Effect of Oral Alpha-chymotrypsin on Sputum Viscosity

Bruce, Robert A.; Quinton, K. C.

doi:10.1136/bmj.1.5274.282

Cited by 16 publications

(6 citation statements)

References 7 publications

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“…This is consistent with evidence suggesting that chymotrypsin may be absorbed in its active form through the intestinal wall (Avakian 1964;Bruce and Quinton 1962;Kabacoff et al 1963). In view of these studies it is tempting to suggest that chymotrypsin produced in the epithelium could be released into the general circulation.…”

Section: Discussionsupporting

confidence: 91%

Chymotrypsin gene expression in rat peripheral organs

Wang

Strauss

et al. 1998

Cell and Tissue Research

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Prior studies have revealed the presence of chymotrypsinlike protease in peripheral organs, although no definitive evidence for the synthesis of this enzyme in tissue other than the pancreas is available. In an attempt to detect chymotrypsinogen mRNA in peripheral organs, a fragment of the pancreatic chymotrypsin mRNA from rat was amplified using PCR. The sequence was identified as a portion of the rat chymotrypsin B gene overlapping exon 5 through exon 7. It was subcloned into the pGEM-4Z vector and used as a template for the vitro transcription of an antisense riboprobe. Using ribonuclease protection and Northern blot analyses, chymotrypsin mRNA was detected in the rat pancreas, stomach, duodenum, ovary, and spleen. Monoclonal and polyclonal antisera against chymotrypsin detected chymotrypsinlike immunoreactivity in rat and human pancreas, rat stomach, duodenum and jejunum. Electrophoresis and immunoblotting revealed chymotrypsin-chymotrypsinogen bands (25-29 kDa) in the stomach and duodenum. Synthesis of a potent protease such as chymotrypsin in tissue other than pancreas is significant, suggesting a potential physiological and/or pathological role in these tissues.

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Section: Discussionsupporting

confidence: 91%

Chymotrypsin gene expression in rat peripheral organs

Wang

Strauss

et al. 1998

Cell and Tissue Research

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“…Previous studies have demonstrated that it has a direct mucolytic effect on sputum. Specifically, it can liquefy the mucus and decrease the viscosity of sputum by destroying the peptide bridge of bi-polymers and hydrolyzing fibrin, mucin, and other sputum proteins into polypeptides or amino acids [ 14 - 16 ]; this favors the removal of purulent secretions and necrotic tissues. A decrease in the viscosity of sputum in patients with chronic bronchitis has also been demonstrated following the oral administration of α-chymotrypsin [ 16 ].…”

Section: Discussionmentioning

confidence: 99%

“…Specifically, it can liquefy the mucus and decrease the viscosity of sputum by destroying the peptide bridge of bi-polymers and hydrolyzing fibrin, mucin, and other sputum proteins into polypeptides or amino acids [ 14 - 16 ]; this favors the removal of purulent secretions and necrotic tissues. A decrease in the viscosity of sputum in patients with chronic bronchitis has also been demonstrated following the oral administration of α-chymotrypsin [ 16 ]. Additionally, α-chymotrypsin exerts an anti-inflammatory effect by increasing the expression levels of anti-inflammatory cytokines, such as IL-4 and IL-17, and decreasing the expression of IFN-γ in inflammatory lesions [ 17 ].…”

Section: Discussionmentioning

confidence: 99%

Management of Plastic Bronchitis Using α-Chymotrypsin: A Novel Treatment Modality

Xiong

Rao

Peng

et al. 2021

Cureus

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“…With this preparation, marked reduction of sputum viscosity in patients with respiratory diseases has been demonstrated. 53 On the other hand, Chymoral is without any effect on patients with mucoviscidosis. 316 The use of chymotrypsin in pulmonary alveolar proteinosis 50 will be discussed in the section on trypsin.…”

Section: Chymotrypsinmentioning

confidence: 99%

Proteolytic enzymes in clinical medicine

Colman

1965

Clin Pharma and Therapeutics

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The explosive expansion of our knowledge of the basic properties of the mammalian proteolytic enzymes has stimulated a parallel growth in their applications to clinical medicine. The outcome of this research has been significant advances in the therapy, diagnosis, and pathogenesis of disease processes in almost all fields of medicine. The enzymes discussed in this paper are pepsin, the pancreatic endopeptidases (chymotTypsin, trypsin, kallikrein, and elastase), the blood proteolytic enzymes (thrombin and plasmin), the pancreatic exopeptidases (leucine aminopeptidase and carboxypeptidases), and the tissue proteases (cathepsins). After a brief summary of the physical and biochemical properties of each enzyme, a critical appraisal is made of its potential and limitations as the enzyme is used in clinical medicine. This review concentrates on a delineation of the more important of the recent contributions, a discussion of certain controversial areas, with speCial emphasis on the therapeutic applications and the suggestion of certain fields of investigation which may require more attention in the future.

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Effect of Oral Alpha-chymotrypsin on Sputum Viscosity

Cited by 16 publications

References 7 publications

Chymotrypsin gene expression in rat peripheral organs

Chymotrypsin gene expression in rat peripheral organs

Management of Plastic Bronchitis Using α-Chymotrypsin: A Novel Treatment Modality

Proteolytic enzymes in clinical medicine

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