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{{Infobox_gene}}
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'''Eosinophil lysophospholipase''' is an [[enzyme]] that in humans is encoded by the ''CLC'' [[gene]].<ref name="pmid1577491">{{cite journal | vauthors = Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ | title = Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14 | journal = Genomics | volume = 13 | issue = 1 | pages = 240–2 |date=Jun 1992 | pmid = 1577491 | pmc =  | doi =10.1016/0888-7543(92)90237-M }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CLC Charcot-Leyden crystal protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1178| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CLC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g86.
| PDB = {{PDB2|1g86}}, {{PDB2|1hdk}}, {{PDB2|1lcl}}, {{PDB2|1qkq}}
| Name = Charcot-Leyden crystal protein
| HGNCid = 2014
| Symbol = CLC
| AltSymbols =; LGALS10; LPPL_HUMAN; MGC149659
| OMIM = 153310
| ECnumber = 
| Homologene = 
| MGIid = 
| GeneAtlas_image1 = PBB_GE_CLC_206207_at_tn.png
| Function = {{GNF_GO|id=GO:0004622 |text = lysophospholipase activity}} {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1178
    | Hs_Ensembl = ENSG00000105205
    | Hs_RefseqProtein = NP_001819
    | Hs_RefseqmRNA = NM_001828
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 44913736
    | Hs_GenLoc_end = 44920508
    | Hs_Uniprot = Q05315
    | Mm_EntrezGene = 
    | Mm_Ensembl =
    | Mm_RefseqmRNA =
    | Mm_RefseqProtein =
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr =
    | Mm_GenLoc_start =   
    | Mm_GenLoc_end =   
    | Mm_Uniprot = 
  }}
}}
'''Charcot-Leyden crystal protein''', also known as '''CLC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CLC Charcot-Leyden crystal protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1178| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias.<ref name="entrez">{{cite web | title = Entrez Gene: CLC Charcot-Leyden crystal protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1178| accessdate = }}</ref>
| summary_text = Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in [[eosinophil]]s and [[basophil]]s. It hydrolyzes [[lysophosphatidylcholine]] to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or [[IgE]]-binding activities. It is both structurally and functionally related to the [[galectin]] family of [[beta-galactoside]] binding proteins. It may be associated with inflammation and some myeloid leukemias.<ref name="entrez" />
}}
}}
==See also==
* [[Charcot-Leyden crystals]]


