Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins.

Tedder, Thomas F.; Isaacs, Cary; Ernst, T J; Demetri, George D.; Adler, David A.; Disteche, Christine M.

doi:10.1084/jem.170.1.123

Cited by 280 publications

(107 citation statements)

References 26 publications

Supporting

Mentioning

105

Contrasting

Order By: Relevance

“…Construct 4. This construct, which used construct 3 as template for the PCR reactions, replaced the proximal ST sequence of the cytoplasmic domain of P-selectin in construct 3 with the corresponding sequence of L-selectin, a receptor delivered to the plasma membrane after synthesis (Tedder et al, 1989). The first PCR product began at the Hpa I site at base 723 of tissue factor and extended to base 855 of tissue factor.…”

Section: Constructsmentioning

confidence: 99%

Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway.

Disdier

Morrissey

Fugate

et al. 1992

MBoC

155

111

View full text Add to dashboard Cite

P-selectin (CD62), formerly called GMP-140 or PADGEM, is a membrane protein located in secretory storage granules of platelets and endothelial cells. To study the mechanisms responsible for the targeting of P-selectin to storage granules, we transfected its cDNA into COS-7 and CHO-Ki cells, which lack a regulated exocytic pathway, or into AtT20 cells, which are capable of regulated secretion. P-selectin was expressed on the plasma membrane of COS-7 and CHO-Kl cells but was concentrated in storage granules of AtT20 cells. Immunogold electron microscopy indicated that the electron-dense granules containing P-selectin in AtT20 cells also stored the endogenous soluble hormone ACTH. Activation of AtT20 cells with 8-Br-cAMP increased the surface expression of P-selectin, consistent with agonist-induced fusion of granule membranes with the plasma membrane. Deletion of the last 23 amino acids of the 35-residue cytoplasmic domain resulted in delivery of Pselectin to the plasma membrane of AtT20 cells. Replacement of the cytoplasmic tail of tissue factor, a plasma membrane protein, with the cytoplasmic domain of P-selectin redirected the chimeric molecule to granules. We conclude that the cytoplasmic domain of P-selectin is both necessary and sufficient for sorting of membrane proteins into the regulated pathway of secretion.

show abstract

Section: Constructsmentioning

confidence: 99%

Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway.

Disdier

Morrissey

Fugate

et al. 1992

MBoC

155

111

View full text Add to dashboard Cite

show abstract

“…The selectins mediate cell binding through interactions between their lectin-like domain and cell surface carbohydrate ligands (McEver et al, 1995;Springer & Lasky, 1991). There are two known singlebase polymorphisms in the L-selectin gene in humans, resulting in amino acid exchange from threonine to serine in the lectin domain at position 49 (Tre49Ser), and from phenylalanine to leucine in the EGF domain at position 206 (PheF206Leu, F206L) (Tedder et al, 1989). F206L has been reported to be associated with chronic renal allograft failure (Mclaren et al, 1999) and atherosclerosis (Blankenberg et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Association between the Phe206Leu polymorphism of L-selectin and brucellosis

