A positional marker for the dorsal embryonic retina is homologous to the high-affinity laminin receptor

Development ◽  
1990 ◽  
Vol 109 (3) ◽  
pp. 521-531 ◽  
Author(s):  
S.A. Rabacchi ◽  
R.L. Neve ◽  
U.C. Drager
Keyword(s):  
Positional Information ◽  
Laminin Receptor ◽  
Western Blots ◽  
Selective Labeling ◽  
Positional Marker ◽  
Spacer Arm ◽  
High Degree ◽  
Embryonic Retina ◽  
Dorsal Retina ◽  
Laminin Binding

In a search for determinants of positional information in the embryonic eye, we isolated two monoclonal antibodies that label strongly the dorsal part of the undifferentiated embryonic retina in mammals, bird and cold-blooded vertebrates. In the chick, the optic tectum is labeled in a corresponding fashion, the ventral tectum more heavily than the dorsal tectum. Through biochemical and molecular analysis both antibodies were found to recognize a protein that has been cloned repeatedly, first in a screen with antibodies to the ‘68K-laminin receptor’ (Wewer et al. (1986) Cancer Res. 47, 5691–5698), a name that may not exhaustively describe its function. Western blots show the protein to be present in most or all tissues, and Western and Southern blots reveal a high degree of conservation in the detected signals up to invertebrates and bacteria. Despite the very strong and selective labeling of the dorsal retina in conventional immunohistochemical preparations, the protein and its mRNA are present in even amounts throughout the embryonic retina, as demonstrated by Western and Northern blots of bisected retinas, and immunohistochemically in retinas fixed with ethylene glycole bissuccinimide (EGS), an NH2-group crosslinker with very long spacer arm. This indicates that the dorsoventral asymmetry in the embryonic retina is not in the amount but in the configuration of this protein; whether this difference relates to laminin binding is not known.

Genes that control dorsoventral polarity affect gene expression along the anteroposterior axis of the Drosophila embryo

Development ◽  
1987 ◽  
Vol 99 (3) ◽  
pp. 327-332 ◽  
Author(s):  
S.B. Carroll ◽  
G.M. Winslow ◽  
V.J. Twombly ◽  
M.P. Scott
Keyword(s):  
Gene Expression ◽  
Cell Fate ◽  
Maternal Effect ◽  
Positional Information ◽  
Drosophila Embryo ◽  
Dorsoventral Polarity ◽  
Anteroposterior Axis ◽  
Positional Marker ◽  
Control Pattern ◽  
The Relationship

At least 13 genes control the establishment of dorsoventral polarity in the Drosophila embryo and more than 30 genes control the anteroposterior pattern of body segments. Each group of genes is thought to control pattern formation along one body axis, independently of the other group. We have used the expression of the fushi tarazu (ftz) segmentation gene as a positional marker to investigate the relationship between the dorsoventral and anteroposterior axes. The ftz gene is normally expressed in seven transverse stripes. Changes in the striped pattern in embryos mutant for other genes (or progeny of females homozygous for maternal-effect mutations) can reveal alterations of cell fate resulting from such mutations. We show that in the absence of any of ten maternal-effect dorsoventral polarity gene functions, the characteristic stripes of ftz protein are altered. Normally there is a difference between ftz stripe spacing on the dorsal and ventral sides of the embryo; in dorsalized mutant embryos the ftz stripes appear to be altered so that dorsal-type spacing occurs on all sides of the embryo. These results indicate that cells respond to dorsoventral positional information in establishing early patterns of gene expression along the anteroposterior axis and that there may be more significant interactions between the different axes of positional information than previously determined.

scholarly journals Isolation of a laminin-binding protein from the protozoan parasite Leishmania donovani that may mediate cell adhesion

1999 ◽  
Vol 337 (3) ◽  
pp. 551-558 ◽  
Author(s):  
Abhijit GHOSH ◽  
Keya BANDYOPADHYAY ◽  
Labanyamoy KOLE ◽  
Pijush K. DAS
Keyword(s):  
Leishmania Donovani ◽  
Biochemical Characterization ◽  
Binding Protein ◽  
Outer Membrane Proteins ◽  
Deae Cellulose ◽  
Integral Membrane Protein ◽  
Mononuclear Phagocytes ◽  
Laminin Receptor ◽  
Laminin Binding Protein ◽  
Laminin Binding

