Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system

Autor: Daniel W. Lambert, Nigel M. Hooper, Anthony J. Turner
Rok vydání: 2007
Předmět:
Lung Diseases
Metallopeptidase
CoV
coronavirus

ACE2
Biochemistry
TNF
tumour necrosis factor

Renin-Angiotensin System
Angiotensin
AT1
angiotensin receptor
type 1

Receptor
ADAM
a disintegrin and metalloproteinase

biology
Liver Diseases
MDCK
Madin–Darby Canine Kidney

Diabetes
Cardiovascular Diseases
Angiotensin-converting enzyme 2
Ang
angiotensin

Kidney Diseases
Angiotensin-Converting Enzyme 2
HNF
hepatocyte nuclear factor

MODY
maturity-onset diabetes mellitus

hormones
hormone substitutes
and hormone antagonists

medicine.medical_specialty
ACE
angiotensin-converting enzyme

Peptidyl-Dipeptidase A
Article
HEK
human embryonic kidney

Internal medicine
RAS
renin–angiotensin system

Renin–angiotensin system
medicine
Animals
Humans
SARS
severe acute respiratory syndrome

ARDS
acute respiratory distress syndrome

ACE
Pharmacology
mas
receptor for Ang (1-7)

SARS
Angiotensin II receptor type 1
business.industry
Angiotensin-converting enzyme
Carboxypeptidase
Angiotensin II
TACE
TNF-α converting enzyme

Endocrinology
biology.protein
ARDS
business
Zdroj: Biochemical Pharmacology
ISSN: 1873-2968
Popis: Components of the renin-angiotensin system are well established targets for pharmacological intervention in a variety of disorders. Many such therapies abrogate the effects of the hypertensive and mitogenic peptide, angiotensin II, by antagonising its interaction with its receptor, or by inhibiting its formative enzyme, angiotensin-converting enzyme (ACE). At the turn of the millennium, a homologous enzyme, termed ACE2, was identified which increasingly shares the limelight with its better-known homologue. In common with ACE, ACE2 is a type I transmembrane metallopeptidase; however, unlike ACE, ACE2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates. One such substrate is angiotensin II, which is hydrolysed by ACE2 to the vasodilatory peptide angiotensin 1-7. In this commentary we discuss the latest developments in the rapidly progressing study of the physiological and patho-physiological roles of ACE2 allied with an overview of the current understanding of its molecular and cell biology. We also discuss parallel developments in the study of collectrin, a catalytically inactive homologue of ACE2 with critical functions in the pancreas and kidney.
Databáze: OpenAIRE