scholarly journals Monoclonal antibodies that immunoreact with a cation-stimulated plant membrane ATPase

1982 ◽  
Vol 203 (1) ◽  
pp. 51-54 ◽  
Author(s):  
J J C Chin
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Marker Enzyme ◽  
Membrane Atpase ◽  
Hybridoma Technology ◽  
Membrane Antigens ◽  
Monospecific Antibodies

Hybridoma technology has been used successfully to generate monoclonal-antibody probes against protoplast membrane antigens. Hybridomas secreting monoclonal antibodies that either inhibit or stimulate a putative plasma-membrane marker enzyme, (K+ + Mg2+)-stimulated pH 6.5 ATPase, have been identified and cloned. The specificity of monoclonal-antibody probes on the activity of other phosphate-hydrolysing enzymes has also been examined. The production and identification of monospecific antibodies capable of immunoreacting with particular component proteins in a complex plant membrane mixture highlight the usefulness of hybridoma methodology for the enzymologist, especially since such monoclonal antibodies can be used in the purification of proteins by immunoaffinity techniques.

scholarly journals Isolation and characterization of monoclonal antibodies directed against plant plasma membrane and cell wall epitopes: identification of a monoclonal antibody that recognizes extensin and analysis of the process of epitope biosynthesis in plant tissues and cell cultures.

1988 ◽  
Vol 107 (1) ◽  
pp. 163-175 ◽  
Author(s):  
D J Meyer ◽  
C L Afonso ◽  
D W Galbraith
Keyword(s):  
Monoclonal Antibody ◽  
Cell Wall ◽  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Solid Phase ◽  
Culture Media ◽  
Gradient Centrifugation ◽  
Cell Suspension Cultures ◽  
Isolation And Characterization

Membranes from tobacco cell suspension cultures were used as antigens for the preparation of monoclonal antibodies. Use of solid phase and indirect immunofluorescence assays led to the identification of hybridomas producing antibodies directed against cell surface epitopes. One of these monoclonal antibodies (11.D2) was found to recognize a molecular species which on two-dimensional analysis (using nonequilibrium pH-gradient electrophoresis and SDS-PAGE) was found to have a high and polydisperse molecular mass and a very basic isoelectric point. This component was conspicuously labeled by [3H]proline in vivo. The monoclonal antibody cross-reacted with authentic tomato extensin, but not with potato lectin nor larch arabinogalactan. Use of the monoclonal antibody as an immunoaffinity reagent allowed the purification of a tobacco glycoprotein which was identical in amino acid composition to extensin. Finally, immunocytological analyses revealed tissue-specific patterns of labeling by the monoclonal antibody that were identical to those observed with a polyclonal antibody raised against purified extensin. We have concluded that monoclonal antibody 11.D2 recognizes an epitope that is carried exclusively by extensin. Analysis of cellular homogenates through differential and isopycnic gradient centrifugation revealed that biosynthesis of the extensin epitope was found on or within the membranes of the endoplasmic reticulum, Golgi region and plasma membrane. This result is consistent with the progressive glycosylation of the newly-synthesized extensin polypeptide during its passage through a typical eukaryotic endomembrane pathway of secretion. The 11.D2 epitope was not found in protoplasts freshly isolated from leaf tissues. However, on incubation of these protoplasts in appropriate culture media, biosynthesis of the epitope was initiated. This process was not impeded by the presence of chemicals that are reported to be inhibitors of cell wall production or of proline hydroxylation.

Analysis of differentiation and development of the specialized infection structures formed by biotrophic fungal plant pathogens using monoclonal antibodies

1995 ◽  
Vol 73 (S1) ◽  
pp. 408-417 ◽  
Author(s):  
Jonathan R. Green ◽  
Naomi A. Pain ◽  
Martin E. Cannell ◽  
Calum P. Leckie ◽  
Sharon McCready ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Powdery Mildew ◽  
Plant Pathogens ◽  
Colletotrichum Lindemuthianum ◽  
Cdna Expression Library ◽  
Erysiphe Pisi ◽  
Infection Structures ◽  
Fungal Plant Pathogens

Monoclonal antibodies have been used to study the differentiation and development of the specialized infection structures formed in the Colletotrichum–bean and powdery mildew – pea interactions. In the Colletotrichum lindemuthianum – bean interaction, monoclonal antibodies have been used to show that the extracellular matrices associated with conidia, germ tubes, and appressoria differ in composition and that the extracellular glycoproteins are organized into specific regions of the fungal cell surface. Monoclonal antibody UB27 has been used to show that the plasma membrane of appressoria is differentiated into distinct domains, with the integral membrane glycoprotein identified by UB27 being excluded from the pore region. UB25 recognizes a glycoprotein located specifically in the cell wall/matrix of intracellular hyphae and is expressed only during the biotrophic phase of development. In the Erysiphe pisi – pea interaction, UB8 and UB10 identify glycoproteins specific to the haustorial plasma membrane within the haustorial complex. Monoclonal antibodies that recognize the extrahaustorial membrane have shown that this membrane contains specific components, as well as glycoproteins in common with the host plasma membrane. UB8 has been successfully used to isolate a gene sequence coding for the protein antigen, by immunoscreening a cDNA expression library prepared from infected epidermis. An antibody that recognizes the plant endoplasmic reticulum has been used to show that this structure reorganizes around the developing haustorial complex in pea epidermal cells. Key words: appressorium, biotrophy, Colletotrichum lindemuthianum, Erysiphe pisi, haustorium, monoclonal antibody, powdery mildew.

