Limitrin, a novel immunoglobulin superfamily protein localized to glia limitans formed by astrocyte endfeet

Glia ◽  
2003 ◽  
Vol 44 (3) ◽  
pp. 190-204 ◽  
Author(s):  
Tomoko Yonezawa ◽  
Aiji Ohtsuka ◽  
Teruhito Yoshitaka ◽  
Shuichi Hirano ◽  
Hiroyuki Nomoto ◽  
...  
Keyword(s):  
Immunoglobulin Superfamily ◽  
Glia Limitans ◽  
Astrocyte Endfeet ◽  
Immunoglobulin Superfamily Protein

Increased rat alveolar macrophage expression of functional iNOS induced by a Dirofilaria immitis immunoglobulin superfamily protein

Nitric Oxide ◽  
2005 ◽  
Vol 13 (4) ◽  
pp. 217-225 ◽  
Author(s):  
M. Amparo Andrade ◽  
Mar Siles-Lucas ◽  
José Luis Pérez Arellano ◽  
Cristina Pou Barreto ◽  
Basilio Valladares ◽  
...  
Keyword(s):  
Alveolar Macrophage ◽  
Dirofilaria Immitis ◽  
Immunoglobulin Superfamily ◽  
Immunoglobulin Superfamily Protein

HEMCAM/CD146 downregulates cell surface expression of (β)1 integrins

2001 ◽  
Vol 114 (10) ◽  
pp. 1847-1859 ◽  
Author(s):  
S. Alais ◽  
N. Allioli ◽  
C. Pujades ◽  
J.L. Duband ◽  
O. Vainio ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Expression ◽  
Matrix Proteins ◽  
Cell Surface Expression ◽  
Immunoglobulin Superfamily ◽  
Fibronectin Receptor ◽  
Adhesion Properties ◽  
Murine Fibroblasts ◽  
Laminin 1 ◽  
Immunoglobulin Superfamily Protein

HEMCAM/gicerin, an immunoglobulin superfamily protein, is involved in homophilic and heterophilic adhesion. It interacts with NOF (neurite outgrowth factor), a molecule of the laminin family. Alternative splicing leads to mRNAs coding for HEMCAM with a short (HEMCAM-s) or a long cytoplasmic tail (HEMCAM-l). To investigate the cellular function of these two variants, we stably transfected murine fibroblasts with either form of HEMCAM. Expression of each isoform of this protein in L cells delayed proliferation and modified their adhesion properties to purified extracellular matrix proteins. Expression of either HEMCAM-s or HEMCAM-l inhibited integrin-dependent adhesion and spreading of fibroblasts to laminin 1, showing that this phenomenon did not depend on the cytoplasmic region. By contrast, L-cell adhesion and spreading to fibronectin depended on the HEMCAM isoform expressed. Flow cytometry and immunoprecipitation studies revealed that the expression of HEMCAM downregulated expression of the laminin-binding integrins (α)3 (β)1, (α)6 (β)1 and (α)7 (β)1, and fibronectin receptor (α)5 (β)1 from the cell surface. Semi-quantitative PCR and northern blot experiments showed that the expression of (α)6 (β)1 integrin modified by HEMCAM occurred at a translation or maturation level. Thus, our data demonstrate that HEMCAM regulates fibroblast adhesion by controlling (β)1 integrin expression. http://www.biologists.com/JCS/movies/jcs1886.html

scholarly journals Transneuronal Dpr12/DIP-δ interactions facilitate compartmentalized dopaminergic innervation of Drosophila mushroom body axons

2019 ◽  
Author(s):  
Bavat Bornstein ◽  
Idan Alyagor ◽  
Victoria Berkun ◽  
Hagar Meltzer ◽  
Fabienne Reh ◽  
...  
Keyword(s):  
Mushroom Body ◽  
Immunoglobulin Superfamily ◽  
Cellular Mechanisms ◽  
Interacting Protein ◽  
Zone Formation ◽  
Unique System ◽  
Output Neurons ◽  
Subcellular Resolution ◽  
Circuit Formation ◽  
Immunoglobulin Superfamily Protein

SummaryThe mechanisms controlling wiring of neuronal networks are largely unknown. The stereotypic architecture of the Drosophila mushroom-body (MB) offers a unique system to study circuit assembly. The adult medial MB γ-lobe is comprised of a long bundle of axons that wires with specific modulatory and output neurons in a tiled manner defining five distinct zones. We found that the immunoglobulin superfamily protein Dpr12 is cell-autonomously required in γ-neurons for their developmental regrowth into the distal γ4/5 zones, where both Dpr12 and its interacting protein, DIP-δ, are enriched. DIP-δ functions in a subset of dopaminergic neurons that wire with γ-neurons within the γ4/5 zone. During metamorphosis, these dopaminergic projections arrive to the γ4/5 zone prior to γ-axons, suggesting that γ-axons extend through a prepatterned region. Thus, Dpr12/DIP-δ transneuronal interaction is required for γ4/5 zone formation. Our study sheds light onto molecular and cellular mechanisms underlying circuit formation within subcellular resolution.

