Über die chemische Natur der Charcot-Leydenschen Kristalle

Buddecke, E.; Essellier, A. F.; Marti, H. R.

doi:10.1515/bchm2.1956.305.1.203

Cited by 8 publications

(2 citation statements)

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“…Primate eosinophils are remarkable in that they form crystalline substances, the CLC (23). Prior studies of CLC had suggested that they were proteinaceous and of low molecular weight (4)(5)(6). CLC were prepared by the method of Archer and Blackwood and crystals with a characteristic dipyramidal structure largely free from contaminating debris formed from the eosinophil homogenates (6).…”

Section: Resultsmentioning

confidence: 99%

Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils.

Gleich¹,

Loegering²,

Mann³

et al. 1976

J. Clin. Invest.

215

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A B S T R A C T Guinea pig eosinophil granules contain a protein, the major basic protein (MBP), which accounts for more than half of the total granule protein, has a high content of arginine, and displays a remarkable tendency to form disulfide-linked aggregates. In this study we have purified a similar protein from human eosinophil granules and have compared the human MBP to the protein comprising the Charcot-Leyden crystal (CLC). Eosinophils from patients with various diseases were purified and disrupted, and the granule fraction was obtained. Examination of the granule fraction by transmission electron microscopy showed numerous typical eosinophil granules. Analyses of granule lysates by gel filtration and by polyacrylamide gel electrophoresis revealed the presence of peroxidase and MBP with properties similar to that previously found in guinea pig eosinophil granules. The human MBP had a molecular weight of 9,200, contained less than 1% carbohydrate, was rich in arginine, and readily formed disulfide-bonded aggregates.CLC were prepared from eosinophil-rich cell suspensions by homogenization in hypotonic saline. The supernates following centrifugation of cell debris spontaneously formed CLC. Analysis of CLC revealed the presence of a protein with a molecular weight of 13,000 containing 1.2% carbohydrate. The

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Section: Resultsmentioning

confidence: 99%

Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils.

Gleich¹,

Loegering²,

Mann³

et al. 1976

J. Clin. Invest.

215

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“…The introduction of additional molecular weight markers, the a and chains of hemoglobin (about 15,000 Mr) (16), confirmed the larger size of CLC and lysophospholipase. Some (5,23), but not all (24), studies of CLC have found increased quantities of zinc associated with CLC, and the sulfhydryl dependence of lysophospholipase (18) allows for the possible binding of zinc ions by sulfhydryl groups of the cysteine residues (12,23). However, the purification of lysophospholipase in the presence of 2 mM EDTA and the ability of purified enzyme to form CLC in the presence of EDTA suggest that zinc is not an integral component of the crystals.…”

Section: Discussionmentioning

confidence: 99%

Identification of human eosinophil lysophospholipase as the constituent of Charcot-Leyden crystals.

Weller¹,

Goetzl²,

Austen³

1980

Proc. Natl. Acad. Sci. U.S.A.

114

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Since the initial descriptions of Charcot-Leyden crystals more than 100 years ago, the presence of these slender, dipyramidal crystals in human tissues and biologic fluids has become a hallmark of eosinophilic leukocyte infiltration, especially in association with allergic and helminthic diseases. The formation of these crystals in vitro after disruption of human eosinophils, but not of other cell types, in hypotonic saline or detergent established the eosinophil as the unique cellular source of the crystalline protein. Charcot-Leyden crystals have now been found to express lysophospholipase activity (lysolecithin acylhydrolase, EC 3.1.1.5), and the solubilized Charcot-Leyden crystal protein presents a single stained protein band that is coincident with the lysophospholipase activity eluted from replicate gels on alkaline polyacrylamide gel electrophoresis. On sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the solubilized Charcot-Leyden crystal protein migrates with a molecular weight of 17,400, which is comparable to that of eosinophil lysophospholipase purified chromatographically to homogeneity; further, on combination, the two proteins comigrate as a single staining band. Finally, the chromatographically purified eosinophil lysophospholipase in hypotonic buffer forms dipyramidal crystals morphologically identical to Charcot-Leyden crystals. The findings that chromatographically purified, homogeneous eosinophil lysophospholipase and Charcot-Leyden crystal protein express the same enzymatic activity, are of the same size and charge, and form crystals of identical morphology indicate that human eosinophil lysophospholipase is the constituent of Charcot-Leyden crystals.

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Chemie und Physiologie biogener Zink‐Verbindungen

Weitzel

1956

Angewandte Chemie

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Als zellvertraute, Zink‐bindende Konfigurationen fungieren in erster Linie Imidazol‐ und SH‐Gruppen. Die hohe Zink‐Affinität einfacher Imidazol‐Verbindungen kehrt wieder bei Histidin und Histidyl‐Peptiden sowie bei den Imidazol‐Gruppen von Proteinen, wie Albumin, Globulin und Insulin. Das Zink‐Bindungsvermögen von Purinen und Nucleosiden beruht ebenfalls maßgeblich auf der in ihnen enthaltenen Imidazol‐Konfiguration. Als Zink‐affine SH‐Verbindungen treten Cystein, Cysteinyl‐Peptide und SH‐haltige Proteine auf. Die Zink‐Anreicherungen in bestimmten Organen des Tierkörpers zeigen dieselben Konfigurationen. So ist das „Inselzink”︁ des Pankreas mit größter Wahrscheinlichkeit an die Imidazol‐Gruppen der blutzuckersteuernden Wirkstoffe gebunden, während im Augenhintergrund verschiedener Säugetierarten große Mengen von Zink‐Cystein enthalten sind. Als dritte, physiologisch wichtige Zink‐affine Gruppierung zeichnen sich gewisse Glutamyl‐Peptide ab.

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Über die chemische Natur der Charcot-Leydenschen Kristalle

Cited by 8 publications

References 0 publications

Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils.

Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils.

Identification of human eosinophil lysophospholipase as the constituent of Charcot-Leyden crystals.

Chemie und Physiologie biogener Zink‐Verbindungen

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