Extracellular matrix (ECM)-binding proteins on the surface of Leishmania are thought to play a crucial role in the onset of leishmaniasis, as these parasites invade mononuclear phagocytes in various organs after migrating through the ECM. In a previous report, we presented several lines of evidence suggesting that Leishmania has a specific receptor for laminin, a major ECM protein, with a Kd in the nanomolar range. Here we describe the identification, purification and biochemical characterization of the Leishmania laminin receptor. When the outer membrane proteins of L. donovani were blotted on to nitrocellulose paper and probed with laminin, a prominent laminin-binding protein of 67 kDa was identified. The purified protein was isolated by a three-step process involving DEAE–cellulose, Con A (concanavalin A)–Sepharose and laminin–Sepharose affinity chromatography and was used to raise a monospecific antibody. The same protein was obtained when parasite membrane extracts were adsorbed to antibody affinity matrix and eluted with glycine. The affinity-purified protein bound to laminin in a detergent-solubilized form as well as after integration into artificial bilayers, and was subsequently characterized as an integral membrane protein. Metaperiodate oxidation and metabolic inhibition of glycosylation studies indicate the binding protein to be glycoprotein in nature and that N-linked oligosaccharides play a part in the interaction of laminin with the binding protein. Surface-labelled parasites attached to microtitre wells coated with laminin and the 67 kDa protein blocked the adhesion to laminin substrate. We propose that the 67 kDa protein is an adhesin involved in the attachment of Leishmaniato host tissues.

scholarly journals A family of fibrinogen-binding MSCRAMMs from Enterococcus faecalis

Microbiology ◽  
2009 ◽  
Vol 155 (7) ◽  
pp. 2390-2400 ◽  
Author(s):  
Jouko Sillanpää ◽  
Sreedhar R. Nallapareddy ◽  
Janeu Houston ◽  
Vannakambadi K. Ganesh ◽  
Agathe Bourgogne ◽  
...  
Keyword(s):  
Structural Similarity ◽  
Gene Encoding ◽  
Western Blots ◽  
Fibrinogen Binding ◽  
Coated Surfaces ◽  
A Minor ◽  
Polypeptide Chains ◽  
High Degree ◽  
Dose Dependent ◽  
Reduced Adherence

We report that three (EF0089, EF2505 and EF1896, renamed here Fss1, Fss2 and Fss3, respectively, for Enterococcus faecalis surface protein) of the recently predicted MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) in E. faecalis strain V583 bind fibrinogen (Fg). Despite an absence of extensive primary sequence homology, the three proteins appear to be related structurally. Within the N-terminal regions of the three enterococcal proteins, we identified pairs of putative IgG-like modules with a high degree of predicted structural similarity to the Fg-binding N2 and N3 domains of the staphylococcal MSCRAMMs ClfA and SdrG. A second N2N3-like segment was predicted in Fss1. Far-UV circular dichroism spectroscopy revealed that all four predicted N2N3-like regions are composed mainly of β-sheets with only a minor proportion of α-helices, which is characteristic of Ig-like folded domains. Three of the four identified enterococcal N2N3-like regions showed potent dose-dependent binding to Fg. However, the specificity of the Fg-binding MSCRAMMs differs, as indicated by far-Western blots, which showed that recombinant segments of the MSCRAMMs bound different Fg polypeptide chains. Enterococci grown in serum-supplemented broth adhere to Fg-coated surfaces, and inactivation in strain OG1RF of the gene encoding Fss2 resulted in reduced adherence, whilst complementation of the mutant restored full Fg adherence. Thus, E. faecalis contains a family of MSCRAMMs that structurally and functionally resemble the Fg-binding MSCRAMMs of staphylococci.

scholarly journals The Regional Specific Alterations in BBB Permeability are Relevant to the Differential Responses of 67-kDa LR Expression in Endothelial Cells and Astrocytes Following Status Epilepticus

2019 ◽  
Vol 20 (23) ◽  
pp. 6025 ◽  
Author(s):  
Hana Park ◽  
Tae-Cheon Kang
Keyword(s):  
Status Epilepticus ◽  
Vasogenic Edema ◽  
Molecular Layer ◽  
Piriform Cortex ◽  
Laminin Receptor ◽  
Edema Formation ◽  
Western Blots ◽  
Expression Levels ◽  
Prolonged Seizure ◽  
Hippocampus Proper

Status epilepticus (a prolonged seizure activity, SE) differently affects vasogenic edema formation and dystrophin-aquaporin 4 (AQP4) expressions between the rat hippocampus and the piriform cortex (PC). In the present study, we explored whether the 67-kDa laminin receptor (LR) expression was relevant to the regional specific susceptibility of vasogenic edema at 3 days after SE. In spite of no difference in expression levels of 67-kDa LR, dystrophin, and AQP4 under physiological conditions, SE-induced serum extravasation was more severe in the PC than the hippocampus. Western blots demonstrated that SE reduced expression levels of 67-kDa LR, dystrophin, and AQP4 in the PC, but not in the hippocampus proper. Immunofluorescent studies revealed that SE increased 67-kDa LR expression in reactive CA1 astrocyte, but reduced it in the PC and the molecular layer of the dentate gyrus due to massive astroglial loss. Furthermore, SE decreased expressions of endothelial 67-kDa LR and SMI-71 (endothelial brain barrier antigen) in these regions. The 67-kDa LR neutralization evoked serum extravasation in these regions of normal animals without astroglial loss. Similar to SE, 67-kDa LR neutralization also reduced dystrophin-AQP4 expressions in the PC more than the total hippocampus. Furthermore, 67-kDa LR IgG infusion increased phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2), but not c-Jun N-terminal kinase, independent of phosphoprotein enriched in astrocytes of 15 kDa (PEA15) activity. Co-treatment of U0126 (an ERK1/2 inhibitor) alleviated vasogenic edema formation and the reduced dystrophin-AQP4 expressions induced by 67-kDa LR neutralization. The 67-kDa LR IgG infusion also increased the susceptibility to SE induction. Therefore, our findings suggested that the cellular specific alterations in 67-kDa LR expression might be involved in the severity of SE-induced vasogenic edema formation in regional specific manners, which might affect the susceptibility to SE induction.

