Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has affected 660 million people and resulted in 6.7 million deaths. At present, a variety of risk factors related to the severity of COVID-19 have been identified, but whether allergic rhinitis and asthma will affect SARS-CoV-2 infection remains controversial. In general, there is no sufficient evidence to support that allergic rhinitis or asthma is a risk factor for increasing the rate of SARS-CoV-2 infection or aggravating the disease. Some studies even show that atopy may be a protective factor to alleviate SARS-CoV-2 infection, which is related to the decreased expression of angiotensin-converting enzyme 2, the receptor required for SARS-CoV-2 to enter cells, in atopic individuals. This paper reviews the influence of the severity and treatment of allergic rhinitis and asthma on SARS-CoV-2 infection, in order to provide some references for establishing strategies for prevention, risk stratification and treatment of COVID-19.
Humans ; COVID-19 ; SARS-CoV-2/metabolism* ; Peptidyl-Dipeptidase A/metabolism* ; Asthma/therapy* ; Rhinitis, Allergic

Coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has affected 660 million people and resulted in 6.7 million deaths. At present, a variety of risk factors related to the severity of COVID-19 have been identified, but whether allergic rhinitis and asthma will affect SARS-CoV-2 infection remains controversial. In general, there is no sufficient evidence to support that allergic rhinitis or asthma is a risk factor for increasing the rate of SARS-CoV-2 infection or aggravating the disease. Some studies even show that atopy may be a protective factor to alleviate SARS-CoV-2 infection, which is related to the decreased expression of angiotensin-converting enzyme 2, the receptor required for SARS-CoV-2 to enter cells, in atopic individuals. This paper reviews the influence of the severity and treatment of allergic rhinitis and asthma on SARS-CoV-2 infection, in order to provide some references for establishing strategies for prevention, risk stratification and treatment of COVID-19.
Humans ; COVID-19 ; SARS-CoV-2/metabolism* ; Peptidyl-Dipeptidase A/metabolism* ; Asthma/therapy* ; Rhinitis, Allergic

Acute Kidney Injury ; chemically induced ; enzymology ; Animals ; Disease Models, Animal ; Gentamicins ; Peptidyl-Dipeptidase A ; metabolism ; Rats

AIMTo establish a method for determinate of the inhibitory activity of angiotensin-converting enzyme inhibitor captopril by high performance capillary electrophoresis.

METHODSThe characteristic absorptive wavelength of hippuric acid determined by ultraviolet spectrophotometer is 228 nm. The method employed a melted capillary column, 50 mmol.L-1 phosphoric acid (pH 8.3) buffer solution, inject pressure 4.8 kPa, inject time 3 s, separation voltage 20 kV and detection wavelength 228 nm.

RESULTSThe reactant and resultant was separated completed within 7 min. IC50 of captopril was 0.019 mumol.L-1. Captopril is a competitive inhibitor, which was proved by enzyme reaction dynamics.

CONCLUSIONThe method was shown to be accurate, simple and rapid and can be used for determination of the inhibitory activity of captopril.

Angiotensin-Converting Enzyme Inhibitors ; pharmacology ; Captopril ; pharmacology ; Electrophoresis, Capillary ; methods ; Hippurates ; analysis ; Peptidyl-Dipeptidase A ; metabolism

OBJECTIVETo investigate the expression of angiotensin converting enzyme (ACE) and ACE2 Gene in lung of paraquat poisoning rats and the protection of sodium dimercaptopropane sulfonate (Na-DMPS).

METHODSOne hundred SD male rats were randomly equally divided into 4 groups:normal control group (10 rats), drug control group (40 rats), paraquat poisoning group (40 rats) and drug intervention group(40 rats). The paraquat poisoning and drug intervention group rats were injected intraperitoneally by paraquat (20 mg/kg). The rats in drug intervention group rats were protected by intraperitoneal injection with Na-DMPS (200 mg/kg) 15 min before exposure of paraquat. Behavioral changes of the rats and histological changes of lung tissues under light microscope were observed. And the expression of ACE and ACE2 mRNA in lung tissues of rats both in paraquat poisoned group and drug intervention group were measured by RT-PCR at different time of 6 h, 24 h, 3 and 7 d after poisoning.

