Human proBNP peptide

Specifications

Form

Lyophilized

General info

Function

Brain natriuretic peptide 32. Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed : 1672777, PubMed : 17372040, PubMed : 1914098, PubMed : 9458824). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses (PubMed : 1672777, PubMed : 17349887, PubMed : 17372040, PubMed : 21098034, PubMed : 25339504, PubMed : 9458824). Involved in regulating the extracellular fluid volume and maintaining the fluid-electrolyte balance through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion (PubMed : 1914098, PubMed : 9458824). Binds the clearance receptor NPR3 (PubMed : 16870210).. NT-proBNP. May affect cardio-renal homeostasis (PubMed : 17372040). Able to promote the production of cGMP although its potency is very low compared to brain natriuretic peptide 32 (PubMed : 17372040).. BNP(3-32). May have a role in cardio-renal homeostasis (PubMed : 17372040). Able to promote the production of cGMP (PubMed : 17372040).

Sequence similarities

Belongs to the natriuretic peptide family.

Post-translational modifications

The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-102 to produce brain natriuretic peptide 32 and NT-proBNP (PubMed:10880574, PubMed:20489134, PubMed:21314817, PubMed:21482747, PubMed:21763278). This likely occurs after it has been secreted into the blood, either during circulation or in the target cells (PubMed:21482747). CORIN also cleaves the precursor molecule at additional residues including Arg-99 and possibly Lys-105 (PubMed:20489134, PubMed:21763278). In patients with heart failure, processing and degradation of natriuretic peptides B occurs but is delayed, possibly due to a decrease in enzyme level or activity of CORIN and DPP4 (PubMed:25339504).. Brain natriuretic peptide 32. Undergoes further proteolytic cleavage by various proteases such as DPP4, MME and possibly FAP, to give rise to a variety of shorter peptides (PubMed:16254193, PubMed:19808300, PubMed:21098034, PubMed:21314817). Cleaved at Pro-104 by the prolyl endopeptidase FAP (seprase) activity (in vitro) (PubMed:21314817). Degraded by IDE (PubMed:21098034). During IDE degradation, the resulting products initially increase the activation of NPR1 and can also stimulate NPR2 to produce cGMP before the fragments are completely degraded and inactivated by IDE (in vitro) (PubMed:21098034).. O-glycosylated on at least seven residues (PubMed:16750161, PubMed:17349887, PubMed:20489134, PubMed:21482747, PubMed:21763278). In cardiomyocytes, glycosylation at Thr-97 is essential for the stability and processing of the extracellular natriuretic peptides B (PubMed:21482747). Glycosylation, especially at Thr-97, may also be important for brain natriuretic peptide 32 stability and/or extracellular distribution (PubMed:21763278). Glycosylation at Thr-97 appears to inhibit FURIN- or CORIN-mediated proteolytic processing, at least in HEK293 cells (PubMed:20489134, PubMed:21763278).