Mouse and Human SHPS-1: Molecular Cloning of cDNAs and Chromosomal Localization of Genes

Yamao, Takuji; Matozaki, Takashi; Amano, Kenji; Matsuda, Yoichi; Takahashi, Nobuaki; Ochi, Fukashi; Fujioka, Yohsuke; Kasuga, Masato

doi:10.1006/bbrc.1996.6047

Cited by 56 publications

(63 citation statements)

References 27 publications

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“…In the present study we have shown that P84 is identical to SHPS-1 (Yamao et al, 1997) and homologous to the family of SIRP-␣ and ␤ gene products described by Kharitonenkov et al (1997). Our findings, coupled with those of these other groups, suggest that P84 and related family members represent a group of proteins that potentially interact with nonreceptor tyrosine phosphatases via their cytoplasmic domains and with cellular receptors via their extracellular domains.…”

Section: Discussionsupporting

confidence: 80%

“…HSU06701 was shown to be on chromosome 20 using human -rodent somatic cell hybrids. We have recently mapped the human P84 gene to the subtelomeric region of chromosome 20, close to the polymorphic marker D20S199 (Eckert et al, 1997;Yamao et al, 1997). There is a high degree (90 -95%) of similarity between murine, rat, and human SHPS-1 (P84) amino acid sequences (Yamao et al, 1997).…”

Section: Sequence Homologiesmentioning

confidence: 99%

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The Murine P84 Neural Adhesion Molecule Is SHPS-1, a Member of the Phosphatase-Binding Protein Family

et al. 1997

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P84 is a neuronal membrane glycoprotein that promotes the attachment and neurite outgrowth of cultured murine cerebellar cells. The heterophilic adhesive properties of P84 and its localization at sites of synaptogenesis suggest that it may be involved in regulation of synapse formation or maintenance. P84 is expressed in subsets of neurons throughout the CNS. By cloning the cDNA encoding murine P84, we have discovered that this molecule is a member of a family of phosphatasebinding proteins and is identical to the murine SHPS-1 cDNA. Here we report the cloning of two alternatively spliced forms of P84 and describe its localization within the CNS by in situ hybridization.

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Section: Discussionsupporting

confidence: 80%

Section: Sequence Homologiesmentioning

confidence: 99%

The Murine P84 Neural Adhesion Molecule Is SHPS-1, a Member of the Phosphatase-Binding Protein Family

et al. 1997

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“…One signal-regulatory protein, Src homology 2 domain-containing protein tyrosine phosphatase substrate 1 (SHPS-1) [19], is also known as signalregulatory protein a1 (SIRP a1) [20], BIT (brain Iglike molecule with tyrosine-based activation motifs) [21], P84 [22], MFR (macrophage fusion receptor) [23] and MyD-1 [24]. In mice, SHPS-1 is expressed in myeloid cells, including monocytes, macrophages and DC [25].…”

Section: Introductionmentioning

confidence: 99%

Src homology 2 domain‐containing protein tyrosine phosphatase substrate 1 regulates the induction of Langerhans cell maturation

Fukunaga

Nagai

et al. 2006

Eur J Immunol

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Recently, we reported that Src homology 2 domain-containing protein tyrosine phosphatase substrate 1 (SHPS-1) plays an important role in the migration of Langerhans cells (LC). Here, we show that SHPS-1 is involved in the maturation of LC. Immunofluorescence analysis on epidermal sheets for I-A or CD86 revealed that LC maturation induced by 2,4-dinitro-1-fluorobenzene (DNFB) or by TNF-a was inhibited by pretreatment with an anti-SHPS-1 monoclonal antibody (mAb) or with CD47-Fc fusion protein, a ligand for SHPS-1. Further, FACS analysis demonstrated that I-A + LC that had emigrated from skin explants expressed CD80 or CD86, whereas CD47-Fc protein reduced CD80 high+ or CD86 high+ cells. CD47-Fc protein also reduced the upregulation of surface CD80 or CD86 by LC remaining in the skin explants. In SHPS-1 mutant mice, we observed that the up-regulation of surface CD86 and CCR7 by LC induced by DNFB as well as that of surface CD80 and CD86 by LC in skin explants was attenuated. Finally, contact hypersensitivity (CHS) response was suppressed in SHPS-1 mutant mice and in wild-type mice treated with an anti-SHPS-1 mAb. These observations indicate that SHPS-1 plays an important role in the maturation of LC ex vivo and in vivo, and that SHPS-1-CD47 interaction may negatively regulate CHS. IntroductionDC are potent antigen-presenting cells that play a crucial role in the initiation of immune responses to pathogens. Langerhans cells (LC) are specialized immature DC in the skin that reside in the suprabasal layers of the epidermis. When LC encounter exogenous antigens, including haptens and microorganisms, they capture and process them to generate MHC/peptide complexes on their surface. LC migrate from the epidermis to draining lymphoid tissues in order to initiate naive T cells and to present the MHC/peptide complexes to Correspondence: Dr. Tatsuya Horikawa, Division of Dermatology, Department of Clinical Molecular Medicine, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe, 650-0017Japan Fax:+81-78-382-6149 e-mail: thorikaw@med.kobe-u.ac.jp Received 12/1/06Revised 13/9/06 Accepted 19/10/06 [DOI 10.1002/eji.200635864] Key words: Contact hypersensitivity Á Langerhans cells Á Maturation Á Src homology 2 domaincontaining protein tyrosine phosphatase substrate 1Abbreviations: CCR7: CC chemokine receptor 7 Á CHS: contact hypersensitivity Á DNFB: 2,4-dinitro-1-fluorobenzene Á LC: Langerhans cell Á SHPS-1: Src homology 2 domaincontaining protein tyrosine phosphatase substrate 1 Á SIRP a1: signal-regulatory protein a1 and . In mice, SHPS-1 is expressed in myeloid cells, including monocytes, macrophages and DC [25]. SHPS-1 is a transmembrane glycoprotein whose extracellular domain comprises three immunoglobulin-like domains with multiple N-linked glycosylation sites, while the cytoplasmic domain of SHPS-1 contains four tyrosine residues that form two ITIM [26]. SHPS-1 was initially discovered as a tyrosine-phosphorylated transmembrane protein that binds SHP-1 or SHP-2. IAP/CD47, an integrin-associated...

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“…SIRP tyrosine phosphorylation and subsequent recruitment of SHP2 to the plasma membrane have been shown to be related to SIRP functional regulation of RTK signaling (Cambier, 1997;Kharitonenkov et al, 1997). Many isoforms of human SIRP and murine SHPS-1 proteins have been identi®ed and multiple transcripts of SIRP and SHPS-1 genes have been observed in many tissues, particularly in neural cells (Fujioka et al, 1996;Kharitonenkov et al, 1997;Yamao et al, 1997;Veillette et al, 1998;Jiang et al, 1999). Two subtypes of the SIRP protein family, containing at least 15 members, have been con®rmed (Kharitonenkov et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by Signal-Regulatory Proteins (SIRPs)

Chen

Ullrich

et al. 2000

Oncogene

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Mouse and Human SHPS-1: Molecular Cloning of cDNAs and Chromosomal Localization of Genes

Cited by 56 publications

References 27 publications

The Murine P84 Neural Adhesion Molecule Is SHPS-1, a Member of the Phosphatase-Binding Protein Family

The Murine P84 Neural Adhesion Molecule Is SHPS-1, a Member of the Phosphatase-Binding Protein Family

Src homology 2 domain‐containing protein tyrosine phosphatase substrate 1 regulates the induction of Langerhans cell maturation

Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by Signal-Regulatory Proteins (SIRPs)

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