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CLC}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Gleich GJ, Loegering DA, Mann KG, Maldonado JE |title=Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils. |journal=J. Clin. Invest. |volume=57 |issue= 3 |pages= 633-40 |year= 1976 |pmid= 942977 |doi=  }}
*{{cite journal  | vauthors=Gleich GJ, Loegering DA, Mann KG, Maldonado JE |title=Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils |journal=J. Clin. Invest. |volume=57 |issue= 3 |pages= 633–40 |year= 1976 |pmid= 942977 |doi=10.1172/JCI108319  | pmc=436696 }}
*{{cite journal  | author=Golightly LM, Thomas LL, Dvorak AM, Ackerman SJ |title=Charcot-Leyden crystal protein in the degranulation and recovery of activated basophils. |journal=J. Leukoc. Biol. |volume=51 |issue= 4 |pages= 386-92 |year= 1992 |pmid= 1373430 |doi=  }}
*{{cite journal  | vauthors=Golightly LM, Thomas LL, Dvorak AM, Ackerman SJ |title=Charcot-Leyden crystal protein in the degranulation and recovery of activated basophils |journal=J. Leukoc. Biol. |volume=51 |issue= 4 |pages= 386–92 |year= 1992 |pmid= 1373430 |doi=  }}
*{{cite journal  | author=Mastrianni DM, Eddy RL, Rosenberg HF, ''et al.'' |title=Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. |journal=Genomics |volume=13 |issue= 1 |pages= 240-2 |year= 1992 |pmid= 1577491 |doi=  }}
*{{cite journal  | author=Dvorak AM |title=Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) and peroxidase in macrophages, eosinophils, and extracellular matrix of the skin in the hypereosinophilic syndrome |journal=Lab. Invest. |volume=62 |issue= 5 |pages= 590–607 |year= 1990 |pmid= 2160562 |doi=  |name-list-format=vanc| author2=Weller PF | author3=Monahan-Earley RA | display-authors=3  | last4=Letourneau  | first4=L  | last5=Ackerman  | first5=SJ  }}
*{{cite journal  | author=Dvorak AM, Weller PF, Monahan-Earley RA, ''et al.'' |title=Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) and peroxidase in macrophages, eosinophils, and extracellular matrix of the skin in the hypereosinophilic syndrome. |journal=Lab. Invest. |volume=62 |issue= 5 |pages= 590-607 |year= 1990 |pmid= 2160562 |doi=  }}
*{{cite journal | vauthors=Dvorak AM, Letourneau L, Weller PF, Ackerman SJ |title=Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) to intracytoplasmic crystals in tumor cells of primary solid and papillary epithelial neoplasm of the pancreas |journal=Lab. Invest. |volume=62 |issue= 5 |pages= 608–15 |year= 1990 |pmid= 2160563 |doi=  }}
*{{cite journal  | author=Dvorak AM, Letourneau L, Weller PF, Ackerman SJ |title=Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) to intracytoplasmic crystals in tumor cells of primary solid and papillary epithelial neoplasm of the pancreas. |journal=Lab. Invest. |volume=62 |issue= 5 |pages= 608-15 |year= 1990 |pmid= 2160563 |doi=  }}
*{{cite journal  | vauthors=Dvorak AM, Ackerman SJ |title=Ultrastructural localization of the Charcot-Leyden crystal protein (lysophospholipase) to granules and intragranular crystals in mature human basophils |journal=Lab. Invest. |volume=60 |issue= 4 |pages= 557–67 |year= 1989 |pmid= 2709814 |doi=10.1111/1523-1747.ep12703656 }}
*{{cite journal  | author=Dvorak AM, Ackerman SJ |title=Ultrastructural localization of the Charcot-Leyden crystal protein (lysophospholipase) to granules and intragranular crystals in mature human basophils. |journal=Lab. Invest. |volume=60 |issue= 4 |pages= 557-67 |year= 1989 |pmid= 2709814 |doi= }}
*{{cite journal  | author=Sieker LC |title=Crystallographic characterization of human eosinophil Charcot-Leyden crystals |journal=J. Mol. Biol. |volume=204 |issue= 2 |pages= 489–91 |year= 1989 |pmid= 3221396 |doi=10.1016/0022-2836(88)90590-6 |name-list-format=vanc| author2=Turley S | author3=Le Trong I | display-authors=3  | last4=Stenkamp  | first4=R  | last5=Weller  | first5=P  | last6=Ackerman  | first6=S }}
*{{cite journal | author=Sieker LC, Turley S, Le Trong I, ''et al.'' |title=Crystallographic characterization of human eosinophil Charcot-Leyden crystals. |journal=J. Mol. Biol. |volume=204 |issue= 2 |pages= 489-91 |year= 1989 |pmid= 3221396 |doi=  }}
*{{cite journal  | vauthors=Weller PF, Bach D, Austen KF |title=Human eosinophil lysophospholipase: the sole protein component of Charcot-Leyden crystals |journal=J. Immunol. |volume=128 |issue= 3 |pages= 1346–9 |year= 1982 |pmid= 6173432 |doi=  }}
*{{cite journal  | author=Weller PF, Bach D, Austen KF |title=Human eosinophil lysophospholipase: the sole protein component of Charcot-Leyden crystals. |journal=J. Immunol. |volume=128 |issue= 3 |pages= 1346-9 |year= 1982 |pmid= 6173432 |doi=  }}
*{{cite journal  | vauthors=Weller PF, Bach DS, Austen KF |title=Biochemical characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase) |journal=J. Biol. Chem. |volume=259 |issue= 24 |pages= 15100–5 |year= 1985 |pmid= 6511787 |doi=  }}
*{{cite journal  | author=Weller PF, Bach DS, Austen KF |title=Biochemical characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). |journal=J. Biol. Chem. |volume=259 |issue= 24 |pages= 15100-5 |year= 1985 |pmid= 6511787 |doi=  }}
*{{cite journal  | author=Gomolin HI |title=Human eosinophil Charcot-Leyden crystal protein: cloning and characterization of a lysophospholipase gene promoter |journal=Blood |volume=82 |issue= 6 |pages= 1868–74 |year= 1993 |pmid= 8400237 |doi=  |name-list-format=vanc| author2=Yamaguchi Y | author3=Paulpillai AV  | display-authors=3  | last4=Dvorak  | first4=LA  | last5=Ackerman  | first5=SJ  | last6=Tenen  | first6=DG  }}
