested that all missense SNPs considered as convergent deleterious caused some kind of structural change to the uroguanylin peptide. Additionally, four of these SNPs were also shown to cause modifications in peptide flexibility, possibly resulting in functional changes.

7. The specific cellular distribution of both GN and UGN differs between duodenum and colon and between human and rat intestines.

8. Uroguanylin concentrations are increased in patients with chronic renal failure, nephrotic syndrome, or those on dialysis.

9. The occurrences of the C-A haplotype (rs883062-rs1047047) and the C-A-G haplotype (rs883062-rs1047047-rs2297566) were significantly higher in the essential hypertension group than in the controls.