Sequence and expression of a rat cDNA for LECAM-1

Watanabe, Toshiki; Song, Yuru; Hirayama, Youko; Tamatani, Takuya; Kuida, Keisuke; Miyasaka, Masayuki

doi:10.1016/0167-4781(92)90033-v

Cited by 26 publications

(13 citation statements)

References 11 publications

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“…Rat L-selectin cDNA [33], human E-selectin cDNA [27], and human P-selectin cDNA [34] were generously provided by Drs. T. Watanabe (Institute of Medical Science, University of Tokyo, Tokyo), T. K. Kishimoto (Boehringer Ingelheim), and T. Tsuji (Faculty of Pharmaceutical Sciences, Hoshi University, Tokyo), respectively.…”

Section: Construction Of Rat L-selectin and Human E-or Pselectin Chimmentioning

confidence: 99%

Characterization of an apparently conserved epitope in E- and P-selectin identified by dual-specific monoclonal antibodies

et al. 1999

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E-and P-selectin recognize a wide and overlapping range of oligosaccharide ligands including sialyl-Lewis X (sLeX) through their highly homologous C-type lectin domains. We report that an epitope apparently conserved between E-and P-selectin is functionally involved in ligand recognition although distantly located from the conventional carbohydrate binding site. We found that a previously established anti-E-selectin monoclonal antibody (mAb), 1.2B6, is cross-reactive with P-selectin, and that the 1.2B6 epitope is in the C-type lectin domain and identical to or overlapping with an epitope recognized by other independently established anti-E-and P-selectin dual-specific mAb. The epitope has been mapped by others to a region distant from the previously identified carbohydrate binding site of E-selectin in its three-dimensional structure. Nevertheless, it is of note that all dual-specific mAb, including 1.2B6, inhibited E-or P-selectin-mediated cell adhesion and also binding to sLeX. Engagement of the apparently conserved epitope by the dual-specific mAb may lead to inhibition of the ligand binding ability of E-and P-selectin by a previously uncharacterized mechanism(s) rather than by direct inhibition of sLeX binding to the hitherto identified ligand binding site.

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Section: Construction Of Rat L-selectin and Human E-or Pselectin Chimmentioning

confidence: 99%

Characterization of an apparently conserved epitope in E- and P-selectin identified by dual-specific monoclonal antibodies

et al. 1999

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“…A plasmid of L-selectin cDNA (pCEV-LS8) (25) and hamster monoclonal anti-selectin antibody (26) were used as a positive control because L-selectin is a cell surface protein. Two days after transfection, the exponentially growing number of cells were incubated with mAb 6A22 followed by fluorescein isothiocyanate-conjugated rabbit antimouse IgG.…”

Section: Isolation Of a Cdna Of Rat Binp-binding Protein Recognized Bmentioning

confidence: 99%

Identification and Molecular Cloning of a Novel Brain-specific Receptor Protein That Binds to Brain Injury-derived Neurotrophic Peptide

