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Angiotensin-converting enzyme

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Title: Angiotensin-converting enzyme  
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Angiotensin-converting enzyme

Angiotensin-converting enzyme
Identifiers
EC number 3.4.15.1
CAS number 9015-82-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Angiotensin I converting enzyme
Rendering of ACE from PDB
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; ACE1; CD143; DCP; DCP1; ICH; MVCD3
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure.

ACE is also known by the following names: dipeptidyl carboxypeptidase I, peptidase P, dipeptide hydrolase, peptidyl dipeptidase, angiotensin converting enzyme, kininase II, angiotensin I-converting enzyme, carboxycathepsin, dipeptidyl carboxypeptidase, "hypertensin converting enzyme" peptidyl dipeptidase I, peptidyl-dipeptide hydrolase, peptidyldipeptide hydrolase, endothelial cell peptidyl dipeptidase, peptidyl dipeptidase-4, PDH, peptidyl dipeptide hydrolase, and DCP.

ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels.[1]

Contents

  • Functions 1
  • Genetics and C and N domains function 2
  • Pathology 3
  • Influence on athletic performance 4
  • See also 5
  • References 6
  • Further reading 7
  • External links 8

Functions

Schematic diagram of the renin–angiotensin–aldosterone system
Anatomical diagram of the renin-angiotensin system, showing the role of ACE at the lungs.[2]

It has two primary functions:

These two actions make ACE inhibition a goal in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy, and type 2 diabetes mellitus. Inhibition of ACE (by ACE inhibitors) results in the decreased formation of angiotensin II and decreased metabolism of bradykinin, leading to systematic dilation of the arteries and veins and a decrease in arterial blood pressure. In addition, inhibiting angiotensin II formation diminishes angiotensin II-mediated aldosterone secretion from the adrenal cortex, leading to a decrease in water and sodium reabsorption and a reduction in extracellular volume.[5]

Genetics and C and N domains function

The ACE gene, ACE, encodes two isozymes. The somatic isozyme is expressed in many tissues, mainly in the lung, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm. Brain tissue has ACE enzyme, which takes part in local RAAS and converts Aβ42 (which aggregates into plaques) to Aβ40 (which is thought to be less toxic) forms of beta amyloid. The latter is predominantly a function of N domain portion on the ACE enzyme. ACE inhibitors that cross the blood–brain barrier and have preferentially select N terminal activity may, therefore, cause accumulation of Aβ42 and progression of dementia.

Pathology

Influence on athletic performance

  • ACE gene is a I/D polymorphism leading to the presence(I) or absence (D) the carriers of the ACE insertion allele of an alu repeat in intron 16 of the gene.[6] With the insertion, observed higher maximum oxygen uptake (VO2max), increase in training, and increased muscle when paired with individuals carrying the deletion allele.
  • Individuals with the insertion are associated with long distance and endurance events. This is seen in studies that suggest that it is due to lower levels of angiotensin II. The deletion of the Alu increases angiotensin II that in turn increases the vasoconstriction of blood vessels. This is observed in short distance events and seen mostly in swimmers.[7]

See also

References

  1. ^
  2. ^ Page 866-867 (Integration of Salt and Water Balance) and 1059 (The Adrenal Gland) in:
  3. ^
  4. ^
  5. ^
  6. ^
  7. ^

Further reading

External links

  • Proteopedia Angiotensin-converting_enzyme - the Angiotensin-Converting Enzyme Structure in Interactive 3D
  • Angiotensin Converting Enzyme at the US National Library of Medicine Medical Subject Headings (MeSH)
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