Evaluation of exocrine pancreatic function

Cotten, Steven W.

doi:10.1016/b978-0-12-815499-1.00033-8

Cited by 4 publications

(6 citation statements)

References 52 publications

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“…including Escherichia coli, as well as spirochetes and fungi [25,28,29]. Neutrophils also employ extracellular neutrophil traps (NETs) as a mechanism to eliminate pathogenic microorganisms.…”

Section: Functionsmentioning

confidence: 99%

“…SPs are enzymes known for their proteolytic degrading nature, as they have a strong affinity for catalyzing the cleavage of carboxyl groups found in small hydrophobic amino acids like glycine, alanine, and valine [25]. However, these enzymes are non-specific degradants, capable of cleaving various types of proteins that constitute the extracellular matrix, including fibronectin, elastin, proteoglycans, collagens, platelet receptor IIb/IIIa, cadherins, and a wide range of plasma proteins [26].…”

Section: Functionsmentioning

confidence: 99%

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Human neutrophil elastase inhibitors: Classification, biological‐synthetic sources and their relevance in related diseases

Ocampo‐Gallego,

Pedroza‐Escobar,

Caicedo‐Ortega

et al. 2023

Fundamemntal Clinical Pharma

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BackgroundHuman neutrophil elastase is a multifunctional protease enzyme whose function is to break the bonds of proteins and degrade them to polypeptides or amino acids. In addition, it plays an essential role in the immune mechanism against bacterial infections and represents a key mediator in tissue remodeling and inflammation. However, when the extracellular release of this enzyme is dysregulated in response to low levels of its physiological inhibitors, it ultimately leads to the degradation of proteins, in particular elastin, as well as other components of the extracellular matrix, producing injury to epithelial cells, which can promote sustained inflammation and affect the innate immune system, and, therefore, be the basis for the development of severe inflammatory diseases, especially those associated with the cardiopulmonary system.ObjectiveThis review aims to provide an update on the elastase inhibitory properties of several molecules, either synthetic or biological sources, as well as their classification and relevance in related pathologies since a clear understanding of the function of these molecules with the inhibitory capacity of this protease can provide valuable information for the development of pharmacological therapies that manage to modify the prognosis and survival of various inflammatory diseases.MethodsCollected data from scientific databases, including PubMed, Google Scholar, Science Direct, Nature, Wiley, Scopus, and Scielo. Articles published in any country and language were included.ResultsWe reviewed and included 132 articles conceptualizing neutrophil elastase activity and known inhibitors.ConclusionUnderstanding the mechanism of action of elastase inhibitors based on particular aspects such as their kinetic behavior, structure–function relationship, chemical properties, origin, pharmacodynamics, and experimental progress has allowed for a broad classification of HNE inhibitors.

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Section: Functionsmentioning

confidence: 99%

Section: Functionsmentioning

confidence: 99%

Human neutrophil elastase inhibitors: Classification, biological‐synthetic sources and their relevance in related diseases

Ocampo‐Gallego,

Pedroza‐Escobar,

Caicedo‐Ortega

et al. 2023

Fundamemntal Clinical Pharma

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“…The sites of chymotrypsin cleavage are peptide bonds formed by the carboxyl groups of aromatic amino acids (tyrosine, phenylalanine, and tryptophan) and leucine [ 72 ]. Elastase is associated with breakdown of the peptide bonds formed by the short aliphatic amino acids such as glycine, alanine, and valine [ 73 ]. The major products of honey proteases are short peptides that function as antioxidants, antitumor, and antimicrobials, and are used as weight loss inducers ( Figure 2 ).…”

Section: Enzymatic Reactions In Honeymentioning

confidence: 99%

“… The proteases in honey: their types, origin, substrate, products, and their contribution to the biological activities of honey [ 6 , 30 , 37 , 69 , 70 , 71 , 72 , 73 ]. …”

Section: Figurementioning

confidence: 99%

Biochemical Reactions and Their Biological Contributions in Honey

et al. 2022

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Honey is known for its content of biomolecules, such as enzymes. The enzymes of honey originate from bees, plant nectars, secretions or excretions of plant-sucking insects, or from microorganisms such as yeasts. Honey can be characterized by enzyme-catalyzed and non-enzymatic reactions. Notable examples of enzyme-catalyzed reactions are the production of hydrogen peroxide through glucose oxidase activity and the conversion of hydrogen peroxide to water and oxygen by catalase enzymes. Production of hydroxymethylfurfural (HMF) from glucose or fructose is an example of non-enzymatic reactions in honey.

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“…To estimate the sites digested by trypsin, elastase, or α-chymotrypsin in the C-terminal region of the ORF2 protein, we aligned the ORF2 amino acid sequences (aa 560-660) of four representative HEV strains (genotype 3b, JE03-1760F, which is used in this study; genotype 1b, SAR-55; genotype 3a, Kernow-C1; genotype 4, HE-JF5/15F). On the basis of the reported protease digestion sites [32][33][34], R578, A579, and L601 were estimated to be the trypsin, elastase, and α-chymotrypsin digestion sites of the ORF2 protein, respectively (Figure 4B). The R578 residue of the ORF2 protein was conserved among 180 HEV strains of genotypes 1-8 (Supplementary Table S1), suggesting that the ORF2 protein of fecal HEV was digested at R578 (furthest away from the C-terminus among the three typical proteases in the intestine), and probably lacked the 88 C-terminal amino acid residues (V579-S660 fragment), consistent with the length of the DOC-treated trypsin-digested ORF2 protein (ORF2tr) observed on SDS-PAGE (Figure 4A).…”

Section: Protease Digestion Sites Of the Orf2 Protein Associated With The Hev Virionmentioning

confidence: 99%

The Capsid (ORF2) Protein of Hepatitis E Virus in Feces Is C-Terminally Truncated

et al. 2021

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The hepatitis E virus (HEV) is a causative agent of hepatitis E. HEV virions in circulating blood and culture media are quasi-enveloped, while those in feces are nonenveloped. The capsid (ORF2) protein associated with an enveloped HEV virion is reported to comprise the translation product of leucine 14/methionine 16 to 660 (C-terminal end). However, the nature of the ORF2 protein associated with fecal HEV remains unclear. In the present study, we compared the molecular size of the ORF2 protein among fecal HEV, cell-culture-generated HEV (HEVcc), and detergent-treated protease-digested HEVcc. The ORF2 proteins associated with fecal HEV were C-terminally truncated and showed the same size as those of the detergent-treated protease-digested HEVcc virions (60 kDa), in contrast to those of the HEVcc (68 kDa). The structure prediction of the ORF2 protein (in line with previous studies) demonstrated that the C-terminal region (54 amino acids) of an ORF2 protein is in flux, suggesting that proteases target this region. The nonenveloped nondigested HEV structure prediction indicates that the C-terminal region of the ORF2 protein moves to the surface of the virion and is unnecessary for HEV infection. Our findings clarify the maturation of nonenveloped HEV and will be useful for studies on the HEV lifecycle.

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Evaluation of exocrine pancreatic function

Cited by 4 publications

References 52 publications

Human neutrophil elastase inhibitors: Classification, biological‐synthetic sources and their relevance in related diseases

Human neutrophil elastase inhibitors: Classification, biological‐synthetic sources and their relevance in related diseases

Biochemical Reactions and Their Biological Contributions in Honey

The Capsid (ORF2) Protein of Hepatitis E Virus in Feces Is C-Terminally Truncated

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