scholarly journals Therapeutic Applications of Monoclonal Antibodies in Urologic-Oncology Management - An Update

2021 ◽  
Author(s):  
Maya Kulshekar ◽  
Shridhar C. Ghagane ◽  
Sridevi I. Puranik ◽  
Rajendra B. Nerli ◽  
Murigendra B. Hiremath
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Hematologic Malignancies ◽  
Treatment Modalities ◽  
Magic Bullet ◽  
Urologic Oncology ◽  
Potential Applications ◽  
Hybridoma Technology ◽  
Cancer Types ◽  
Antibody Design

The idea of utilizing immunotherapy for the treatment of cancers has been appealing to scientists and clinicians for over a several decades. Immunotherapy for cancers encompasses knowledge gained from a wide range of disciplines and has the potential to procure the ‘magic bullet’ for the treatment of cancer. Monoclonal antibody-based treatment of cancer has been recognized as one of the most successful therapeutic strategies for both hematologic malignancies and solid tumours in the last 20 years. The discovery of hybridoma technology in late 1975 and the development of chimeric, humanized, and human antibodies have increased the availability and utility of immunotherapy for the treatment of cancer. Metastatic or recurrent cancer continues to be the bane of the urological oncologist. Despite recent improvements in therapeutic management and outcomes for clinically localized disease overall survival rate in patients with the majority of metastatic and recurrent genitourinary malignancies remains relatively unchanged. By targeting tumours through specific or associated antigens, it is possible to selectively eliminate tumour cells and maintain an acceptable toxicity profile. Therapeutic antibodies that target immune cells are also being developed with the goal of breaking local tolerance and stimulating the patient’s anti-tumor immune response. As with other treatment modalities, immunotherapy is far from perfect and requires additional study to optimize clinical response and overcome therapeutic resistance. Modern advances in the field of immunotherapy hold the promise of providing the clinical urologist/oncologist with new tools to fight urological cancer. However, the literature on monoclonal antibody-based immunotherapy with a particular emphasis on target antigens, monoclonal antibody design and potential applications in the field of urology is limited. Hence, the present chapter focuses on the applications of Immunotherapy using monoclonal antibodies for urologic oncology settings such as prostate, bladder, renal, testicular and penile with a hope to highlight its clinical efficacy and also its mechanisms of action in each of these cancer types.

Identification of somatic hybrids in plant protoplast fusions with monoclonal antibodies to plasma-membrane antigens

Planta ◽  
1987 ◽  
Vol 170 (1) ◽  
pp. 49-54 ◽  
Author(s):  
M. S. Fitter ◽  
P. M. Norman ◽  
M. G. Hahn ◽  
V. P. M. Wingate ◽  
C. J. Lamb
Keyword(s):  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Somatic Hybrids ◽  
Plant Protoplast ◽  
Membrane Antigens

scholarly journals Development of a novel monoclonal antibody against chitinase-like protein YKL-39 applicable for immunohistochemistry

2019 ◽  
Vol 18 (2) ◽  
pp. 27-31
Author(s):  
A. N. Gratchev ◽  
D. V. Samoilova ◽  
S. N. Kurochkin ◽  
O. V. Kovaleva
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Western Blot ◽  
Full Length ◽  
High Expression ◽  
Secreted Protein ◽  
Hybridoma Technology ◽  
Potential Biomarkers

Introduction. Mammalian chitinase-like proteins are produced in the areas of inflammation and in tumors. Some members of chitinase-like proteins family are studied as potential biomarkers of tumors (glioma, prostate and ovary). YKL-39 also known as chitinase-3-like 2 (CHI3L2) is a secreted protein produced by chondrocytes. Its high expression is also found in synoviocytes, lung heart and macrophages.The aim of this study was the development of highly specific monoclonal antibodies against human YKL-39. Materials and methods. Using recombinant full-length human YKL-39 as immunogen using hybridoma technology we have generated monoclonal antibody 1B2G4, that specifically binds YKL-39 in ELISA.Results and conclusion. Obtained antibody was successfully tested in Western blot, immunocytochemistry, immunofluorescence and immunohistochemistry on FFPE sections. It was shown that the antibody binds the full-length YKL-39 protein and does not interact with other chitinase-like proteins. 