Hama¹,

Maruyama²,

Katoh‐Semba³

et al. 2001

Journal of Biological Chemistry

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Brain injury-derived neurotrophic peptide (BINP) is a synthetic 13-mer peptide that supports neuronal survival and protects hippocampal neurons in primary cultures from cell death caused by glutamate. We have developed a monoclonal antibody named mAb 6A22 against the 40-kDa BINP-binding protein, p40BBP. mAb 6A22 inhibits binding between BINP and rat brain synaptosomes and abolishes the protective effect of BINP. The antigen of mAb 6A22 should be the BINP-binding protein that mediates the neuroprotective action of BINP. Using an expression cloning approach with mAb 6A22, we isolated a cDNA encoding a novel receptor protein that shows binding activity of BINP. COS7 cells transfected with the cloned cDNA show binding of BINP and cell surfaces that are stained by 6A22. The mRNA for p40BBP is specific for the rat brain and is increased after birth. From immunohistochemical studies using mAb 6A22, p40BBP increased after kainic acid treatment in rat hippocampal neurons.The normal functioning of the central nervous system presupposes well balanced interactions between different biochemically and structurally linked neuronal systems. Several proteins support neuronal survival and activities. Recently, some researchers have indicated that the central nervous system has the potential for partial recovery from injury. Neurotrophic factors play important roles in the maintenance of neuronal survival and normal brain function in the central nervous system (1), with much evidence indicating that a lack of neurotrophic factor(s) causes cell death. Furthermore, various studies have indicated that neurotrophic factor(s) may protect the nervous system from cell death initiated by disease or injury. Recently, many kinds of neurotrophic factors have been found and identified in the central nervous system, while some have been only newly discovered and are still to be characterized. Neurotrophic factors are produced by various kinds of cells, depending on the developmental stage, and some are increased at the sites of injury (2-8). It is therefore hoped that neurotrophic factors may have a possible therapeutic role in degenerative diseases of the nervous system (9). Understanding how neurons die and how neurotrophic factors prevent this cell death may be helpful for the development of clinically useful compounds. In the case of nerve growth factor, the receptors are TrkA and p75 (10). Nerve growth factor induces cell death in some cells that express only p75 (11-14); however, it supports the survival of neurons that express both TrkA and p75 (15-18). Receptor studies are necessary to elucidate the functions of these factors. Other kinds of receptors, such as G-protein-coupled receptor proteins, also exist in the brain. These receptor proteins are coupled to signal cascades and have biological functions (19,20).We have been studying neuronal survival using a 13-mer brain injury-derived neurotrophic peptide (BINP).1 BINP enhances the survival of cholinergic and mesencephalic dopaminergic neurons in cultures from P14 rats (21). It also ...

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“…Thus, L-selectin was first known as the 'peripheral lymph node homing receptor', and was initially identified by monoclonal antibodies to murine and rat lymphocytes which blocked the capacity of the cells to attach to HEV in vitro and the ability of lymphocytes to specifically migrate to these peripheral lymphoid tissues in vivo [10]. The definitive identification of the 'homing receptor' as a member of the selectin molecules was made by cloning in the late 1980s, and full-length cDNA clones encoding Lselectin have been characterized and sequenced from a variety of mammals including humans [11][12][13][14], mice [15,16] and rats [17,18]. For each of the species, the predicted coding region is 372 amino acids, which includes a 38-residue leader sequence, a 23-residue C-terminal hydrophobic membrane insertion region and a 17-residue cyto plasmic tail.…”

Section: The Physiology Of L-selectinmentioning

confidence: 99%

Expression of an L-Selectin Ligand on Hematopoietic Progenitor Cells

Sackstein

1997

Acta Haematol

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The process of hematopoiesis is dependent on discrete cell-cell and cell-matrix interactions which are tightly regulated by expression of adhesion molecules. L-selectin, an adhesion protein best known for regulating leukocyte attachment to endothelium, is characteristically expressed on the earliest hematopoietic progenitor cells. Ligands for L-selectin have been extensively characterized on endothelial cells. We recently identified a ligand for L-selectin expressed on the human hematopoietic progenitor cell line KG1a. This molecule is an integral membrane glycoprotein which is structurally different from all ligands previously described. We hypothesize that this molecule may mediate L-selectin-specific adhesive interactions during hematopoiesis. This article discusses the biology of L-selectin and its ligands, and reviews our current understanding of the structure and distribution of the L-selectin ligand expressed on hematopoietic cells.

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Sequence and expression of a rat cDNA for LECAM-1

Cited by 26 publications

References 11 publications

Characterization of an apparently conserved epitope in E- and P-selectin identified by dual-specific monoclonal antibodies

Characterization of an apparently conserved epitope in E- and P-selectin identified by dual-specific monoclonal antibodies

Identification and Molecular Cloning of a Novel Brain-specific Receptor Protein That Binds to Brain Injury-derived Neurotrophic Peptide

Expression of an L-Selectin Ligand on Hematopoietic Progenitor Cells

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