Charcot–Leyden crystals: do they exist in veterinary species? A case report and literature review

Eun ju Choi, Andrew D. Miller, Elizabeth Devenish, Makoto Asakawa, Marina McConkey, Jeanine Peters-Kennedy

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The Charcot–Leyden crystal (CLC) is a major human eosinophil protein that readily crystallizes; these crystals are common in eosinophilic diseases. Although anecdotal existence of these crystals is known in veterinary pathology, definitive reports do not exist, to our knowledge. We identified eosinophilic crystals in a laryngeal myxosarcoma from a 2-y-old, spayed female, Labrador Retriever dog that were tentatively interpreted as CLCs. However, Ziehl–Neelsen acid-fast stain was negative, arguing against CLCs. The crystals stained red with Masson trichrome, precluding collagen. Periodic acid–Schiff and alcian blue were negative. The crystals stained positively with Okajima, and no myoglobin immunoreactivity was detected, supporting their identity as hemoglobin crystals. In the absence of a hematologic abnormality, these crystals were interpreted to be abnormal hemoglobin breakdown products. Protein sequence comparison was pursued to determine whether a protein similar to CLC exists in mammals. Only 3 nonhuman primate species, the Sumatran orangutan (Pongo abelii), rhesus macaque (Macaca mulatta), and cynomolgus monkey (Macaca fascicularis), had a sequence similarity of >80%. Of the crystal-forming residues, 12 of 54 (22%) were different in the Sumatran orangutan and 15 of 54 (28%) were different in the Macaca spp., which may affect the crystallization process. The lack of reports of CLCs in nonhuman species and our results collectively suggest that CLCs are human-specific.

Original languageEnglish (US)
Pages (from-to)904-909
Number of pages6
JournalJournal of Veterinary Diagnostic Investigation
Volume29
Issue number6
DOIs
StatePublished - Nov 1 2017
Externally publishedYes

Fingerprint

Pongo abelii
crystals
Macaca fascicularis
case studies
Macaca mulatta
Myxosarcoma
Veterinary Pathology
Abnormal Hemoglobins
Newfoundland and Labrador
Alcian Blue
Proteins
Myoglobin
Macaca
Crystallization
Eosinophils
Primates
Mammals
Hemoglobins
Coloring Agents
Collagen

Keywords

  • Charcot–Leyden crystal protein
  • histocytochemistry
  • sequence homology

ASJC Scopus subject areas

  • veterinary(all)

Cite this

Charcot–Leyden crystals : do they exist in veterinary species? A case report and literature review. / Choi, Eun ju; Miller, Andrew D.; Devenish, Elizabeth; Asakawa, Makoto; McConkey, Marina; Peters-Kennedy, Jeanine.

In: Journal of Veterinary Diagnostic Investigation, Vol. 29, No. 6, 01.11.2017, p. 904-909.

Research output: Contribution to journalArticle

Choi, Eun ju ; Miller, Andrew D. ; Devenish, Elizabeth ; Asakawa, Makoto ; McConkey, Marina ; Peters-Kennedy, Jeanine. / Charcot–Leyden crystals : do they exist in veterinary species? A case report and literature review. In: Journal of Veterinary Diagnostic Investigation. 2017 ; Vol. 29, No. 6. pp. 904-909.
@article{fd13bc7806034104ac35be73ea5ef714,
title = "Charcot–Leyden crystals: do they exist in veterinary species? A case report and literature review",
abstract = "The Charcot–Leyden crystal (CLC) is a major human eosinophil protein that readily crystallizes; these crystals are common in eosinophilic diseases. Although anecdotal existence of these crystals is known in veterinary pathology, definitive reports do not exist, to our knowledge. We identified eosinophilic crystals in a laryngeal myxosarcoma from a 2-y-old, spayed female, Labrador Retriever dog that were tentatively interpreted as CLCs. However, Ziehl–Neelsen acid-fast stain was negative, arguing against CLCs. The crystals stained red with Masson trichrome, precluding collagen. Periodic acid–Schiff and alcian blue were negative. The crystals stained positively with Okajima, and no myoglobin immunoreactivity was detected, supporting their identity as hemoglobin crystals. In the absence of a hematologic abnormality, these crystals were interpreted to be abnormal hemoglobin breakdown products. Protein sequence comparison was pursued to determine whether a protein similar to CLC exists in mammals. Only 3 nonhuman primate species, the Sumatran orangutan (Pongo abelii), rhesus macaque (Macaca mulatta), and cynomolgus monkey (Macaca fascicularis), had a sequence similarity of >80{\%}. Of the crystal-forming residues, 12 of 54 (22{\%}) were different in the Sumatran orangutan and 15 of 54 (28{\%}) were different in the Macaca spp., which may affect the crystallization process. The lack of reports of CLCs in nonhuman species and our results collectively suggest that CLCs are human-specific.",
keywords = "Charcot–Leyden crystal protein, histocytochemistry, sequence homology",
author = "Choi, {Eun ju} and Miller, {Andrew D.} and Elizabeth Devenish and Makoto Asakawa and Marina McConkey and Jeanine Peters-Kennedy",
year = "2017",
month = "11",
day = "1",
doi = "10.1177/1040638717725783",
language = "English (US)",
volume = "29",
pages = "904--909",
journal = "Journal of Veterinary Diagnostic Investigation",
issn = "1040-6387",
publisher = "American Association of Veterinary Laboratory Diagnosticians",
number = "6",

