Lachesin: an immunoglobulin superfamily protein whose expression correlates with neurogenesis in grasshopper embryos

Development ◽  
1993 ◽  
Vol 118 (2) ◽  
pp. 509-522 ◽  
Author(s):  
R.O. Karlstrom ◽  
L.P. Wilder ◽  
M.J. Bastiani
Keyword(s):  
Fruit Fly ◽  
The Body ◽  
Developmental Expression ◽  
Immunoglobulin Superfamily ◽  
Glycosyl Phosphatidylinositol ◽  
Surface Recognition ◽  
Poliovirus Receptor ◽  
Mother Cells ◽  
Immunoglobulin Superfamily Proteins ◽  
Immunoglobulin Superfamily Protein

We describe the developmental expression in grasshopper (Schistocerca americana) and molecular characterization in grasshopper and fruit fly (Drosophila melanogaster) of Lachesin, a novel immunoglobulin superfamily protein. Lachesin is expressed on the surfaces of differentiating neuronal cells from the onset of neurogenesis in both the central and peripheral nervous systems. Lachesin expression begins in some cells of the neurogenic ectoderm immediately after engrailed expression begins in the posterior cells of each future segment. All neurogenic cells express Lachesin early, but only those cells that become neuroblasts continue to express Lachesin. Ectodermal cells in the neurogenic region that adopt non-neuronal fates lose Lachesin at the time that they diverge from a potentially neurogenic pathway. Neuroblasts, ganglion mother cells and neurons all express Lachesin early in their lives, but expression becomes restricted to a subset of neurons as development progresses. Sensory neurons express Lachesin as they delaminate from the body wall ectoderm. Lachesin is also present on growing axons of the CNS and PNS and becomes restricted to a subset of axons later in development. This expression is unique among known insect neurogenic genes and suggests a role for Lachesin in early neuronal differentiation and axon outgrowth. Grasshopper Lachesin is a 38 × 10(3) M(r) protein linked to cell membranes through a glycosyl phosphatidylinositol anchor. We have cloned the Lachesin gene from both grasshopper and fly. The proteins are highly conserved (70% identical) between the two species. Lachesin is similar to Drosophila amalgam, bovine OBCAM and the human poliovirus receptor, putting it into a subgroup of the immunoglobulin superfamily containing one V- and two C2-type immunoglobulin domains. Lachesin is also similar to several other vertebrate immunoglobulin superfamily proteins (TAG-1, F11, L1 and NgCAM) known to function in neurite outgrowth and other cell surface recognition events.

scholarly journals Early Adhesion of Candida albicans onto Dental Acrylic Surfaces

2017 ◽  
Vol 96 (8) ◽  
pp. 917-923 ◽  
Author(s):  
S. Aguayo ◽  
H. Marshall ◽  
J. Pratten ◽  
D. Bradshaw ◽  
J.S. Brown ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Clinical Isolate ◽  
Force Spectroscopy ◽  
Laboratory Strain ◽  
Culture Conditions ◽  
The Body ◽  
Yeast Cells ◽  
Adhesion Forces ◽  
Reliable Technique ◽  
Mother Cells

Denture-associated stomatitis is a common candidal infection that may give rise to painful oral symptoms, as well as be a reservoir for infection at other sites of the body. As poly (methyl methacrylate) (PMMA) remains the main material employed in the fabrication of dentures, the aim of this research was to evaluate the adhesion of Candida albicans cells onto PMMA surfaces by employing an atomic force microscopy (AFM) single-cell force spectroscopy (SCFS) technique. For experiments, tipless AFM cantilevers were functionalized with PMMA microspheres and probed against C. albicans cells immobilized onto biopolymer-coated substrates. Both a laboratory strain and a clinical isolate of C. albicans were used for SCFS experiments. Scanning electron microscopy (SEM) and AFM imaging of C. albicans confirmed the polymorphic behavior of both strains, which was dependent on growth culture conditions. AFM force-spectroscopy results showed that the adhesion of C. albicans to PMMA is morphology dependent, as hyphal tubes had increased adhesion compared with yeast cells ( P < 0.05). C. albicans budding mother cells were found to be nonadherent, which contrasts with the increased adhesion observed in the tube region. Comparison between strains demonstrated increased adhesion forces for a clinical isolate compared with the lab strain. The clinical isolate also had increased survival in blood and reduced sensitivity to complement opsonization, providing additional evidence of strain-dependent differences in Candida-host interactions that may affect virulence. In conclusion, PMMA-modified AFM probes have shown to be a reliable technique to characterize the adhesion of C. albicans to acrylic surfaces.

