Further characterization of the antigen defined by the monoclonal antibody M27

1989 ◽  
Vol 94 (4) ◽  
pp. 725-731
Author(s):  
M.E. Bramwell ◽  
S.M. Humm
Keyword(s):  
Monoclonal Antibody ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Reducing Conditions ◽  
Rat Lymphocytes ◽  
Foetal Liver ◽  
Cultivation In Vitro

Using immunoblotting techniques, the antigen that binds the monoclonal antibody M27 has been clearly defined in terms of apparent molecular mass and distribution. In reducing conditions it has an apparent mass of 178K (K = 10(3) Mr) and is present in the cytoplasm and membranes of all mammalian tissue culture cells so far examined. It is absent from lines derived from avian, piscine and amphibian sources. It is also absent from foetal liver of both rat and mouse, but subsequently appears after cultivation in vitro. Similarly, it can be detected on rat lymphocytes only after mitogenic stimulation. However, it is found on both hepatoma and lymphoma cells in vitro, and on in vivo tumours from murine sources. It thus appears to be associated with cell proliferation.

scholarly journals Characterization of the in vitro and in vivo properties of CFZ533, a blocking and non-depleting anti-CD40 monoclonal antibody

2018 ◽  
Vol 18 (12) ◽  
pp. 2895-2904 ◽  
Author(s):  
Jacinda Ristov ◽  
Pascal Espie ◽  
Peter Ulrich ◽  
Denise Sickert ◽  
Thierry Flandre ◽  
...  
Keyword(s):  
Monoclonal Antibody

scholarly journals Analysis of the Dynein-Dynactin Interaction In Vitro and In Vivo

2003 ◽  
Vol 14 (12) ◽  
pp. 5089-5097 ◽  
Author(s):  
Stephen J. King ◽  
Christa L. Brown ◽  
Kerstin C. Maier ◽  
Nicholas J. Quintyne ◽  
Trina A. Schroer
Keyword(s):  
Cytoplasmic Dynein ◽  
Binding Assays ◽  
Microtubule Organization ◽  
Binding Domains ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Dynein Intermediate Chain ◽  
Transient Overexpression

Cytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding assays were used to define binding domains in the dynein intermediate chain (IC) and dynactin p150Glued subunit. Transient overexpression of a series of fragments of the dynein IC was used to determine the importance of this subunit for dynein function in mammalian tissue culture cells. Our results suggest that a functional dynein-dynactin interaction is required for proper microtubule organization and for the transport and localization of centrosomal components and endomembrane compartments. The dynein IC fragments have different effects on endomembrane localization, suggesting that different endomembranes may bind dynein via distinct mechanisms.

scholarly journals Characterization of a humanized IgG4 anti-HLA-DR monoclonal antibody that lacks effector cell functions but retains direct antilymphoma activity and increases the potency of rituximab

Blood ◽  
2006 ◽  
Vol 108 (8) ◽  
pp. 2736-2744 ◽  
Author(s):  
Rhona Stein ◽  
Zhengxing Qu ◽  
Susan Chen ◽  
David Solis ◽  
Hans J. Hansen ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Effector Cell ◽  
Cell Functions ◽  
Hla Dr ◽  
Complement Dependent Cytotoxicity ◽  
Survival Pathway ◽  
Anti Cd20

AbstractHLA-DR is under investigation as a target for monoclonal antibody (mAb) therapy of malignancies. Here we describe a humanized IgG4 form of the anti-HLA-DR mAb L243, hL243γ4P (IMMU-114), generated to provide an agent with selectivity toward neoplastic cells that can kill without complement-dependent cytotoxicity (CDC) or antibody-dependent cellular-cytotoxicity (ADCC), so as to reduce reliance on intact immunologic systems in the patient and effector mechanism-related toxicity. In vitro studies show that replacing the Fc region of hL243γ1, a humanized IgG1 anti-HLA-DR mAb, with the IgG4 isotype abrogates the effector cell functions of the antibody (ADCC and CDC) while retaining its antigen-binding properties, antiproliferative capacity (in vitro and in vivo), and the ability to induce apoptosis concurrent with activation of the AKT survival pathway. Growth inhibition was evaluated compared with and in combination with the anti-CD20 mAb rituximab, with the combination being more effective than rituximab alone in inhibiting proliferation. Thus, hL243γ4P is indistinguishable from hL243γ1 and the parental murine mAb in assays dependent on antigen recognition. The abrogation of ADCC and CDC, which are believed to play a major role in side effects of mAb therapy, may make this antibody an attractive clinical agent. In addition, combination of hL243γ4P with rituximab offers the prospect for improved patient outcome.

scholarly journals Biochemical Characterization of the Drosophila Wingless Signaling Pathway Based on RNA Interference

