86 results about "Phagocyte" patented technology

Conjugates containing as a ligand a chemokine receptor targeting agents, such as chemokines, and a targeted agent, such as a toxin are provided. These conjugates are used to treat inflammatory responses associated with activation, proliferation and migration of immune effector cells, including leukocyte cell types, neutrophiles, macrophages, and eosinophils. The conjugates provided herein are used to lessen or inhibit these processes to prevent or at least lessen the resulting secondary effects. In particular, the conjugates are used to target toxins to receptors on secondary tissue damage-promoting cells. The ligand moiety can be selected to deliver the cell toxin to such secondary tissue damage-promoting cells as mononuclear phagocytes, leukocytes, natural killer cells, dendritic cells, and T and B lymphocytes, thereby suppressing the proliferation, migration, or physiological activity of such cells. Among preferred conjugates are fusion proteins having a chemokine, or a biologically active fragment thereof, as the ligand moiety linked to a cell toxin via a peptide linker of from 2 to about 60 amino acid residues.

Causative microorganisms of infectious diseases are detected and / or identified rapidly and with high sensitivity by taking phagocytes from clinical specimens containing active phagocytes, immobilizing the phagocytes so taken, treating the phagocytes to improve cell membrane permeabilities thereof, further treating the phagocytes to bare DNA in the causative microorganisms which might exist in the phagocytes, and detecting the causative microorganisms with DNA probes which can hybridize with such DNA under stringent conditions.

Conjugates containing as a ligand chemokine receptor targeting agents, such as chemokines, and a targeted agent, such as a toxin are provided. These conjugates are used to treat inflammatory responses associated with activation, proliferation and migration of immune effector cells, including leukocyte cell types, neutrophils, macrophages, and eosinophils. The conjugates provided herein are used to lessen or inhibit these processes to prevent or at least lessen the resulting secondary effects. In particular, the conjugates can be used to target toxins to receptors on secondary tissue damage-promoting cells. The ligand moiety can be selected to deliver the cell toxin to such secondary tissue damage-promoting cells as mononuclear phagocytes, leukocytes, natural killer cells, dendritic cells, and T and B lymphocytes, thereby suppressing the proliferation, migration, or physiological activity of such cells. Among preferred conjugates are fusion proteins having a chemokine, or a biologically active fragment thereof, as the ligand moiety linked to a cell toxin via a peptide linker of from 2 to about 60 amino acid residues.

The invention discloses a method for extracting ganoderma lucidum fruit body polysaccharides by using superpressure; the ganoderma lucidum fruit body polysaccharides are new endogenetic active materials extracted from the ganoderma lucidum fruit bodies. The ingredients of the ganoderma lucidum polysaccharides can improve the phagocytosis of phagocytes, the humoral immunity and cellular immune function, which can improve the SOD activity of superoxide dismutases in red blood cells in human bodies. However, the ganoderma lucidum cells are compact, and the polysaccharides are difficult to be extracted from ganoderma lucidum. The methods of extraction which are most used currently are defective. The method for extracting ganoderma lucidum fruit body polysaccharides comprises the steps of selecting ganoderma lucidum fruit bodies, adding extracting solution, sealing and immersing the ganoderma lucidum fruit bodies in the extracting solution, treating the ganoderma lucidum fruit bodies under superpressure, filtration and condensation, drying the condensed filtrate, getting the polysaccharides from the ganoderma lucidum fruit bodies. High temperature does not occur during the extraction; active ingredients in the ganoderma lucidum fruit bodies can be preserved; the extraction takes little time with high yield and low impurity content. In addition, some microbes can be killed through pressurization to complete extraction and sterilization at one step. The method for extracting ganoderma lucidum fruit body polysaccharides overwhelms the defects of the prior methods for extracting polysaccharides from ganoderma lucidum.

In order to accurately and reliably quantitate HLE on the plasma membranes of the lymphocytes and mononuclear phagocytes, a test sample containing the lymphocytes and mononuclear phagocytes is initially treated with a first antiserum specific for CD4 receptors on the plasma membrane or with a second antiserum specific for chemokine receptors on the plasma membrane. Once the CD4 or chemokine receptors have been rendered non-reactive (competitive) relative to the HLE receptors (also “binding sites”) on the plasma membrane, the test sample is contacted with an immunoreagent specific for interaction with one or more of the HLE receptors on the plasma membranes of the lymphocytes and mononuclear phagocytes. The immunoreagent forms a complex with the HLE binding sites and produces a characteristic physical change in the lymphocytes and mononuclear phagocytes that can be monitored by any one of a number of standard techniques, (e.g., confocal laser scanning microscopy and flow cytometry).

The present invention features therapeutic bacteriophage deficient in the lysin protein (“Lys minus” phage). Lys minus bacteriophage are incapable of facilitating efficient lysis of the bacterial host since the enzymatic activity of the lysin of the phage is needed for breaking down the peptidoglycan layer of the bacterial cell wall. Lys minus bacteriophage retain activity in invasion of its appropriate bacterial host, destruction of the bacterial genome, and replication, which are sufficient to inhibit bacterial growth and replication. Therefore, the therapeutic Lys minus phage stops the spread of infection by the bacterial pathogen without lysis of the bacterium. This approach is attractive as it also prevents the release of the phage progeny, thus reducing or eliminating the potential for generation of immune responses against the phage. The incapacitated bacterial pathogen is then removed by the normal defense systems such as phagocytes and macrophages.

