Intercellular adhesion molecule-4 and CD36 are implicated in the abnormal adhesiveness of sickle cell SAD mouse erythrocytes to endothelium.
BACKGROUND adhesiveness abnormal red blood cells to the endothelium has been involved in vaso-occlusive crisis of sickle cell disease. This study examines whether the SAD mouse model showed the same abnormality adhesion of red blood cells found in human sickle cell disease.
METHOD The repertoire of adhesion molecules in murine erythrocytes and bEnd.3 microvascular endothelial cells was determined by flow cytometry using monoclonal antibodies or by Western blotting. Adhesion investigated under dynamic conditions and are measured at different shear stresses.
RESULTS CD36, CD47 and adhesion molecules between blood type-4, but not Lutheran antigen / basal cell adhesion molecules, which are present in the adult mouse erythrocytes. alpha (4) beta (1) is expressed on the SAD and the wild types of reticulocytes. bEnd.3 endothelial cells express alpha (v) beta (3), alpha (4) beta (1), CD47, vascular cell adhesion molecule-1, and the Lutheran blood group antigen molecules / basal cell adhesion, but not CD36.
Red blood cell adhesion SAD are: (i) 2 to 3 times higher than the wild-type red blood cells; (Ii) a further increase in platelet activating factor-activated endothelium; (Iii) are not stimulated by epinephrine; (Iv) inhibited after treating endothelial peptides bind to reproduce one of the sequences between mouse adhesion molecule-4, or with a mon-oclonal antibodies against murine alpha (v) integrin; and (v) inhibited after pretreatment red blood cells with monoclonal antibody anti-mouse CD36. Combination treatment with an adhesion molecule-4 peptides and anti-CD36 monoclonal antibody remove excess red blood cell adhesion SAD. Phosphorylation state of adhesion between the molecules-4 and CD36 may not engage in over-the adhesiveness of erythrocytes SAD.
CONCLUSION inter adhesion molecule-4 / alpha (v) beta (3) and CD36 / thrombospondin interaction may contribute to an abnormally high adhesion of red blood cells SAD. Mouse SAD is a valuable animal model to investigate the process of adhesion of sickle cell disease.
Intercellular adhesion molecule-4 and CD36 are implicated in the abnormal adhesiveness of sickle cell SAD mouse erythrocytes to endothelium.
The globoside receptor triggers structural changes in the viral capsid B19 that facilitates virus internalization.
Globoside (Gb4Cer), Ku80 auto anti gene, and α 5 β1 integrin has been identified as a cell receptors / coreceptors for human parvovirus B19 (B19V), but their role and mechanisms of interaction with the virus largely unknown. In UT7 / Epo cells, expression Gb4Cer and CD49e ( integrin alpha – 5 ) is high, but not significant Ku80 expression. B19V colocalized with Gb4Cer and, to a lesser extent, with CD49e. However, only anti -Gb4Cer anti the body can interfere with the attachment of the virus. Only a small portion of the cell-bound viruses are internalized, while the majority became detached from the receptor. When added to cells that are not infected, the virus receptor-detached shows superior binding capacity of cells and infectivity.
B19V attachment to the cell triggers a conformational change in the capsid leads to the accessibility of the N terminus of VP1 (VP1u) to anti body, which is maintained in a separate virus-receptor. VP1u be equally accessible to anti the following entities B19V particle incubation with increasing concentrations of purified Gb4Cer. Exposure VP1u receptor-mediated internalization is crucial for the virus, because less VP1 capsids can bind cells but not internalized.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation (2). It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1 (2). The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation (2). It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1 (2). The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: Based on its helical structure, LIF (Leukemia Inhibitory Factor) is considered a member of the Interleukin-6 family of cytokines. Functionally, it has been implicated in a many physiological processes including development, hematopoiesis, bone metabolism, and inflammation. Some cell types known to express LIF include activated T cells, monocytes, astrocytes, osteoblasts, keratinocytes, regenerating skeletal muscle, mast cells, and fibroblasts.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF.
Description: Leukemia inhibitory factor (LIF) is a member of Interleukin 6 family. This protein is mainly expressed in the trophectoderm of the developing embryo, with its receptor LIFR expressed throughout the inner cell mass. LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. LIF is used in mouse embryonic stem cell culture, because that removal of LIF pushes stem cells toward differentiation, but they retain their proliferative potential or pluripotency. It is also used in phase II clinical trial, which can assist embryo implantation in women who have failed to become pregnant despite assisted reproductive technologies (ART). Mature mouse LIF shares 78 % a.a. sequence identity with Human LIF.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF. Recombinant mouse LIF produced in E. coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.86 kDa.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF. Recombinant mouse LIF produced in E. coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.86 kDa.
Description: Description of target: Leukemia inhibitory factor, or LIF, is an interleukin 6 class cytokine that affects cell growth by inhibiting differentiation. When LIF levels drop, the cells differentiate. The LIF was mapped gene to 22q11-q12.2 by Southern analysis of a series of mouse/human somatic cell hybrids and by in situ hybridization to the chromosomes of 2 normal males and some individuals with chromosomal rearrangements. The gene maps between the Philadelphia translocation BCR1 and the breakpoint of the translocation in cell line GM2324 at 22q12.2. LIF derives its name from its ability to induce the terminal differentiation of myeloid leukemic cells, thus preventing their continued growth. Other properties attributed to the cytokine include: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: <10pg/ml
Description: Description of target: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.;Species reactivity: Mouse;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.039 ng/mL
Description: Based on its helical structure, LIF (Leukemia Inhibitory Factor) is considered a member of the Interleukin-6 family of cytokines. Functionally, it has been implicated in a many physiological processes including development, hematopoiesis, bone metabolism, and inflammation. Some cell types known to express LIF include activated T cells, monocytes, astrocytes, osteoblasts, keratinocytes, regenerating skeletal muscle, mast cells, and fibroblasts.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF.
Description: Mouse LIF Protein, Tag Free (LIF-M5219) is expressed from human 293 cells (HEK293). It contains AA Ser 24 - Phe 203 (Accession # P09056-1).
Description: A Rabbit polyclonal antibody against Mouse Leukemia Inhibitory Factor (LIF). This antibody is labeled with PE.
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In addition, a anti the body of the N terminus of VP1u disrupted virus internalization, but only if it is present during and after the attachment of the virus, which indicates the involvement of these regions in the binding events required for internalization.
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