The chemistry of connective tissues. 5. The elastase activity of proteolytic enzymes

Thomas, J. D. R.; Partridge, S. M.

doi:10.1042/bj0740600

Cited by 38 publications

(11 citation statements)

References 27 publications

(27 reference statements)

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“…This assumption is supported by another experiment that was carried out using TR, which cleaves C-terminal to K and R residues. The results were consistent with earlier studies which reported virtually no elastinolytic activity for TR [Thomas and Partridge, 1960;Heinz et al, 2014]. Overall, it was found that TR neither cleaves elastin from WBS patients nor elastin from healthy individuals, which indicates that the K residues are mostly involved in cross-linking.…”

supporting

confidence: 93%

Elastins from patients with Williams–Beuren syndrome and healthy individuals differ on the molecular level

Heinz

Huertas

Schräder

et al. 2016

American J of Med Genetics Pt A

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Williams-Beuren syndrome (WBS) is a congenital disorder, which involves the heterozygous deletion of the elastin gene and other genes on chromosome 7. Clinical symptoms that are associated with hemizygosity of the essential extracellular matrix protein elastin include premature aging of the skin and supravalvular aortic stenosis. However, only little is known about the molecular basis of structural abnormalities in the connective tissue of WBS patients. Therefore, for the first time this study aimed to systematically characterize and compare the structure and amount of elastin present in skin and aortic tissue from WBS patients and healthy individuals. Elastin fibers were isolated from tissue biopsies, and it was found that skin of WBS patients contains significantly less elastin compared to skin of healthy individuals. Scanning electron microscopy and mass spectrometric measurements combined with bioinformatics data analysis were used to investigate the molecular-level structure of elastin. Scanning electron microscopy revealed clear differences between WBS and healthy elastin. With respect to the molecular-level structure, it was found that the proline hydroxylation degree differed between WBS and healthy elastin, while the tropoelastin isoform appeared to be the same. In terms of cross-linking, no differences in the content of the tetrafunctional cross-links desmosine and isodesmosine were found between WBS and healthy elastin. However, principal component analysis revealed differences between enzymatic digests of elastin from healthy probands and WBS patients, which indicates differing susceptibility toward enzymatic cleavage. Overall, the study contributes to a better understanding of the correlation between genotypic and elastin-related phenotypic features of WBS patients. © 2016 Wiley Periodicals, Inc.

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supporting

confidence: 93%

Elastins from patients with Williams–Beuren syndrome and healthy individuals differ on the molecular level

Heinz

Huertas

Schräder

et al. 2016

American J of Med Genetics Pt A

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“…The histological features of this lesion include dilatation of air spaces, particularly alveolar ducts, and alterations in elastin and reticulin fibers (11). Since papain has broad proteolytic activity, including elastolytic activity (12), it seems likely that the observed histological changes are due to enzymatic attack on lung proteins.…”

Section: Introductionmentioning

confidence: 99%

Effects of Elastase, Collagenase, and Papain on Structure and Function of Rat Lungs In Vitro

Johanson¹,

Pierce²

1972

J. Clin. Invest.

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A B S T R A C T Present concepts of the roles of collagen and elastin in lung elastic behavior and maintenance of lung structure have been largely inferred from anatomical observations or from studies of isolated fibers in vitro. Based on the intimate association of elastin and collagen it has been postulated that elastin contributes little to elastic behavior and that collagen is the major determinant of lung structure. Using clostridial collagenase, pancreatic elastase, and papain we have selectively degraded these fibers and studied the resulting changes in elastic behavior and structure of rat lungs in vitro.Pressure-volume curves were recorded during continuous slow air inflation and deflation (10.5 ml/min) before and after the intratracheal instillation of 0.5 ml of control or enzyme solution. Surface tension-lowering activity of lavaged material was studied. All lungs were fixed inflated at 25 cm H20 pressure and whole lung sections were stained for elastin, collagen, and reticulin. Collagenase produced a marked susceptibility to pleural rupture but did not alter elastic behavior or lung structure. Elastase and papain produced segments of lung with increased

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“…Besides its lytic action on elastin, elastase may act on other proteins. It possesses a relative specificity for aliphatic, hydrophobic aminoacids (Thomas and Partridge, 1960;Naughton and Sanger, 1961). Although several of the serum protease inhibitors do act on elastase, cxi-antitrypsin and cx2-macroglobulin were shown to be the most potent inhibitors (Heimburger and Haupt, 1966;Baumstark, 1967Baumstark, , 1970Bieth et al, 1970;Lieberman and Kaneshiro, 1972;Katayama and Fujita, 1974;Turino et al, 1974).…”

Section: Injurymentioning

confidence: 99%

Serum elastase and its inhibitors in the blood of heavily burnt patients.

Miskulin¹,

Moati²,

Robert³

et al. 1978

J Clin Pathol

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SUMMARY Serum elastase and its inhibitors were determined in the sera of heavily burnt patients. Serum elastase levels were elevated at two to eight days after a severe bum-accident and returned towards normal values from the 10th day on. Both oe,-antitrypsin and cV2-macroglobulin levels were also elevated in the sera of heavily burnt patients. acl-Antitrypsin showed a parallel evolution to the elastase level but 02-macroglobulin followed a somewhat different time curve. Plasminogen and antithrombin were not elevated significantly. It is suggested that serum elastase may play a role in tissue degradation in burnt patients.

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The chemistry of connective tissues. 5. The elastase activity of proteolytic enzymes

Cited by 38 publications

References 27 publications

Elastins from patients with Williams–Beuren syndrome and healthy individuals differ on the molecular level

Elastins from patients with Williams–Beuren syndrome and healthy individuals differ on the molecular level

Effects of Elastase, Collagenase, and Papain on Structure and Function of Rat Lungs In Vitro

Serum elastase and its inhibitors in the blood of heavily burnt patients.

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