Regulation by SIRPα of dendritic cell homeostasis in lymphoid tissues

Blood ◽  
2010 ◽  
Vol 116 (18) ◽  
pp. 3517-3525 ◽  
Author(s):  
Yasuyuki Saito ◽  
Hiroko Iwamura ◽  
Tetsuya Kaneko ◽  
Hiroshi Ohnishi ◽  
Yoji Murata ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Bone Marrow Cells ◽  
Regulatory Protein ◽  
Mutant Mice ◽  
Immunoglobulin Superfamily ◽  
Lymphoid Tissues ◽  
Mutant Form ◽  
Double Negative ◽  
Immunoglobulin Superfamily Protein

Abstract The molecular basis for regulation of dendritic cell (DC) development and homeostasis remains unclear. Signal regulatory protein α (SIRPα), an immunoglobulin superfamily protein that is predominantly expressed in DCs, mediates cell-cell signaling by interacting with CD47, another immunoglobulin superfamily protein. We now show that the number of CD11chigh DCs (conventional DCs, or cDCs), in particular, that of CD8−CD4+ (CD4+) cDCs, is selectively reduced in secondary lymphoid tissues of mice expressing a mutant form of SIRPα that lacks the cytoplasmic region. We also found that SIRPα is required intrinsically within cDCs or DC precursors for the homeostasis of splenic CD4+ cDCs. Differentiation of bone marrow cells from SIRPα mutant mice into DCs induced by either macrophage-granulocyte colony-stimulating factor or Flt3 ligand in vitro was not impaired. Although the accumulation of the immediate precursors of cDCs in the spleen was also not impaired, the half-life of newly generated splenic CD4+ cDCs was markedly reduced in SIRPα mutant mice. Both hematopoietic and nonhematopoietic CD47 was found to be required for the homeostasis of CD4+ cDCs and CD8−CD4−(double negative) cDCs in the spleen. SIRPα as well as its ligand, CD47, are thus important for the homeostasis of CD4+ cDCs or double negative cDCs in lymphoid tissues.

scholarly journals Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact.

1989 ◽  
Vol 8 (2) ◽  
pp. 489-495 ◽  
Author(s):  
P. R. Schofield ◽  
K. C. McFarland ◽  
J. S. Hayflick ◽  
J. N. Wilcox ◽  
T. M. Cho ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Immunoglobulin Superfamily ◽  
Cell Contact ◽  
Opioid Binding ◽  
Immunoglobulin Superfamily Protein

A novel immunoglobulin superfamily receptor (19A) related to CD2 is expressed on activated lymphocytes and promotes homotypic B-cell adhesion

2002 ◽  
Vol 361 (3) ◽  
pp. 431-436 ◽  
Author(s):  
John J. MURPHY ◽  
Paul HOBBY ◽  
Juan VILARINO-VARELA ◽  
Benjamin BISHOP ◽  
Panagiota IORDANIDOU ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
B Cell ◽  
Molecular Model ◽  
Immunoglobulin Superfamily ◽  
Activated Lymphocytes ◽  
Lymphocyte Adhesion ◽  
Cell Line Model ◽  
Specific Immunoglobulin ◽  
Immunoglobulin Superfamily Protein

A novel lymphocyte-specific immunoglobulin superfamily protein (19A) has been cloned. The predicted 335-amino-acid sequence of 19A represents a Type 1 membrane protein with homology with the CD2 family of receptors. A molecular model of the two predicted extracellular immunoglobulin-like domains of 19A has been generated using the crystal structure of CD2 as a template. In isolated lymphocytes, expression of 19A is induced by various activation stimuli, and enforced expression of the 19A gene promotes homotypic cell adhesion in a B-cell-line model. Collectively these data imply that the 19A protein plays a role in regulation of lymphocyte adhesion.

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