RESULTSThe poisoning symptoms of shortness of breath, cramps appeared and deteriorated progressively in rats after paraquat exposure and the protection of NA-DMPS could delay and reduce these symptoms significantly. Histological appearance of disorganization of pulmonary capillary and alveolus, exudation in alveolar space, pulmonary edema, severe bleeding, and inflammatory cells infiltration were obvious in lungs of rats after paraquat poisoning, whereas the histological changes were extenuated by protection of NA-DMPS. As compared with normal control group (NC group), the expressions of ACE, ACE2 mRNA in lung tissue decreased, and the lowest level of ACE mRNA expressions appeared at 24 h (0.457 +/- 0.262), on 3 d (0.385 +/- 0.179) after Paraquat exposure (P < 0.05), while lowest level of ACE2 mRNA expressions appeared on 3 d (0.415 +/- 0.247), 7 d (0.365 +/- 0.215) (P < 0.05). As compared with paraquat poisoned group, the expressions of ACE mRNA in lung tissue of rats in NA-DMPS protected group increased significantly at 24 h (0.739 +/- 0.558) and 3 d (0.749 +/- 0.414) (P < 0.05), while the expressions of ACE2 mRNA increased markedly on 3 d (0.584 +/- 0.345) and 7 d (0.493 +/- 0.292) (P < 0.05). But the expression of ACEmRNA and ACE2 mRNA in lungs had no statistical significance between normal control group and drug intervention group (P > 0.05).

CONCLUSIONThe expressions of ACE and ACE2 mRNA in lung tissue of the rats with paraquat poisoning are decreased. Na-DMPS can effectively improve the balance of RAS in local lung tissue and reduce the pathological changes of lung tissue, delay the poisoning symptoms and show protective effects for acute lung injury induced by paraquat.

Animals ; Lung ; drug effects ; enzymology ; Male ; Paraquat ; poisoning ; Peptidyl-Dipeptidase A ; biosynthesis ; genetics ; metabolism ; Rats ; Rats, Sprague-Dawley ; Unithiol ; pharmacology

Angiotensin I-converting enzyme (ACE, EC3.4.15.1) plays an important role in regulating blood pressure. The C-domain of ACE has been identified as the main catalytic site of angiotensin I cleavage in vivo. The ACE gene fragment of the C-domain was amplified by PCR and cloned into the pPIC9K secretory expression plasmid. The recombinant plasmid was transformed into Pichia pastoris strain GS115. Positive clones were selected and subject to electroporation. Antibiotic G418 was used for the screening of multicopy inserts. After optimization of the expression system, the protein yield reached 0.5 g/L by flask-shaking culture fermentation, and enzyme activity reached 7.178 U/mL in the fermentation supernatant. The purity of the target protein obtained was 97% after Ni+ affinity chromatography. Enzyme inhibitory activity assay using Captopril showed that it is promising to use ACE-C domain as new generation of target for screening ACE inhibitor antihypertensive drugs.
Angiotensin-Converting Enzyme Inhibitors ; Catalytic Domain ; genetics ; Electroporation ; Humans ; Peptidyl-Dipeptidase A ; biosynthesis ; genetics ; Pichia ; genetics ; metabolism ; Recombinant Proteins ; biosynthesis ; genetics

Angiotensin converting enzyme (ACE, EC 3.4.15.1) is a membrane-bound, zinc dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor ocatapeptide angiotensin II, by removing two C-terminal amino acids. ACE is well known as a key part of the renin angiotenisn system that regulates blood pressure, and its inhibitors have potential for the treatment of hypertension. This paper reviewed the characteristics of ACE in aspects of its structure-function relationship, gene polymorphism and inhibitor development. In particular, the catalytic mechanisms of the two active sites of somatic ACE in the cleavage of angiotensin I and bradykin are different. Therefore, it would likely provide a new way for exploiting novel ACE inhibitors with fewer side-effects by specifically-targeting the individual active sites of somatic ACE.
Angiotensin-Converting Enzyme Inhibitors ; pharmacology ; Antihypertensive Agents ; pharmacology ; Humans ; Peptidyl-Dipeptidase A ; chemistry ; genetics ; metabolism ; Polymorphism, Genetic ; Structure-Activity Relationship

