Trypsin, chymotrypsin and elastase in health and disease DOI Creative Commons
Oladoyin Grace Famutimi,

Victor Gbolahan Adebiyi,

Bukola Grace Akinmolu

et al.

Future Journal of Pharmaceutical Sciences, Journal Year: 2024, Volume and Issue: 10(1)

Published: Sept. 17, 2024

Abstract Background Serine proteases represent over 1% of all proteins in humans. This family is found on cell surfaces, subcellular organelles like lysosomes or mitochondria, within the nucleus and protoplasm. Main body abstract Among them, trypsin, chymotrypsin elastase have aroused great interest because their numerous functions pathophysiological processes. Altered expression these enzymes experimental animal models humans has been related to various pathologies, developmental defects, metabolic dysfunctions, cancer, peripheral vascular diseases infectious diseases. Trypsin chymotrypsin-like activate, less oftentimes inactivate, substrates, together with growth factors, receptors, adhesion molecules, angiogenic factors metalloproteases. a number them are key cancer progression, metastasis severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) disease. Elastin-degrading enzyme- elastase, slowly damages elastin lifetime an organism. The physiological processes triggered by leads progression different conditions such as syndrome, pulmonary emphysema, atherosclerosis, chronic obstructive These serine currently considered be targets for development new potent therapeutics. Short conclusion cumulative knowledge that outlined pathological implications proposed strategies regulate activities targeting therapeutic application validation selected disease states highlighted. should enhance our appreciation roles aetiology some well chemotherapeutic benefits inhibition modulation.

Language: Английский

Mammalian orthoreovirus: Pathogenicity, Zoonotic Potential, and Therapeutic Promise DOI

Radwa A. Lela,

Hager A. Bendary,

Ahmed H. Ghonaim

et al.

Published: Jan. 1, 2025

Language: Английский

Citations

0
Trypsin, chymotrypsin and elastase in health and disease DOI Creative Commons
Oladoyin Grace Famutimi,

Victor Gbolahan Adebiyi,

Bukola Grace Akinmolu

et al.

Future Journal of Pharmaceutical Sciences, Journal Year: 2024, Volume and Issue: 10(1)

Published: Sept. 17, 2024

Abstract Background Serine proteases represent over 1% of all proteins in humans. This family is found on cell surfaces, subcellular organelles like lysosomes or mitochondria, within the nucleus and protoplasm. Main body abstract Among them, trypsin, chymotrypsin elastase have aroused great interest because their numerous functions pathophysiological processes. Altered expression these enzymes experimental animal models humans has been related to various pathologies, developmental defects, metabolic dysfunctions, cancer, peripheral vascular diseases infectious diseases. Trypsin chymotrypsin-like activate, less oftentimes inactivate, substrates, together with growth factors, receptors, adhesion molecules, angiogenic factors metalloproteases. a number them are key cancer progression, metastasis severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) disease. Elastin-degrading enzyme- elastase, slowly damages elastin lifetime an organism. The physiological processes triggered by leads progression different conditions such as syndrome, pulmonary emphysema, atherosclerosis, chronic obstructive These serine currently considered be targets for development new potent therapeutics. Short conclusion cumulative knowledge that outlined pathological implications proposed strategies regulate activities targeting therapeutic application validation selected disease states highlighted. should enhance our appreciation roles aetiology some well chemotherapeutic benefits inhibition modulation.

Language: Английский

Citations

2