Lift and power requirements of hovering flight inDrosophila virilis

2002 ◽  
Vol 205 (16) ◽  
pp. 2413-2427 ◽  
Author(s):  
Mao Sun ◽  
Jian Tang
Keyword(s):  
Flight Control ◽  
Stokes Equations ◽  
Fruit Fly ◽  
The Body ◽  
Drosophila Virilis ◽  
Specific Power ◽  
Aerodynamic Forces ◽  
Hovering Flight ◽  
Power Expenditure ◽  
The Mean

SUMMARYThe lift and power requirements for hovering flight in Drosophila virilis were studied using the method of computational fluid dynamics. The Navier-Stokes equations were solved numerically. The solution provided the flow velocity and pressure fields, from which the unsteady aerodynamic forces and moments were obtained. The inertial torques due to the acceleration of the wing mass were computed analytically. On the basis of the aerodynamic forces and moments and the inertial torques, the lift and power requirements for hovering flight were obtained.For the fruit fly Drosophila virilis in hovering flight (with symmetrical rotation), a midstroke angle of attack of approximately 37°was needed for the mean lift to balance the insect weight, which agreed with observations. The mean drag on the wings over an up- or downstroke was approximately 1.27 times the mean lift or insect weight (i.e. the wings of this tiny insect must overcome a drag that is approximately 27 % larger than its weight to produce a lift equal to its weight). The body-mass-specific power was 28.7 W kg-1, the muscle-mass-specific power was 95.7 W kg-1 and the muscle efficiency was 17 %.With advanced rotation, larger lift was produced than with symmetrical rotation, but it was more energy-demanding, i.e. the power required per unit lift was much larger. With delayed rotation, much less lift was produced than with symmetrical rotation at almost the same power expenditure; again, the power required per unit lift was much larger. On the basis of the calculated results for power expenditure, symmetrical rotation should be used for balanced, long-duration flight and advanced rotation and delayed rotation should be used for flight control and manoeuvring. This agrees with observations.

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

scholarly journals Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Shouqiang Cheng ◽  
James Ashley ◽  
Justyna D Kurleto ◽  
Meike Lobb-Rabe ◽  
Yeonhee Jenny Park ◽  
...  
Keyword(s):  
Axon Guidance ◽  
Molecular Basis ◽  
Surface Proteins ◽  
Synaptic Connectivity ◽  
Immunoglobulin Superfamily ◽  
Neuronal Connectivity ◽  
Cell Surface Proteins ◽  
Synaptic Specificity ◽  
Immunoglobulin Superfamily Proteins ◽  
Synapse Targeting

In stereotyped neuronal networks, synaptic connectivity is dictated by cell surface proteins, which assign unique identities to neurons, and physically mediate axon guidance and synapse targeting. We recently identified two groups of immunoglobulin superfamily proteins in Drosophila, Dprs and DIPs, as strong candidates for synapse targeting functions. Here, we uncover the molecular basis of specificity in Dpr–DIP mediated cellular adhesions and neuronal connectivity. First, we present five crystal structures of Dpr–DIP and DIP–DIP complexes, highlighting the evolutionary and structural origins of diversification in Dpr and DIP proteins and their interactions. We further show that structures can be used to rationally engineer receptors with novel specificities or modified affinities, which can be used to study specific circuits that require Dpr–DIP interactions to help establish connectivity. We investigate one pair, engineered Dpr10 and DIP-α, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring.

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 Chimeric Nectin1-Poliovirus Receptor Molecules Identify a Nectin1 Region Functional in Herpes Simplex Virus Entry

2001 ◽  
Vol 75 (17) ◽  
pp. 7987-7994 ◽  
Author(s):  
Francesca Cocchi ◽  
Marc Lopez ◽  
Patrice Dubreuil ◽  
Gabriella Campadelli Fiume ◽  
Laura Menotti
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Entry ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Immunoglobulin Superfamily ◽  
Binding Studies ◽  
Entry Site ◽  
Poliovirus Receptor ◽  
Simplex Virus

ABSTRACT Human nectin1 (hNectin1), an adhesion molecule belonging to the nectin family of the immunoglobulin superfamily, mediates entry of herpes simplex virus (HSV) into cells. The hNectin1 domain that mediates virus entry into cells and also binds glycoprotein D (gD) has been localized to the first N-terminal V-type domain. The poliovirus receptor (PVR) is a structural homolog to nectins, but it cannot function as an HSV entry receptor. hNectin1-PVR chimeras were constructed to functionally locate the site on hNectin1 involved in HSV entry (HSV entry site). The epitope recognized by monoclonal antibody (MAb) R1.302, which is able to block HSV entry, was also located. The chimeric receptors were designed to preserve the overall structure of the V domain. The HSV entry activity mapped entirely to the hNectin1 portion located between residues 64 and 94 (64-94), likely to encode the C, C′, and C" β-strands and intervening loops. In turn, this site consisted of two portions: one with low-level basal activity for HSV entry (77-94), and one immediately upstream (residues 64 to 76) which greatly enhanced the HSV entry activity of the downstream region. The gD-binding site mapped substantially to the same site, whereas the MAb R1.302 epitope also required a further downstream portion (95-102). The involvement of the 64-76 portion is at difference with previous indirect mapping results that were based on competitive binding studies (C. Krummenacher et al., J. Virol. 74:10863–10872, 2000). The A, A′, B, D, E, F, and G β-strands and intervening loops did not appear to play any role in HSV entry. According to the predicted three-dimensional structure of PVR, the C C′ C" site is located peripherally in the V domain and very likely represents an accessible portion at the cell surface.

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.

Sign in / Sign up

Export Citation Format

Share Document