Screening of some Yemeni medicinal plants for inhibitory activity against peptidases

Alasbahi, Rawiya H.; Melzig, Matthias F.

doi:10.1055/s-2008-1047849

Cited by 5 publications

(4 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Microbial pathogens have developed resistance against currently available antibiotics; which has triggered much interest in the isolation of antimicrobial proteins (Alasbahi and Melzig, 2008). The trypsin inhibitor protein from Acacia nilotica potently inhibits the growth of many pathogenic bacterial and fungal species and is therefore excellent candidate for the development of novel antimicrobial agents.…”

Section: Discussionmentioning

confidence: 99%

Model prediction of a Kunitz-type trypsin inhibitor protein from seeds of Acacianilotica L. with strong antimicrobial and insecticidal activity

Mehmood¹,

Imran²,

Ali³

et al. 2020

Turk J Biol

View full text Add to dashboard Cite

Kunitz-type trypsin inhibitor was first characterized from Enterolobium contortisiliquum (EcTI) (Batista et al., 1996). Plant-based KTIs have shown inhibition of trypsin or chymotrypsin along other serine proteinases such as subtilisin and elastase (Revina et al., 2004; Sumikawa et al., 2006). Some individual KTIs typically have shown more specific activities in comparison to those that inhibit cysteine or aspartic proteinases (Heibges et al., 2003). Kunitz-type trypsin inhibitors are also found in

show abstract

Section: Discussionmentioning

confidence: 99%

Model prediction of a Kunitz-type trypsin inhibitor protein from seeds of Acacianilotica L. with strong antimicrobial and insecticidal activity

Mehmood¹,

Imran²,

Ali³

et al. 2020

Turk J Biol

View full text Add to dashboard Cite

show abstract

“…Research for APN inhibitors aims to develop novel anticancer and anti-inflammatory drugs while dual neutral endopeptidase (NEP)/ angiotensin converting enzyme (ACE) inhibitors are targets to produce new class of antidepressant analgesics devoid of morphine side effects. No extract of P. longiflora showed activity against ACE nor APN [69].…”

Section: Hepatoprotectionmentioning

confidence: 87%

Therapeutic Potential of Pavetta L. Genus: An Updated Review of Its Traditional Uses, Phytochemistry, Pharmacology and Toxicological Aspects

Al-Madhagy

El‐Hawary²,

Sabry³

et al. 2022

Egypt. J. Chem.

View full text Add to dashboard Cite

Pavetta L. genus is one of the largest genera in Rubiaceae family. Although of the wide distribution and the variety of traditional uses of it plants, research covered only limited species of Pavetta L. genus. The purpose of this review is to provide an in-depth understanding of traditional uses, phytochemical, pharmacological, and toxicological characteristics of these plants, which may lead to new insights into new therapeutic benefits of them. To achieve that, literatures without time limitation was used to gather information about all features of Pavetta L. genus including its botanical description and geographical distribution.

show abstract

“…To confirm the inhibitory effect of the interaction between EGCG and neutrophil elastase on the activity of this enzyme, we measured the enzymatic activity of neutrophil elastase after treatment with EGCG or sivelestat sodium. Alasbahi 28 had verified the method of the elastase enzymatic activity assay. EGCG exerted a concentration-dependent inhibitory effect on the enzymatic activity of neutrophil elastase.…”

Section: Discussionmentioning

confidence: 99%

EGCG reverses human neutrophil elastase-induced migration in A549 cells by directly binding to HNE and by regulating α1-AT

Xiaokaiti

et al. 2015

Sci Rep

View full text Add to dashboard Cite

Lung carcinogenesis is a complex process that occurs in unregulated inflammatory environment. EGCG has been extensively investigated as a multi-targeting anti-tumor and anti-inflammatory compound. In this study, we demonstrated a novel mechanism by which EGCG reverses the neutrophil elastase-induced migration of A549 cells. We found that neutrophil elastase directly triggered human adenocarcinoma A549 cell migration and that EGCG suppressed the elevation of tumor cell migration induced by neutrophil elastase. We observed that EGCG directly binds to neutrophil elastase and inhibits its enzymatic activity based on the CDOCKER algorithm, MD stimulation by GROMACS, SPR assay and elastase enzymatic activity assay. As the natural inhibitor of neutrophil elastase, α1-antitrypsin is synthesized in tumor cells. We further demonstrated that the expression of α1-antitrypsin was up-regulated after EGCG treatment in neutrophil elastase-treated A549 cells. We preliminarily discovered that the EGCG-mediated induction of α1-antitrypsin expression might be correlated with the regulatory effect of EGCG on the PI3K/Akt pathway. Overall, our results suggest that EGCG ameliorates the neutrophil elastase-induced migration of A549 cells. The mechanism underlying this effect may include two processes: EGCG directly binds to neutrophil elastase and inhibits its enzymatic activity; EGCG enhances the expression of α1-antitrypsin by regulating the PI3K/AKT pathway.

show abstract

Screening of some Yemeni medicinal plants for inhibitory activity against peptidases

Cited by 5 publications

References 9 publications

Model prediction of a Kunitz-type trypsin inhibitor protein from seeds of Acacianilotica L. with strong antimicrobial and insecticidal activity

Model prediction of a Kunitz-type trypsin inhibitor protein from seeds of Acacianilotica L. with strong antimicrobial and insecticidal activity

Therapeutic Potential of Pavetta L. Genus: An Updated Review of Its Traditional Uses, Phytochemistry, Pharmacology and Toxicological Aspects

EGCG reverses human neutrophil elastase-induced migration in A549 cells by directly binding to HNE and by regulating α1-AT

Contact Info

Product

Resources

About