*{{cite journal  | author=Gomolin HI, Yamaguchi Y, Paulpillai AV, ''et al.'' |title=Human eosinophil Charcot-Leyden crystal protein: cloning and characterization of a lysophospholipase gene promoter. |journal=Blood |volume=82 |issue= 6 |pages= 1868-74 |year= 1993 |pmid= 8400237 |doi=  }}
*{{cite journal  | author=Ackerman SJ |title=Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily |journal=J. Immunol. |volume=150 |issue= 2 |pages= 456–68 |year= 1993 |pmid= 8419478 |doi=  |name-list-format=vanc| author2=Corrette SE  | author3=Rosenberg HF  | display-authors=3 | last4=Bennett  | first4=JC  | last5=Mastrianni  | first5=DM  | last6=Nicholson-Weller | first6=A | last7=Weller  | first7=PF  | last8=Chin  | first8=DT  | last9=Tenen  | first9=DG  }}
*{{cite journal | author=Ackerman SJ, Corrette SE, Rosenberg HF, ''et al.'' |title=Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. |journal=J. Immunol. |volume=150 |issue= 2 |pages= 456-68 |year= 1993 |pmid= 8419478 |doi= }}
*{{cite journal | author=Leonidas DD |title=Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins |journal=Structure |volume=3 |issue= 12 |pages= 1379–93 |year= 1996 |pmid= 8747464 |doi=10.1016/S0969-2126(01)00275-1 |name-list-format=vanc| author2=Elbert BL  | author3=Zhou Z  | display-authors=3  | last4=Leffler  | first4=Hakon  | last5=Ackerman  | first5=Steven J  | last6=Acharya  | first6=K.Ravi }}
*{{cite journal  | author=Leonidas DD, Elbert BL, Zhou Z, ''et al.'' |title=Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. |journal=Structure |volume=3 |issue= 12 |pages= 1379-93 |year= 1996 |pmid= 8747464 |doi=  }}
*{{cite journal  | vauthors=Dyer KD, Handen JS, Rosenberg HF |title=The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes |journal=Genomics |volume=40 |issue= 2 |pages= 217–21 |year= 1997 |pmid= 9119387 |doi= 10.1006/geno.1996.4590 }}
*{{cite journal | author=Dyer KD, Handen JS, Rosenberg HF |title=The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. |journal=Genomics |volume=40 |issue= 2 |pages= 217-21 |year= 1997 |pmid= 9119387 |doi= 10.1006/geno.1996.4590 }}
*{{cite journal  | author=Swaminathan GJ |title=Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution |journal=Biochemistry |volume=38 |issue= 42 |pages= 13837–43 |year= 1999 |pmid= 10529229 |doi=10.1021/bi990756e  |name-list-format=vanc| author2=Leonidas DD  | author3=Savage MP  | display-authors=3  | last4=Ackerman  | first4=Steven J. | last5=Acharya  | first5=K. Ravi }}
*{{cite journal  | author=Swaminathan GJ, Leonidas DD, Savage MP, ''et al.'' |title=Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. |journal=Biochemistry |volume=38 |issue= 42 |pages= 13837-43 |year= 1999 |pmid= 10529229 |doi=  }}
*{{cite journal  | author=Larramendy ML |title=Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis |journal=Haematologica |volume=87 |issue= 6 |pages= 569–77 |year= 2003 |pmid= 12031912 |doi=  |name-list-format=vanc| author2=Niini T  | author3=Elonen E  | display-authors=3  | last4=Nagy  | first4=B  | last5=Ollila  | first5=J  | last6=Vihinen  | first6=M  | last7=Knuutila  | first7=S  }}
*{{cite journal  | author=Larramendy ML, Niini T, Elonen E, ''et al.'' |title=Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis. |journal=Haematologica |volume=87 |issue= 6 |pages= 569-77 |year= 2003 |pmid= 12031912 |doi= }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Abedin MJ |title=Potential roles of galectins in myeloid differentiation into three different lineages |journal=J. Leukoc. Biol. |volume=73 |issue= 5 |pages= 650–6 |year= 2003 |pmid= 12714580 |doi=10.1189/jlb.0402163  |name-list-format=vanc| author2=Kashio Y  | author3=Seki M  | display-authors=3  | last4=Nakamura  | first4=K  | last5=Hirashima  | first5=M  }}
*{{cite journal  | author=Abedin MJ, Kashio Y, Seki M, ''et al.'' |title=Potential roles of galectins in myeloid differentiation into three different lineages. |journal=J. Leukoc. Biol. |volume=73 |issue= 5 |pages= 650-6 |year= 2003 |pmid= 12714580 |doi=  }}
*{{cite journal  | author=Grimwood J |title=The DNA sequence and biology of human chromosome 19 |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399  |name-list-format=vanc| author2=Gordon LA  | author3=Olsen A  | display-authors=3  | last4=Terry  | first4=Astrid  | last5=Schmutz  | first5=Jeremy  | last6=Lamerdin  | first6=Jane  | last7=Hellsten  | first7=Uffe  | last8=Goodstein  | first8=David  | last9=Couronne  | first9=Olivier }}
*{{cite journal  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Nielsen K |title=Altered expression of CLC, DSG3, EMP3, S100A2, and SLPI in corneal epithelium from keratoconus patients |journal=Cornea |volume=24 |issue= 6 |pages= 661–8 |year= 2005 |pmid= 16015083 |doi=10.1097/01.ico.0000153556.59407.69  |name-list-format=vanc| author2=Heegaard S  | author3=Vorum H  | display-authors=3  | last4=Birkenkamp-Demtr??Der  | first4=Karin  | last5=Ehlers  | first5=Niels  | last6=Orntoft  | first6=Torben Falck }}
*{{cite journal  | author=Nielsen K, Heegaard S, Vorum H, ''et al.'' |title=Altered expression of CLC, DSG3, EMP3, S100A2, and SLPI in corneal epithelium from keratoconus patients. |journal=Cornea |volume=24 |issue= 6 |pages= 661-8 |year= 2005 |pmid= 16015083 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1178}}
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Revision as of 09:45, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Eosinophil lysophospholipase is an enzyme that in humans is encoded by the CLC gene.[1][2]