scholarly journals siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis

2008 ◽  
Vol 13 (3) ◽  
Author(s):  
Tharinee Susantad ◽  
Duncan Smith
Keyword(s):  
Critical Role ◽  
Annexin V ◽  
Laminin Receptor ◽  
Strongly Correlated ◽  
Over Expression ◽  
High Affinity ◽  
Propidium Iodide Staining ◽  
Hep3b Cells ◽  
Laminin Binding Protein ◽  
Laminin Binding

AbstractThe laminin-binding protein, variously called the 37/67-kDa high affinity laminin receptor or p40, mediates the attachment of normal cells to the laminin network, and also has a role as a ribosomal protein. Over-expression of this protein has been strongly correlated with the metastatic phenotype. However, few studies have investigated the cellular consequence of the ablation of this gene’s expression. To address this issue, the expression of the 37/67-kDa high affinity laminin receptor was knocked out with several siRNA constructs via RNA interference in transformed liver (Hep3B) cells. In each case where the message was specifically ablated, apoptosis was induced, as determined by annexin V/propidium iodide staining, and by double staining with annexin V and an antibody directed against the 37/67-kDa high affinity laminin receptor. These results suggest that this protein plays a critical role in maintaining cell viability.

Aldehyde dehydrogenase is a positional marker in the retina

Development ◽  
1991 ◽  
Vol 112 (3) ◽  
pp. 693-702 ◽  
Author(s):  
P. McCaffery ◽  
P. Tempst ◽  
G. Lara ◽  
U.C. Drager
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Adult Mouse ◽  
Mouse Retina ◽  
Retinal Position ◽  
Embryonic Mouse ◽  
Undifferentiated Cells ◽  
Positional Marker ◽  
Optic Axons ◽  
Asymmetrically Distributed ◽  
Dorsal Retina

An asymmetrically distributed protein in the embryonic mouse retina was identified as an aldehyde dehydrogenase through protein microsequencing. It was characterized as a cytosolic isoform with basic isoelectric point and preference for aliphatic substrates, features that resemble those of the isoform AHD-2 which is known to oxidize retinaldehyde to retinoic acid. Immunohistochemistry with aldehyde dehydrogenase antisera showed strong labeling of the dorsal retina from the early eye vesicle stage into adulthood. In addition, optic axons originating from the dorsal retina were transiently labeled during their outgrowth phase. Whereas in the embryo the enzyme was expressed in undifferentiated cells and in neurons, in the retina of the adult mouse the asymmetrically distributed isoform was mainly expressed in Muller glia, with the number of labeled glial cells varying with retinal position.

Extracellular matrix receptors in the kidney cortex

1990 ◽  
Vol 259 (5) ◽  
pp. F783-F792 ◽  
Author(s):  
E. E. Simon ◽  
J. A. McDonald
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cells ◽  
Human Kidney ◽  
Positional Information ◽  
Laminin Receptor ◽  
Kidney Cortex ◽  
Alpha Subunits ◽  
Laminin Receptors ◽  
Tubule Cells ◽  
Receptor Distribution

Extracellular matrix (ECM) receptors anchor cells to substratum and impart positional information to cells. Within the group of ECM receptors known as integrins, alpha-subunits of these alpha beta heterodimers define ligand specificity, whereas beta-subunits define the subclass. We used immunofluorescence with anti-ECM receptor antibodies to examine distribution within human kidney cortex of all known alpha-subunits in the beta 1 subclass of integrins as well as a non-integrin 67-kDa elastin/lamin receptor. The alpha 1-subunit (alpha 1 beta 1 defines a collagen receptor) was present in mesangium and base of all tubule epithelial cells; alpha 2 (collagen) was present in mesangium and in distal but not proximal tubule cells; alpha 3 (collagen, laminin, fibronectin) was diffusely distributed within glomeruli but tubule staining was less intense; alpha 4 (fibronectin) was absent; alpha 5 (fibronectin) was present in blood vessels; and alpha 6 (laminin) was present along basolateral aspect of all tubule cells but absent in glomeruli. The elastin/laminin receptor was present in all tubule epithelial cells, but staining was heavier in distal tubules, especially intercalated cells. Thus striking heterogeneity in ECM receptor distribution was noted. For collagen receptors, differences in tubule staining were pronounced. Despite the presence of laminin within both glomeruli and tubules, laminin receptors also showed marked differences in staining between these structures. Both differences in ECM structure and intrinsic differences among different cells may underlie these differences in ECM receptor distribution.

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