[6] Production of IgA-secreting rat × rat hybridomas

Dean, Christopher; Gyure, L A; Jg, Hall; Styles, J M

doi:10.1016/0076-6879(86)21008-3

Cited by 14 publications

(7 citation statements)

References 8 publications

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“…After storage in liquid nitrogen for 7 d these cells were thawed and fused with rat myeloma Y3-Ag 1.2.3 cells. 26 Hybridomas were cultured in a 1 : 1 mixture of DMEM (Dulbecco's Modi®ed Eagle Medium) and Ham's F12 (Life Technologies, Paisley) supplemented with 10% vav FBS (foetal bovine serum) (Hyclone Europe Ltd, Cramlington), cloned by the limiting dilution method and monoclonal antibody puri®ed by Protein G af®nity chromatography (Bioprocessing Ltd., UK). Isotype was determined using a commercial kit (Serotec Ltd., Oxford).…”

Section: Cell Linesmentioning

confidence: 99%

The tissue distribution of the human β3-adrenoceptor studied using a monoclonal antibody: Direct evidence of the β3-adrenoceptor in human adipose tissue, atrium and skeletal muscle

et al. 1999

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The tissue distribution of the human b b 3 -adrenoceptor studied using a monoclonal antibody: Direct evidence of the b b 3 -adrenoceptor in human adipose tissue, atrium and skeletal muscle 2,3 The human b 3 -adrenoceptor was later cloned by Emorine et al. 4 The pharmacology of the cloned b 3 -adrenoceptor agreed with the pharmacological data previously obtained in rodent adipose tissue, gut, and skeletal muscle in that the badrenoceptors in these tissues were insensitive to classical b-adrenoceptor antagonists such as propranolol.5 ± 8 Aryloxypropanolamine b 1 ab 2 adrenoceptor antagonists, exempli®ed by CGP12177, evoke a lipolytic response in rat adipose tissue through agonism at b 3 -adrenoceptors. 9 Similarly, selective b 3 -adrenoceptor agonists, such as BRL-37344, showed similar or greater potency than isoproterenol in stimulating lipolysis, but were much less potent than isoproterenol in stimulating responses mediated by b 1 -or b 2 -adrenoceptors. 10 The assessment of the pharmacological role of b 3 -adrenoceptors in human tissues has proved more controversial. For example, lipolysis in human white adipocytes induced by isoproterenol is sensitive to propranolol.11 Also, CGP12177-induced lipolytic responses have been demonstrated by some 12 ± 14 but not others. 9,15 It is now evident from comparisons of cloned human and rat b 3 -adrenoceptors that there are signi®cant species differences in pharmacology. 16 Attempts to detect b 3 -mRNA in human tissues using reverse-transcription PCR have also given conicting results. Krief et al 17 detected b 3 -adrenoceptor mRNA in several tissues, including gall bladder, adipose tissue and colon, while Thomas and Liggett 18 failed to detect a b 3 -adrenoceptor signal. Recently, RNAase protection assays, that do not rely on ampli®cation techniques, were used to identify b 3 -adrenoceptor mRNA in a variety of human tissues, including

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Section: Cell Linesmentioning

confidence: 99%

The tissue distribution of the human β3-adrenoceptor studied using a monoclonal antibody: Direct evidence of the β3-adrenoceptor in human adipose tissue, atrium and skeletal muscle

et al. 1999

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“…A rat monoclonal antibody to Brk, ICR 100, was raised by immunizing CBH/cbi rats via their Peyer's patches with recombinant Brk-glutathione S-transferase protein, and fusing cells from the mesenteric nodes into the Y3 rat myeloma as described previously (Dean et al, 1986). Mouse monoclonal antibody specific for the SV40 T-antigen, PAb416 (Harlow et al, 1981), was a gift from Dr. L. Crawford (Imperial Cancer Research Fund, Cambridge, United Kingdom).…”

Section: Antibodiesmentioning

confidence: 99%

Brk, a Breast Tumor-derived Non-receptor Protein-tyrosine Kinase, Sensitizes Mammary Epithelial Cells to Epidermal Growth Factor

Kamalati

Jolin

Mitchell

et al. 1996

Journal of Biological Chemistry

117

175

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brk (breast tumor kinase) shows homology to the src family of non-receptor protein-tyrosine kinases and is expressed in breast carcinomas. In order to investigate the role of brk in breast tumor development, we have examined the growth and transformation properties of human mammary epithelial cells engineered to overexpress Brk. Interestingly, like c-Src, overexpression of Brk leads to sensitization to EGF, and also results in a partially transformed phenotype. Further investigation of the latter activity was attempted by mutational analysis, targeting key residues known to affect tyrosine kinase activity in Src-like kinases. Mutation of amino acid residue Lys-219 to Met, by analogy to Src, abolished both kinase activity and transformation capacity. Mutation of amino acid residue Tyr-447 to Phe, however, resulted in a decrease in transforming potential without affecting kinase activity. These results suggest that while Src and Brk share some functional properties, they act differently during transformation. These differences are discussed in the context of the mechanisms underlying breast cancer development.

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“…After disaggregation, lo8 node cells were fused with 5 X lo7 exponentially growing cells of the rat myeloma line Y3 Ag 1.2.3. (Galfrk et al, 1979) as described by Dean et al (1986). Supernatants were screened 10 days later for the presence of antibodies that bound specifically to breast carcinoma cell lines grown as monolayers in Nunc 96-well plates (Gibco, Paisley, Scotland).…”

Section: Production Of Monoclonal Antibodiesmentioning

confidence: 99%

Rat monoclonal antibodies to the external domain of the product of the C‐erbB‐2 proto‐oncogene

Styles

Harrison

Gusterson

et al. 1990

Intl Journal of Cancer

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With the breast carcinoma cell line BT 474 used as a source of antigen, four rat monoclonal antibodies (MAbs) (3 IgG2a and I IgA) have been prepared against the external domain of the product of the c-erbB-2 proto-oncogene. All 4 antibodies stain frozen sections of tissues that over-express the product of the c-erbB-2 proto-oncogene, and competitive binding assays showed that the antibodies recognized 2 non-overlapping epitopes. Representative antibodies from the two groups (ICR12 and 13) were shown to specifically immunoprecipitate a 190 kDa protein from 35S-methionine-labelled breast carcinoma cells where the c-erbB-2 is amplified (BT 474 and MDA-MB 361). Two of the antibodies (ICR12 and ICR17) bind to the denatured antigen in Western blots and ICR12 stains formolsaline-fixed sections of breast carcinoma tissue that over-expresses the product of the c-erbB-2 proto-oncogene. These antibodies should be useful not only for immunocytochemical diagnoses but also for radio-immunoscintigraphic and therapeutic applications.

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[6] Production of IgA-secreting rat × rat hybridomas

Cited by 14 publications

References 8 publications

The tissue distribution of the human β3-adrenoceptor studied using a monoclonal antibody: Direct evidence of the β3-adrenoceptor in human adipose tissue, atrium and skeletal muscle

The tissue distribution of the human β3-adrenoceptor studied using a monoclonal antibody: Direct evidence of the β3-adrenoceptor in human adipose tissue, atrium and skeletal muscle

Brk, a Breast Tumor-derived Non-receptor Protein-tyrosine Kinase, Sensitizes Mammary Epithelial Cells to Epidermal Growth Factor

Rat monoclonal antibodies to the external domain of the product of the C‐erbB‐2 proto‐oncogene

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