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ACE

GeneName

ACE

Summary

ACE, also known as angiotensin converting enzyme, AChE, or DCP, is a 150kDa membrane-bound enzyme primarily expressed in the endothelial cells of blood vessels, as well as in various tissues including the heart, kidneys, and brain. It plays a crucial role in the renin-angiotensin system by converting angiotensin I to angiotensin II, a potent vasoconstrictor, thereby regulating blood pressure and fluid balance. ACE is also involved in the metabolism of bradykinin and other peptides, influencing cardiovascular and renal functions. The enzyme is localised to the plasma membrane and extracellular space, and it exhibits various enzymatic activities, including endopeptidase and exopeptidase activities, as well as binding capabilities with ions and proteins.

Importance

ACE is relevant to: - Hypertension and cardiovascular diseases through its role in regulating blood pressure and vascular tone - Kidney function and fluid homeostasis as it influences renal blood flow and sodium balance - Heart failure and remodeling due to its involvement in cardiac function and structure - Neurodegenerative diseases linked to its role in amyloid-beta metabolism and synaptic plasticity - Inflammatory responses and immune regulation through its effects on neutrophil activity and cytokine production

Top Products

For researchers investigating ACE, we highly recommend the top-selling recombinant antibody, Anti-Angiotensin Converting Enzyme 1 antibody [EPR22291-247] (ab254222). This antibody has been validated in knockout models, ensuring its reliability in various applications, including Western blotting (WB), immunohistochemistry (IHC), and ELISA. With 23 citations, it is well-regarded in the research community, making it an excellent choice for those seeking robust and consistent results in their studies of ACE. The Anti-Angiotensin Converting Enzyme 1 antibody ELISA Kit (ab254222), supported by 23 citations, is an excellent option for researchers looking to accurately measure ACE levels in their samples.

Abcam Product Citation Summary

The data indicates that ACE antibodies have been utilised in various experimental contexts, particularly focusing on the effects of miR-34a in mouse models and the role of ACE in the renin–angiotensin system within human kidney tissue. This suggests a significant interest in ACE's involvement in both genetic regulation and age-related renal changes.

Abcam Product Citation Table

Product Code
Species
Application
Study Context
PMID
ab254278
Mouse
WB
Effects of miR-34a
32178735
ab75762
Human
IHC
Renin–angiotensin system and cellular senescence in aging kidneys
31318148

Function

Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubMed:2558109, PubMed:4322742, PubMed:7523412, PubMed:7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:10913258, PubMed:1320019, PubMed:1851160, PubMed:19773553, PubMed:7683654, PubMed:7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:11432860, PubMed:1851160, PubMed:19773553, PubMed:23056909, PubMed:4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:15615692, PubMed:2558109, PubMed:4322742, PubMed:6055465, PubMed:6270633, PubMed:7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed:15615692, PubMed:6208535, PubMed:6270633, PubMed:656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed:2982830, PubMed:6270633, PubMed:656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed:26403559, PubMed:7876104, PubMed:8257427, PubMed:8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed:11604391, PubMed:16154999, PubMed:19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:10336644, PubMed:2983326, PubMed:7683654, PubMed:9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed:10336644, PubMed:19773553, PubMed:7876104).

Angiotensin-converting enzyme, soluble form

Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.

Isoform Testis-specific

Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (PubMed:1651327, PubMed:1668266). In contrast to somatic isoforms, only contains one catalytic domain (PubMed:1651327, PubMed:1668266). Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed:1668266, PubMed:24297181). The identity of substrates that are needed for male fertility is unknown (By similarity). May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity). This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (By similarity).

Involvement in disease

Ischemic stroke

ISCHSTR

A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.

None

Disease susceptibility is associated with variants affecting the gene represented in this entry.

Renal tubular dysgenesis

RTD

Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).

None

The disease is caused by variants affecting the gene represented in this entry.

Microvascular complications of diabetes 3

MVCD3

Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.

None

Disease susceptibility is associated with variants affecting the gene represented in this entry.

Intracerebral hemorrhage

ICH

A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.

None

Disease susceptibility is associated with variants affecting the gene represented in this entry.

Post-translational modifications

Angiotensin-converting enzyme, soluble form

Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). Cleavage can take place at different sites of the juxtamembrane stalk region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769).

Phosphorylated by CK2 on Ser-1299; which allows membrane retention (PubMed:12386153). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (By similarity).

Sequence Similarities

Belongs to the peptidase M2 family.

Tissue Specificity

Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate.

Isoform Testis-specific

Specifically expressed in spermatocytes and adult testis.

Cellular localization

Alternative names

CD143, DCP, DCP1, ACE, Angiotensin-converting enzyme, Dipeptidyl carboxypeptidase I, Kininase II

swissprot:P12821 entrezGene:1636 omim:106180

Other research areas