The rostral ventrolateral medulla (RVLM) is a key region in cardiovascular regulation. It has been demonstrated that cholinergic synaptic transmission in the RVLM is enhanced in hypertensive rats. Angiotensin-converting enzyme 2 (ACE2) in the brain plays beneficial roles in cardiovascular function in hypertension. The purpose of this study was to determine the effect of ACE2 overexpression in the RVLM on cholinergic synaptic transmission in spontaneously hypertensive rats (SHRs). Four weeks after injecting lentiviral particles containing enhanced green fluorescent protein and ACE2 bilaterally into the RVLM, the blood pressure and heart rate were notably decreased. ACE2 overexpression significantly reduced the concentration of acetylcholine in microdialysis fluid from the RVLM and blunted the decrease in blood pressure evoked by bilateral injection of atropine into the RVLM in SHRs. In conclusion, we suggest that ACE2 overexpression in the RVLM attenuates the enhanced cholinergic synaptic transmission in SHRs.
Acetylcholine ; metabolism ; Animals ; Blood Pressure ; physiology ; Cardiovascular System ; metabolism ; Cholinergic Neurons ; metabolism ; Hypertension ; metabolism ; Male ; Peptidyl-Dipeptidase A ; metabolism ; Rats ; Rats, Inbred SHR ; metabolism

OBJECTIVETo investigate the mRNA expression of severe acute respiratory syndrome-associated coronavirus (SARS-COV) functional receptor, angiotensin-converting enzyme 2 (ACE2), in human femoral head and conjunctiva, and explore the possible entry route of SARS-COV in human femoral head.

METHODSACE2 mRNA in human femoral head was detected by nested RT-PCR with human beta actin gene as the positive control.

RESULTSThe mRNA of human beta actin gene could be amplified efficiently in all the tissue samples. The mRNA of human ACE2 was expressed efficiently in the normal lung tissue, but not in the cartilage and cancellous bone under the weight-bearing area of the femoral head.

CONCLUSIONSARS-COV can not infect the femoral head tissue and lead to avascular necrosis of the femoral head directly by the spike glycoprotein, and mechanism of the virus for causing avascular necrosis needs further investigation.

Femoral Neck Fractures ; metabolism ; Femur Head ; metabolism ; Gene Expression ; Humans ; Peptidyl-Dipeptidase A ; genetics ; RNA, Messenger ; biosynthesis ; genetics ; Receptors, Virus ; genetics ; Reverse Transcriptase Polymerase Chain Reaction ; SARS Virus ; metabolism

OBJECTIVETo investigate the inhibitory effect of angiotensin-converting enzyme 2 (ACE2) on angiotensin II (Ang II)-induced down-regulation of albumin expression and enhancement of cell migration in rat hepatocytes.

METHODSCultured rat hepatocyte were treated with Ang II (10-7 mol/L) for different time lengths, and the protein expressions of vimentin and albumin and cell migration were detected. The cells transfected with lentiGFP or lentiACE2 were treated with A779 for 1 h and then with Ang II, and Western blotting and immunofluorescent cytochemistry were used to detect the protein levels; the cell migration was evaluated by Transwell assay.

RESULTAng II induced significantly increased vimentin expression and reduced albumin expression in rat hepatocytes in a time-dependent manner. Overexpression of ACE2 obviously inhibited the up-regulation of vimentin expression, reduction of albumin expression, and enhancement of cell migration induced by Ang II.

CONCLUSIONACE2 overexpression can inhibit Ang II-induced up-regulation of vimentin, reduction of albumin expression, and enhancement of cell migration in rat hepatocytes.

Albumins ; metabolism ; Angiotensin II ; pharmacology ; Animals ; Cell Movement ; Cells, Cultured ; Down-Regulation ; Hepatocytes ; cytology ; Lentivirus ; Peptidyl-Dipeptidase A ; genetics ; metabolism ; Rats ; Transfection ; Up-Regulation ; Vimentin ; metabolism