About: B38-CAP is a bacteria-derived ACE2-like enzyme that suppresses hypertension and cardiac dysfunction

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About: B38-CAP is a bacteria-derived ACE2-like enzyme that suppresses hypertension and cardiac dysfunction Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	B38-CAP is a bacteria-derived ACE2-like enzyme that suppresses hypertension and cardiac dysfunction
Creator	Imai, Yumiko Kuba, Keiji Sato, Teruki Watanabe, Hiroyuki Gotoh, Takeshi Hoshizaki, Midori Inagaki, Tadakatsu Koyota, Souichi Minato, Takafumi Motoyama, Satoru Nakahara, Kazuhiko Nakaoka, Yoshikazu Natsui, Miyuki Nirasawa, Satoru Ozawa, Ryo Takahashi, Saori Yamaguchi, Tomokazu Yokota, Saki Yoshihashi, Tadashi Yoshiya, Taku Yoshizawa-Kumagaye, Kumiko Penninger, Josef
Source	PMC
abstract	Angiotensin-converting enzyme 2 (ACE2) is critically involved in cardiovascular physiology and pathology, and is currently clinically evaluated to treat acute lung failure. Here we show that the B38-CAP, a carboxypeptidase derived from Paenibacillus sp. B38, is an ACE2-like enzyme to decrease angiotensin II levels in mice. In protein 3D structure analysis, B38-CAP homolog shares structural similarity to mammalian ACE2 with low sequence identity. In vitro, recombinant B38-CAP protein catalyzed the conversion of angiotensin II to angiotensin 1–7, as well as other known ACE2 target peptides. Treatment with B38-CAP suppressed angiotensin II-induced hypertension, cardiac hypertrophy, and fibrosis in mice. Moreover, B38-CAP inhibited pressure overload-induced pathological hypertrophy, myocardial fibrosis, and cardiac dysfunction in mice. Our data identify the bacterial B38-CAP as an ACE2-like carboxypeptidase, indicating that evolution has shaped a bacterial carboxypeptidase to a human ACE2-like enzyme. Bacterial engineering could be utilized to design improved protein drugs for hypertension and heart failure.
has issue date	2020-02-26(xsd:dateTime)
bibo:doi	10.1038/s41467-020-14867-z
bibo:pmid	32103002
has license	cc-by
sha1sum (hex)	95f3513f4173df6761cba6c75b1b518b66ce5502
schema:url	https://doi.org/10.1038/s41467-020-14867-z
resource representing a document's title	B38-CAP is a bacteria-derived ACE2-like enzyme that suppresses hypertension and cardiac dysfunction
has PubMed Central identifier	PMC7044196
has PubMed identifier	32103002
schema:publication	Nat Commun
resource representing a document's body	covid:95f3513f4173df6761cba6c75b1b518b66ce5502#body_text
is schema:about of	named entity 'LIKE' named entity 'ACE2' named entity 'CONVERSION' named entity 'PROTEIN ' named entity 'ENGINEERING' named entity 'INVOLVED' named entity 'CARBOXYPEPTIDASE' named entity 'IN VITRO' named entity 'OVERLOAD' named entity 'TREATMENT' named entity 'INDUCED' named entity 'RECOMBINANT' named entity 'ANGIOTENSIN-CONVERTING ENZYME 2' named entity 'HUMAN' named entity 'PAENIBACILLUS SP. B38' named entity 'ACE2' named entity 'EVALUATED' named entity 'ENZYME' named entity 'MICE' named entity 'DERIVED' named entity 'SHAPED' named entity 'PEPTIDES' named entity 'LIKE' named entity '3D STRUCTURE' named entity 'SIMILARITY' named entity 'TO DECREASE' named entity 'CARDIAC DYSFUNCTION' named entity 'PRESSURE' named entity 'IDENTIFY' named entity 'INHIBITED' named entity 'KNOWN' named entity 'ANGIOTENSIN 1-7' named entity 'CARDIAC HYPERTROPHY' named entity 'COULD BE' named entity 'BACTERIAL' named entity 'HYPERTENSION' named entity 'SHARES' named entity 'ACUTE' named entity 'HERE' named entity 'LOW' named entity 'INDICATING' named entity 'CARDIOVASCULAR PHYSIOLOGY' named entity 'HYPERTROPHY' named entity 'PATHOLOGICAL' named entity 'SUPPRESSED' named entity 'HYPERTENSION' named entity 'CARDIAC DYSFUNCTION' named entity 'CAP' named entity 'SEQUENCE IDENTITY' named entity 'BACTERIA' named entity 'B38' named entity 'SUPPRESSES' named entity 'DERIVED' named entity 'IS A' named entity 'CAP' named entity 'LEVELS' named entity 'STRUCTURAL' named entity 'DATA' named entity 'ENZYME' named entity 'EVOLUTION'

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