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias.[2]

See also

References

  1. ↑ Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ (Jun 1992). "Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14". Genomics. 13 (1): 240–2. doi:10.1016/0888-7543(92)90237-M. PMID 1577491.
  2. ↑ 2.0 2.1 "Entrez Gene: CLC Charcot-Leyden crystal protein".

External links

Further reading

  • Gleich GJ, Loegering DA, Mann KG, Maldonado JE (1976). "Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils". J. Clin. Invest. 57 (3): 633–40. doi:10.1172/JCI108319. PMC 436696. PMID 942977.
  • Golightly LM, Thomas LL, Dvorak AM, Ackerman SJ (1992). "Charcot-Leyden crystal protein in the degranulation and recovery of activated basophils". J. Leukoc. Biol. 51 (4): 386–92. PMID 1373430.
  • Dvorak AM, Weller PF, Monahan-Earley RA, et al. (1990). "Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) and peroxidase in macrophages, eosinophils, and extracellular matrix of the skin in the hypereosinophilic syndrome". Lab. Invest. 62 (5): 590–607. PMID 2160562.
  • Dvorak AM, Letourneau L, Weller PF, Ackerman SJ (1990). "Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) to intracytoplasmic crystals in tumor cells of primary solid and papillary epithelial neoplasm of the pancreas". Lab. Invest. 62 (5): 608–15. PMID 2160563.
  • Dvorak AM, Ackerman SJ (1989). "Ultrastructural localization of the Charcot-Leyden crystal protein (lysophospholipase) to granules and intragranular crystals in mature human basophils". Lab. Invest. 60 (4): 557–67. doi:10.1111/1523-1747.ep12703656. PMID 2709814.
  • Sieker LC, Turley S, Le Trong I, et al. (1989). "Crystallographic characterization of human eosinophil Charcot-Leyden crystals". J. Mol. Biol. 204 (2): 489–91. doi:10.1016/0022-2836(88)90590-6. PMID 3221396.
  • Weller PF, Bach D, Austen KF (1982). "Human eosinophil lysophospholipase: the sole protein component of Charcot-Leyden crystals". J. Immunol. 128 (3): 1346–9. PMID 6173432.
  • Weller PF, Bach DS, Austen KF (1985). "Biochemical characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase)". J. Biol. Chem. 259 (24): 15100–5. PMID 6511787.
  • Gomolin HI, Yamaguchi Y, Paulpillai AV, et al. (1993). "Human eosinophil Charcot-Leyden crystal protein: cloning and characterization of a lysophospholipase gene promoter". Blood. 82 (6): 1868–74. PMID 8400237.
  • Ackerman SJ, Corrette SE, Rosenberg HF, et al. (1993). "Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily". J. Immunol. 150 (2): 456–68. PMID 8419478.
  • Leonidas DD, Elbert BL, Zhou Z, et al. (1996). "Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins". Structure. 3 (12): 1379–93. doi:10.1016/S0969-2126(01)00275-1. PMID 8747464.
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