NPPB
GeneName
NPPB
Summary
NPPB, also known as BNP or proBNP, is a 15 kDa peptide hormone predominantly expressed in the heart, particularly in the ventricles. It is secreted into the extracellular space and plays a vital role in the regulation of blood pressure and fluid balance. NPPB functions as a diuretic hormone, promoting natriuresis and diuresis, and is involved in several biological processes including blood vessel diameter maintenance and vasodilation. It exerts its effects through binding to specific receptors, activating guanylyl cyclase and stimulating cGMP-mediated signalling pathways, which contribute to its regulatory roles in the cardiovascular system.
Importance
NPPB is relevant to: - Heart failure diagnostics, as elevated levels of BNP are indicative of cardiac stress and are used as a biomarker in clinical settings - Understanding fluid homeostasis and blood pressure regulation, providing insights into conditions like hypertension - Research into cardiac physiology and pathophysiology, particularly in the context of cardiac remodeling and vascular health - Potential therapeutic targets in cardiovascular diseases, given its role in regulating vascular permeability and angiogenesis
Top Products
For researchers investigating NPPB, we recommend two excellent primary antibodies. The first is the well-cited polyclonal antibody, Anti-BNP antibody (ab19645), which has garnered 44 citations, reflecting its reliability in Western blotting (WB). This antibody is a trusted choice for those looking to study NPPB in detail. Additionally, we offer the recombinant antibody, Anti-BNP antibody [EPR3736] (ab174856), which is also validated for WB. This recombinant option provides the advantage of batch-to-batch consistency, making it an ideal choice for researchers who require dependable results in their experiments. The Human proBNP peptide ELISA Kit (ab42238) is an excellent option for researchers looking to measure NPPB levels in their samples.
Abcam Product Citation Summary
The data indicates that the NPPB antibody (ab19645) has been effectively used in various studies focusing on cardiac health and function in both rat and mouse models. The applications of western blotting and immunohistochemistry highlight its utility in examining the effects of sodium intake, exercise training, cardiac hypertrophy, and aging in heart tissues.
Abcam Product Citation Table
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).
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).
Sequence Similarities
Belongs to the natriuretic peptide family.
Tissue Specificity
Brain natriuretic peptide 32
Detected in the cardiac atria (at protein level) (PubMed:2136732, PubMed:2138890). Detected in the kidney distal tubular cells (at protein level) (PubMed:9794555).
Cellular localization
- NT-proBNP
- Secreted
- Detected in blood.
- proBNP(3-108)
- Secreted
- Detected in blood.
- Brain natriuretic peptide 32
- Secreted
- Detected in blood.
- BNP(3-32)
- Secreted
- Detected in blood.
Alternative names
Natriuretic peptides B, Brain natriuretic factor prohormone, Gamma-brain natriuretic peptide, Iso-ANP, preproBNP, proBNP, NPPB