2004 ◽  
Vol 24 (5) ◽  
pp. 2012-2024 ◽  
Author(s):  
Hiroko Matsubayashi ◽  
Sonoka Sese ◽  
Jong-Seo Lee ◽  
Tadaoki Shirakawa ◽  
Takeshi Iwatsubo ◽  
...  
Keyword(s):  
Rna Interference ◽  
Biochemical Characterization ◽  
The Other ◽  
Protein Levels ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Mediated Priming ◽  
Kinase A

ABSTRACT Regulation of Armadillo (Arm) protein levels through ubiquitin-mediated degradation plays a central role in the Wingless (Wg) signaling. Although zeste-white3 (Zw3)-mediated Arm phosphorylation has been implicated in its degradation, we have recently shown that casein kinase Iα (CKIα) also phosphorylates Arm and induces its degradation. However, it remains unclear how CKIα and Zw3, as well as other components of the Arm degradation complex, regulate Arm phosphorylation in response to Wg. In particular, whether Wg signaling suppresses CKIα- or Zw3-mediated Arm phosphorylaytion in vivo is unknown. To clarify these issues, we performed a series of RNA interference (RNAi)-based analyses in Drosophila S2R+ cells by using antibodies that specifically recognize Arm phosphorylated at different serine residues. These analyses revealed that Arm phosphorylation at serine-56 and at threonine-52, serine-48, and serine-44, is mediated by CKIα and Zw3, respectively, and that Zw3-directed Arm phosphorylation requires CKIα-mediated priming phosphorylation. Daxin stimulates Zw3- but not CKIα-mediated Arm phosphorylation. Wg suppresses Zw3- but not CKIα-mediated Arm phosphorylation, indicating that a vital regulatory step in Wg signaling is Zw3-mediated Arm phosphorylation. In addition, further RNAi-based analyses of the other aspects of the Wg pathway clarified that Wg-induced Dishevelled phosphoylation is due to CKIα and that presenilin and protein kinase A play little part in the regulation of Arm protein levels in Drosophila tissue culture cells.

scholarly journals In vitro and In vivo Characterization of 64Cu-Labeled AbegrinTM, a Humanized Monoclonal Antibody against Integrin αvβ3

2006 ◽  
Vol 66 (19) ◽  
pp. 9673-9681 ◽  
Author(s):  
Weibo Cai ◽  
Yun Wu ◽  
Kai Chen ◽  
Qizhen Cao ◽  
David A. Tice ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Integrin Αvβ3 ◽  
Humanized Monoclonal Antibody ◽  
In Vivo Characterization

scholarly journals Binding of parbendazole to tubulin and its influence on microtubules in tissue-culture cells as revealed by immunofluorescence microscopy

1981 ◽  
Vol 49 (1) ◽  
pp. 195-204
Author(s):  
J.C. Havercroft ◽  
R.A. Quinlan ◽  
K. Gull
Keyword(s):  
Immunofluorescence Microscopy ◽  
Microtubule Assembly ◽  
Animal Cells ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Benzimidazole Carbamates ◽  
Cytoplasmic Microtubules ◽  
Tubulin Immunofluorescence

We have shown that the benzimidazole carbamate, parbendazole, is a potent inhibitor of microtubule assembly in vitro and in vivo. Radiolabelled parbendazole was shown to bind to purified tubulin. Immunofluorescence studies using antitubulin antibody showed that parbendazole effectively depolymerizes cytoplasmic microtubules in animal cells leaving only one or two microtubules associated with one centriole. The usefulness of parbendazole and other benzimidazole carbamates as inhibitors of microtubule functions is discussed.

A monoclonal antibody (SJ-9A4) to P24 present on common ALLS, neuroblastomas and platelets — II. Characterization of P24 and shedding in vitro and in vivo

1983 ◽  
Vol 7 (4) ◽  
pp. 499-507 ◽  
Author(s):  
Yoshihiro Komada ◽  
Stephen C. Peiper ◽  
Susan L. Melvin ◽  
Betty Tarnowski ◽  
Alexander A. Green
Keyword(s):  
Monoclonal Antibody

In Vitro and In Vivo Models of Spinal Muscular Atrophy

2017 ◽  
Author(s):  
W. David Arnold ◽  
Arthur H. M. Burghes
Keyword(s):  
Tissue Culture ◽  
Spinal Muscular Atrophy ◽  
Muscular Atrophy ◽  
In Vivo Models ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Smn Protein

Spinal muscular Atrophy (SMA) is caused by reduced levels of the SMN protein. In humans this is caused by loss of SMN1 and retention of SMN2. The challenge in modelling SMA, in either tissue culture cells or animals, is first to obtain the desired SMN levels equivalent to what is observed in SMA. Various models of SMA in tissue culture cells, invertebrates, and mammals have been created have been developed. The targets of SMN reduction that are most relevant for the pathogenesis of SMA and how the phenotype of SMA can be modified independent of SMN levels are two important questions that remain unanswered. Here the current in vitro and in vivo models of SMA are summarized.

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