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Titolo:
The transmembrane form of the CX3CL1 chemokine fractalkine is expressed predominantly by epithelial cells in vivo
Autore:
Lucas, AD; Chadwick, N; Warren, BF; Jewell, DP; Gordon, S; Powrie, F; Greaves, DR;
Indirizzi:
Univ Oxford, Sir William Dunn Sch Pathol, Oxford OX1 3RE, England Univ Oxford Oxford England OX1 3RE n Sch Pathol, Oxford OX1 3RE, England John Radcliffe Hosp, Nuffield Dept Surg, Oxford OX3 9DU, England John Radcliffe Hosp Oxford England OX3 9DU Surg, Oxford OX3 9DU, England John Radcliffe Hosp, Dept Cellular Pathol, Oxford OX3 9DU, England John Radcliffe Hosp Oxford England OX3 9DU thol, Oxford OX3 9DU, England Radcliffe Infirm, Gastroenterol Unit, Oxford OX2 6HE, England Radcliffe Infirm Oxford England OX2 6HE ol Unit, Oxford OX2 6HE, England
Titolo Testata:
AMERICAN JOURNAL OF PATHOLOGY
fascicolo: 3, volume: 158, anno: 2001,
pagine: 855 - 866
SICI:
0002-9440(200103)158:3<855:TTFOTC>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEMBRANE-BOUND CHEMOKINE; DENDRITIC CELLS; RECEPTOR CX(3)CR1; ENDOTHELIAL-CELLS; IN-VIVO; ADHESION; IDENTIFICATION; INFLAMMATION; ACTIVATION; MONOCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Greaves, DR Univ Oxford, Sir William Dunn Sch Pathol, S Parks Rd, Oxford OX1 3RE, England Univ Oxford S Parks Rd Oxford England OX1 3RE X1 3RE, England
Citazione:
A.D. Lucas et al., "The transmembrane form of the CX3CL1 chemokine fractalkine is expressed predominantly by epithelial cells in vivo", AM J PATH, 158(3), 2001, pp. 855-866

Abstract

Fractalkine (CX3CL1) is synthesized as a type I transmembrane protein. Itsunique CX3C chemokine domain is attached to a 241-amino acid mucin stalk, a 19-amino acid transmembrane domain, and a 37-amino acid intracellular domain of unknown function. A soluble form of fractalkine can be generated by proteolytic cleavage at the base of the mucin stalk. Novel monoclonal and polyclonal antibodies that specifically recognize only the amino- or carboxyl-terminal ends of the human fractalkine molecule have revealed that epithelial cells are the predominant cell type expressing transmembrane forms of fractalkine in human skin, the tonsil, and the large intestine. Using thesespecific anti-fractalkine reagents we do not detect high-level expression of fractalkine on endothelial cells in normal or inflamed colon samples obtained from patients with Crohn's disease or ulcerative colitis. In contrastto previous reports we do not detect fractalkine expression by Langerhans cells or immature dendritic cells in mucosal-associated lymphoid tissues invivo. We show that the reagent used in previous studies, an anti-fractalkine N-terminal peptide antisera, cross-reacts with human CD84. Finally we discuss potential roles for fractalkine in constitutive leukocyte traffickingbased on its observed pattern of expression in epithelia.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 00:51:57