}

TY - JOUR

T1 - Charcot–Leyden crystals

T2 - do they exist in veterinary species? A case report and literature review

AU - Choi, Eun ju

AU - Miller, Andrew D.

AU - Devenish, Elizabeth

AU - Asakawa, Makoto

AU - McConkey, Marina

AU - Peters-Kennedy, Jeanine

PY - 2017/11/1

Y1 - 2017/11/1

N2 - The Charcot–Leyden crystal (CLC) is a major human eosinophil protein that readily crystallizes; these crystals are common in eosinophilic diseases. Although anecdotal existence of these crystals is known in veterinary pathology, definitive reports do not exist, to our knowledge. We identified eosinophilic crystals in a laryngeal myxosarcoma from a 2-y-old, spayed female, Labrador Retriever dog that were tentatively interpreted as CLCs. However, Ziehl–Neelsen acid-fast stain was negative, arguing against CLCs. The crystals stained red with Masson trichrome, precluding collagen. Periodic acid–Schiff and alcian blue were negative. The crystals stained positively with Okajima, and no myoglobin immunoreactivity was detected, supporting their identity as hemoglobin crystals. In the absence of a hematologic abnormality, these crystals were interpreted to be abnormal hemoglobin breakdown products. Protein sequence comparison was pursued to determine whether a protein similar to CLC exists in mammals. Only 3 nonhuman primate species, the Sumatran orangutan (Pongo abelii), rhesus macaque (Macaca mulatta), and cynomolgus monkey (Macaca fascicularis), had a sequence similarity of >80%. Of the crystal-forming residues, 12 of 54 (22%) were different in the Sumatran orangutan and 15 of 54 (28%) were different in the Macaca spp., which may affect the crystallization process. The lack of reports of CLCs in nonhuman species and our results collectively suggest that CLCs are human-specific.

AB - The Charcot–Leyden crystal (CLC) is a major human eosinophil protein that readily crystallizes; these crystals are common in eosinophilic diseases. Although anecdotal existence of these crystals is known in veterinary pathology, definitive reports do not exist, to our knowledge. We identified eosinophilic crystals in a laryngeal myxosarcoma from a 2-y-old, spayed female, Labrador Retriever dog that were tentatively interpreted as CLCs. However, Ziehl–Neelsen acid-fast stain was negative, arguing against CLCs. The crystals stained red with Masson trichrome, precluding collagen. Periodic acid–Schiff and alcian blue were negative. The crystals stained positively with Okajima, and no myoglobin immunoreactivity was detected, supporting their identity as hemoglobin crystals. In the absence of a hematologic abnormality, these crystals were interpreted to be abnormal hemoglobin breakdown products. Protein sequence comparison was pursued to determine whether a protein similar to CLC exists in mammals. Only 3 nonhuman primate species, the Sumatran orangutan (Pongo abelii), rhesus macaque (Macaca mulatta), and cynomolgus monkey (Macaca fascicularis), had a sequence similarity of >80%. Of the crystal-forming residues, 12 of 54 (22%) were different in the Sumatran orangutan and 15 of 54 (28%) were different in the Macaca spp., which may affect the crystallization process. The lack of reports of CLCs in nonhuman species and our results collectively suggest that CLCs are human-specific.

KW - Charcot–Leyden crystal protein

KW - histocytochemistry

KW - sequence homology

UR - http://www.scopus.com/inward/record.url?scp=85031906613&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85031906613&partnerID=8YFLogxK

U2 - 10.1177/1040638717725783

DO - 10.1177/1040638717725783

M3 - Article

C2 - 28782436

AN - SCOPUS:85031906613

VL - 29

SP - 904

EP - 909

JO - Journal of Veterinary Diagnostic Investigation

JF - Journal of Veterinary Diagnostic Investigation

SN - 1040-6387

IS - 6

ER -