Monoclonal antibodies to plant plasma-membrane antigens

Planta ◽  
1986 ◽  
Vol 167 (4) ◽  
pp. 452-459 ◽  
Author(s):  
P. M. Norman ◽  
V. P. M. Wingate ◽  
M. S. Fitter ◽  
C. J. Lamb
Keyword(s):  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Membrane Antigens ◽  
Plant Plasma Membrane

NEUROBLASTOMA IMMUNOTHERAPY

2019 ◽  
Vol 65 (2) ◽  
pp. 181-187
Author(s):  
Aleksandr Druy ◽  
Svetlana Kuleva
Keyword(s):  
T Cells ◽  
Monoclonal Antibodies ◽  
High Risk ◽  
Checkpoint Inhibitors ◽  
Innate And Adaptive Immunity ◽  
Car T Cells ◽  
Car T ◽  
Membrane Antigens ◽  
Theoretical Evidence ◽  
Blocking Antibodies

The recent data about innate and adaptive immunity against neuroblastoma are described in the article. The era of neuroblastoma immunotherapy started since the evidence of anti-GD2 monoclonal antibodies efficiency. Nowadays monoclonal antibodies against GD2 are introduced into schemes of maintenance therapy for high-risk neuroblastoma patients. Developing of T-cells expressing chimeric antigen receptor (CAR-T cells) directed to membrane antigens is the perspective of neuroblastoma immunotherapy. PD1/PD-L1 blocking antibodies as immune checkpoint inhibitors have the theoretical evidence of potential effectiveness. Application of immunotherapeutic approaches in high-risk neuroblastoma patients together with conventional multimodal therapies requires further investigation.

PERSPECTIVES OF APPLICATION OF ANTIBODIES AGAINST ENDOGLIN (CD105) FOR VISUALIZATION AND ANTI-ANGIOGENE THERAPY OF TUMORS

2018 ◽  
Vol 64 (4) ◽  
pp. 504-507
Author(s):  
Vladimir Klimovich ◽  
Natalya Vartanyan ◽  
Anastasiya Stolbovaya ◽  
Lidiya Terekhina ◽  
Olga Shashkova ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Monoclonal Antibodies ◽  
Human Plasma ◽  
Vascular Endothelium ◽  
Immune Complexes ◽  
Targeted Delivery ◽  
Biological Fluids ◽  
Therapeutic Drugs ◽  
Cultured Endothelial Cells ◽  
Hybridoma Technology

During last years monoclonal antibodies (MAB) directed against vascular endothelium markers demonstrated their efficiency for visualization and targeted delivery of therapeutic drugs to tumors. Endoglin (CD105) which serves as a key element that determines endothelial cells quiescence or activation is one of such markers. Endoglin is highly expressed on the vascular endothelium of growing tumors. A first panel of MAB against endoglin in our country was produced at the hybridoma technology laboratory of RRC RST named after A.M. Granov. On the basis of these MAB ELISA was created allowing detection of endoglin in human plasma and other biological fluids. Several MAB had been shown to bind endoglin on the membrane of the cultured endothelial cells and to persist there for several hours. During the first 30 min after binding some of the immune complexes “endoglin-MAB” were internalized into the cytoplasm and were found included in the endosomes. In future these MAB can be used to create the reagents for the addressed delivery of isotope tags both on the membrane and into the cytoplasm of endothelial cells.

Rapid quantification and in situ detection of nitrifying bacteria in biofilms by monoclonal antibody method

2000 ◽  
Vol 41 (4-5) ◽  
pp. 301-308 ◽  
Author(s):  
N. Noda ◽  
H. Ikuta ◽  
Y. Ebie ◽  
A. Hirata ◽  
S. Tsuneda ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Fluorescent Antibody ◽  
Nitrifying Bacteria ◽  
Fluorescent Antibody Technique ◽  
Antibody Technique ◽  
Antibody Method ◽  
In Situ Detection ◽  
Rapid Quantification

Fluorescent antibody technique by the monoclonal antibody method is very useful and helpful for the rapid quantification and in situ detection of the specific bacteria like nitrifiers in a mixed baxterial habitat such as a biofilm. In this study, twelve monoclonal antibodies against Nitrosomonas europaea (IFO14298) and sixteen against Nitrobacter winogradskyi (IFO14297) were raised from splenocytes of mice (BALB/c). It was found that these antibodies exhibited little cross reactivity against various kinds of heterotrophic bacteria. The direct cell count method using monoclonal antibodies could exactly detect and rapidly quantify N. europaea and N. winogradskyi. Moreover, the distribution of N. europaea and N. winogradskyi in a biofilm could be examined by in situ fluorescent antibody technique. It was shown that most of N. winogradskyi existed near the surface part and most of N. europaea existed at the inner part of the polyethylene glycol (PEG) gel pellet, which had entrapped activated sludge and used in a landfill leachate treatment reactor. It was suggested that this monoclonal antibody method was utilized for estimating and controlling the population of nitrifying bacteria as a quick and favorable tool.

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