The invention is directed to methods for treating, inhibiting or prevent the incidence of vascular disease in a subject or in a non-human animal by administering visfatin. Particularly, the invention provides for methods to prevent phagocyte cell death due to ER-stress by the administration of visfatin. The invention also encompasses methods for identifying a visfatin polypeptide or a visfatin nucleic acid capable of treating a vascular disease as well as pharmaceutical compositions comprising visfatin.

The invention provides methods and compositions for the detection and treatment of Anaplasma phagocytophilum and Anaplasma platys infection.

The invention provides methods and compositions for the detection and treatment of Anaplasma phagocytophilum and Anaplasma platys infection.

We have successfully sequenced and cloned the gene expressing the Major Surface Protein 5 (MSP5) of A. phagocytophilum. The recombinant MSP5 (rMSP5) protein has been tested using sera from humans and dogs infected with A. phacytophilum. The polypeptide has been found to be immunogenic and useful as a diagnostic test antigen. The polypeptide antigen of the subject invention can provide the basis of a diagnostic assay that would allow the rapid, in-house, laboratory diagnosis of infection with A. phagocytophilum using a sample (e.g., serum, plasma, or whole blood) from an infected human or animal. Additionally, the subject invention provides methods of detecting the presence of A. phagocytophilum in biological or environmental samples utilizing antibodies provided by the subject invention. Furthermore, the use of the single antigen in the diagnosis of this important disease offers many advantages including enhanced test specificity, ease of testing and consistency of results using synthetically produced test antigens instead of cultured, whole organisms.

The invention discloses a bovine derived anti-staphylococcus aureus fusion antibody scFv-Fc and a preparation method thereof. The fusion antibody scFv-Fc at least has a light chain variable region ofthe amino acid sequence shown as SEQ ID No:1, a heavy chain variable region of the amino acid sequence shown as SEQ ID No:2, an intermediate connecting peptide between the light chain variable regionand the heavy chain variable region, and a Fc fragment of the amino acid sequence shown as SEQ ID No:3. The ELISA result shows that the fusion antibody can be specifically bound to a staphylococcus aureus antigen; in in-vitro bacteriostatic test, the fusion antibody can completely inhibit the growth of staphylococcus aureus within 24h; moreover, the fusion antibody can mediate dairy cow peripheralblood phagocytes in terms of playing the role of conditioning phagocytosis. The fusion antibody can be used in related reagents or drugs for diagnosis, prevention and treatment of staphylococcus aureus cow mastitis.

Evidence is presented that inflammation and injury involves activation of xanthine oxidoreductase (XOR) in the newly recruited mononuclear phagocytes (MNP). XOR has been shown to be increased predominantly in the MNP that increase rapidly in the lungs of rats that develop acute lung injury (ALI) following intratracheal cytokine insufflation. XOR was recovered from the MNP largely converted to its oxygen radical generating, reversible O-form, and alveolar MNP exhibited increased oxidative stress as evidenced by increased nitrotyrosine staining. Cytokine insufflation also increased alveolar cell apoptosis. A functional role for XOR in cytokine induced inflammation was demonstrated. Tungsten and allopurinol decreased MNP XOR induction, nitrotyrosine staining, inflammatory cell infiltration, and alveolar cell apoptosis. Transfer of control or allopurinol treated MNP into rat lungs and confirmed a specific role for MNP XOR in promoting lung inflammation. These data indicate that XOR can contribute to lung inflammation by its expression and conversion in a highly mobile inflammatory cell population.

Causative microorganisms of infectious diseases are detected and / or identified rapidly and high-sensitively by taking phagocytes from the clinical specimens containing active phagocytes, immobilizing the phagocytes so taken, treating the phagocytes to improve cell membrane permeabilities thereof, further treating the phagocytes to bare DNA in the causative microorganisms which might be existed in the phagocytes, and detecting the causative microorganisms with DNA probes which can hybridize with such DNA under stringent conditions.

Malignant melanoma cells spontaneously generate reactive oxygen species (ROS) that promote constitutive activation of the transcription factor nuclear factor-kB (NF-kB). Although antioxidants and inhibitors of NAD(P)H oxidases significantly reduce constitutive NF-kB activation and suppress cell proliferation, the nature of the enzyme responsible for ROS production in melanoma cells has not been determined. To address this issue, we now have characterized the source of ROS production in melanoma cells. ROS are generated by isolated, cytosol-free melanoma plasma membranes, with inhibition by NAD(P)H oxidase inhibitors. The p22phox, gp91phox and p67phox components of the human phagocyte NAD(P)H oxidase, and the 91phox homolog NOX4 were demon-strated in melanomas by RT-PCR and sequencing, and protein product for both p22phox and gp91phox were detected in cell membranes by immunoassay. Normal human epidermal melanocytes expressed only p22phox and NOX4. Melanoma proliferation was reduced by NAD(P)H oxidase inhibitors and by transfection of antisense but not sense oligonucleotides for p22phox and NOX4. Also, the flavoprotein inhibitor diphenylene iodonium inhibited constitutive DNA binding of nuclear protein to the NF-kB and cyclic-AMP response element consensus oligonucleotides, without affecting DNA binding activity to AP-1 or OCT-1.