title: Identification of SAF-2, a novel siglec expressed on eosinophils, mast cells, and basophils.
abstract: BACKGROUND
  Eosinophils, basophils, and mast cells are believed to be the central tenet cells in allergic conditions including allergic rhinitis, asthma, and eczema. The molecular mechanisms underlying the recruitment of these cells to sites of allergic inflammation are poorly understood.
  
  
  OBJECTIVE
  Our aim was to identify a common adhesion molecule that could potentially be responsible for mediating the recruitment of the allergic cell types to the lungs and other sites of allergy.
  
  
  METHODS
  We have cloned a sialoadhesin molecule from a human eosinophil library with the use of expressed sequence tag technology and characterized its expression on allergic cells by the use of flow cytometry and specific mAbs.
  
  
  RESULTS
  With the use of expressed sequence tag sequencing, we have identified a novel siglec molecule, SAF-2. SAF-2 has homology with other sialoadhesin family members (CD33 and siglec-5) and belongs to a subgroup of the Ig superfamily. SAF-2 is a 431-amino acid protein composed of 3 Ig domains with a 358-amino acid extracellular domain and a 47-amino acid tail. SAF-2 is highly restricted to eosinophils, basophils, and mast cells. Antibodies to SAF-2 do not modulate Ca(++) mobilization or chemotaxis of human eosinophils induced by eotaxin.
  
  
  CONCLUSIONS
  SAF-2 is a highly restricted sialoadhesin molecule, which may be useful in the detection and/or modulation of allergic cells.
authors.affiliation: Department of Immunology, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406, USA.
authors.forename: K K
authors.initials: KK
authors.lastname: Kikly
authors.forename: B S
authors.initials: BS
authors.lastname: Bochner
authors.forename: S D
authors.initials: SD
authors.lastname: Freeman
authors.forename: K B
authors.initials: KB
authors.lastname: Tan
authors.forename: K T
authors.initials: KT
authors.lastname: Gallagher
authors.forename: K J
authors.initials: KJ
authors.lastname: D'alessio
authors.forename: S D
authors.initials: SD
authors.lastname: Holmes
authors.forename: J A
authors.initials: JA
authors.lastname: Abrahamson
authors.forename: C L
authors.initials: CL
authors.lastname: Erickson-Miller
authors.forename: P R
authors.initials: PR
authors.lastname: Murdock
authors.forename: H
authors.initials: H
authors.lastname: Tachimoto
authors.forename: R P
authors.initials: RP
authors.lastname: Schleimer
authors.forename: J R
authors.initials: JR
authors.lastname: White
mesh_terms: D015703:Antigens, CD / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D000944:Antigens, Differentiation, B-Lymphocyte / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D000954:Antigens, Surface / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D001491:Basophils / Q000378:metabolism*; D004804:Eosinophils / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D006967:Hypersensitivity / Q000473:pathology*; D037102:Lectins; D008407:Mast Cells / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000494:pharmacology; D012333:RNA, Messenger / Q000235:genetics; D017386:Sequence Homology, Amino Acid
chemical_list: D015703:Antigens, CD; D000944:Antigens, Differentiation, B-Lymphocyte; D000954:Antigens, Surface; D037102:Lectins; D012333:RNA, Messenger; C403967:SIGLEC8 protein, human; D019158:N-Acetylneuraminic Acid