Rafiei

Hajilooi²,

Shakib

et al. 2006

Journal of Medical Microbiology

View full text Add to dashboard Cite

Brucellosis remains a major zoonosis worldwide; therefore, better understanding of its immunology is a priority for the development of new therapeutic and vaccination strategies. Genetic factors appear to have an important role in the pathogenesis of infectious diseases such as brucellosis. Adhesion molecules, such as members of the selectin family, participate in the interaction between leukocytes and the endothelium, as well as in inflammatory cell recruitment. The impact of L-selectin polymorphisms on brucellosis has not so far been investigated. The aim of this study was to assess an L-selectin Phe206Leu (F206L) polymorphism in patients with active brucellosis, and to analyse its possible relationship with disease progression. A case-control association study was carried out on 619 subjects, including 374 patients with brucellosis and 245 age-and sex-matched healthy controls. Genomic DNA was isolated, and amplification of L-selectin genomic regions was performed by PCR incorporating sequence-specific primers (PCR-SSP) to distinguish the genotypes. The frequencies of the F206L polymorphism were studied. A significant difference in F206L polymorphism was found between patients with brucellosis and controls. The 206Leu allele was more frequent in patients than in healthy individuals (36?6 versus 28 %, P=0?003). In addition, there was an association between the presence of the 206Leu allele and a relapse of brucellosis (odds ratio 6?53, 95 % confidence interval 1?5-28?8, P=0?005). The higher frequency of L-selectin genotypes in patients with brucellosis than in control individuals, as well as the association between the 206Leu allele and the occurrence of brucellosis relapse, suggest that the F206L polymorphism could make individuals more vulnerable to brucellosis.

show abstract

“…Mammals evolved from a common ancestor *100 million years ago and all mammals have peripheral lymph nodes with differentiated HEV that are the major sites of L-selectin biological activity [5-7, 10, 29, 38]. To examine the effect of thermal stress on L-selectin adhesion, representative mammalian species were initially selected in which L-selectin had been previously identified at either the nucleic acid or protein level (human, mouse, rat, rabbit, dog and cow) [14][15][16][17][18][19][20][21]. Leukocytes isolated from peripheral blood or spleen were either maintained at normothermal temperatures or cultured for 6 h at a physiologically relevant febrile temperature (e.g.1.5-5 C above normal core temperature; see Materials and methods).…”

Section: Resultsmentioning

confidence: 99%

“…In this regard, the ligandbinding lectin domain of human, mouse, rat, rabbit, dog and cow L-selectin are predicted to have 72% amino acid identity [14][15][16][17][18][19][20][21]. Moreover, selected mAb directed against functional epitopes within the lectin domain of human L-selectin cross-react broadly with leukocytes from numerous mammalian species (monkey, rabbit, sheep, cat, guinea pig, goat, dog, pig and cow) [22,23].…”

Section: Introductionmentioning

confidence: 99%

Conservation of IL‐6 trans‐signaling mechanisms controlling L‐selectin adhesion by fever‐range thermal stress

et al. 2007

View full text Add to dashboard Cite

Fever is associated with improved survival during infection in endothermic and ectothermic species although the protective mechanisms are largely undefined. Previous studies indicate that fever-range thermal stress increases the binding activity of the L-selectin homing receptor in human or mouse leukocytes, thereby promoting trafficking to lymphoid tissues across high endothelial venules (HEV). Here, we examined the evolutionary conservation of thermal regulation of L-selectin-like adhesion. Leukocytes from animals representing four taxa of vertebrates (mammals, avians, amphibians, teleosts) were shown to mediate L-selectin-like adhesion under shear to MECA-79-reactive ligands on mouse HEV in cross-species in vitro adherence assays. L-selectin-like binding activity was markedly increased by fever-range thermal stress in leukocytes of all species examined. Comparable increases in L-selectin-like adhesion were induced by thermal stress, IL-6, or the IL-6/soluble IL-6 receptor fusion protein, hyper-IL-6. Analysis of the molecular basis of thermal regulation of L-selectinlike adhesion identified a common IL-6 trans-signaling mechanism in endotherms and ectotherms that resulted in activation of JAK/STAT signaling and was inhibited by IL-6 neutralizing antibodies or recombinant soluble gp130. Conservation of IL-6-dependent mechanisms controlling L-selectin adhesion over hundreds of millions of years of vertebrate evolution strongly suggests that this is a beneficial focal point regulating immune surveillance during febrile inflammatory responses.

show abstract

Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins.

Cited by 280 publications

References 26 publications

Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway.

Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway.

Association between the Phe206Leu polymorphism of L-selectin and brucellosis

Conservation of IL‐6 trans‐signaling mechanisms controlling L‐selectin adhesion by fever‐range thermal stress

Contact Info

Product

Resources

About