Id |
Subject |
Object |
Predicate |
Lexical cue |
T466 |
0-110 |
Sentence |
denotes |
A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. |
T467 |
111-200 |
Sentence |
denotes |
The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. |
T468 |
201-269 |
Sentence |
denotes |
Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. |
T469 |
270-300 |
Sentence |
denotes |
ADAM17 mediates ACE2 shedding. |
T470 |
301-390 |
Sentence |
denotes |
SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. |
T471 |
391-540 |
Sentence |
denotes |
Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. |
T472 |
541-665 |
Sentence |
denotes |
ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. |
T473 |
666-822 |
Sentence |
denotes |
Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. |
T474 |
823-892 |
Sentence |
denotes |
The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. |
T475 |
893-969 |
Sentence |
denotes |
However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. |
T476 |
970-1158 |
Sentence |
denotes |
SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. |
T477 |
1159-1250 |
Sentence |
denotes |
Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. |
T478 |
1251-1324 |
Sentence |
denotes |
Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. |
T479 |
1325-1381 |
Sentence |
denotes |
SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. |
T480 |
1382-1447 |
Sentence |
denotes |
The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. |
T481 |
1448-1553 |
Sentence |
denotes |
Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. |
T482 |
1554-1622 |
Sentence |
denotes |
SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. |
T483 |
1623-1743 |
Sentence |
denotes |
If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. |
T484 |
1744-1927 |
Sentence |
denotes |
Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. |
T485 |
1928-2050 |
Sentence |
denotes |
Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms. |