Immunoglobulin heavy-chain expression and class switching in a murine leukaemia cell line

Nature ◽  
1982 ◽  
Vol 296 (5855) ◽  
pp. 325-331 ◽  
Author(s):  
Frederick W. Alt ◽  
Naomi Rosenberg ◽  
Rose J. Casanova ◽  
Elise Thomas ◽  
David Baltimore
Keyword(s):  
Cell Line ◽  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Class Switching ◽  
Leukaemia Cell ◽  
Leukaemia Cell Line

scholarly journals Phosphorylation of the myosin heavy chain. Its effect on actin-activated Mg2+-stimulated ATPase in leukaemic myeloblasts

1983 ◽  
Vol 214 (3) ◽  
pp. 839-843 ◽  
Author(s):  
J Sagara ◽  
K Nagata ◽  
Y Ichikawa
Keyword(s):  
Alkaline Phosphatase ◽  
Atpase Activity ◽  
Myeloid Leukaemia ◽  
Cell Line ◽  
Heavy Chain ◽  
Light Chain ◽  
Leukaemia Cell ◽  
Leukaemia Cell Line ◽  
Heavy Chains ◽  
Phosphatase Treatment

Myosin purified from a murine myeloid leukaemia cell line (M1) that had been incubated with [32P]orthophosphate incorporated 32P into the heavy, but not the light, chain. When the heavy chain was dephosphorylated by bacterial alkaline phosphatase, myosin that had low actin-activated ATPase activity gained higher activity only in the presence of the light-chain kinase. In the absence of the light-chain kinase, however, the Mg2+-stimulated ATPase activity of myosin was not activated by actin, regardless of phosphatase treatment. These results indicate that the activity of M1 myosin ATPase is regulated by phosphorylation of both the light and heavy chains. A scheme for this regulation by phosphorylation is presented and discussed.

Immunoglobulin heavy-chain class switching in a pre-B cell line is accompanied by DNA rearrangement

Nature ◽  
1983 ◽  
Vol 306 (5940) ◽  
pp. 243-246 ◽  
Author(s):  
Peter D. Burrows ◽  
Gabriele B. Beck-Engeser ◽  
Matthias R. Wabl
Keyword(s):  
B Cell ◽  
Cell Line ◽  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Dna Rearrangement ◽  
Class Switching

Purification and sequencing of glycosylation variants of BSF-1, as a MAF, from the EL-4 leukaemia cell line

1989 ◽  
Vol 17 (1) ◽  
pp. 65-74 ◽  
Author(s):  
C. Sutton ◽  
P. Depledge ◽  
L. Bawden ◽  
A. Carne ◽  
M. Meltzer ◽  
...  
Keyword(s):  
Cell Line ◽  
Leukaemia Cell ◽  
Leukaemia Cell Line

scholarly journals Vindesine receptors in cells of a human leukaemia cell line

1982 ◽  
Vol 46 (3) ◽  
pp. 392-396 ◽  
Author(s):  
K Totsuka ◽  
K Oshimi ◽  
H Mizoguchi
Keyword(s):  
Cell Line ◽  
Leukaemia Cell ◽  
Leukaemia Cell Line ◽  
Human Leukaemia Cell ◽  
Human Leukaemia ◽  
In Cells

Induction of erythroid differentiation in the human leukaemia cell line K562

Nature ◽  
1979 ◽  
Vol 278 (5702) ◽  
pp. 364-365 ◽  
Author(s):  
LEIF C. ANDERSSON ◽  
MIKKO JOKINEN ◽  
CARL G. GAHMBERG
Keyword(s):  
Cell Line ◽  
Erythroid Differentiation ◽  
Leukaemia Cell ◽  
Leukaemia Cell Line ◽  
Human Leukaemia Cell ◽  
Human Leukaemia

DNA rearrangement causes a high rate of spontaneous mutation at the immunoglobulin heavy-chain locus of a mouse myeloma cell line

1986 ◽  
Vol 6 (12) ◽  
pp. 4228-4235
Author(s):  
H Yu ◽  
L A Eckhardt
Keyword(s):  
Cell Line ◽  
Heavy Chain ◽  
Spontaneous Mutation ◽  
Immunoglobulin Heavy Chain ◽  
Myeloma Cell ◽  
Chain Gene ◽  
Parent Cell ◽  
Mrna Levels ◽  
Dna Rearrangement ◽  
Myeloma Cell Line

The spontaneous mutation rate of immunoglobulin genes expressed in myeloma cells is well above that of other genes expressed in these or in other cell types. The nature of such mutations in one myeloma cell line, MPC11, was explored at the molecular level. Included in this study were MPC11 variants representing 24 independent and spontaneous mutations affecting immunoglobulin secretion. Of the mutants studied, 19 had ceased immunoglobulin heavy chain (IgH) production (nonproducers), and 5 produced from as little as 1/1,000 to as much as 1/10 the amount of immunoglobulin produced by MPC11 (low producers). Only one of the MPC11 mutants (a nonproducer) showed no evidence of DNA rearrangement in or near the expressed IgH gene. The formerly expressed gamma 2b gene had been deleted in 18 of the 19 nonproducers. All of the low producers had undergone DNA rearrangement in or near the expressed IgH gene, and three of them produced immunoglobulin of a new heavy chain class. The cause for reduced heavy-chain synthesis in the low producers is not yet known. However, in several of these mutants, the defect appeared to be posttranscriptional. In these cell lines, steady-state IgH mRNA levels were much lower than in the parent cell line, while the heavy-chain gene transcription rate remained unchanged.

scholarly journals Rate of replication of the murine immunoglobulin heavy-chain locus: evidence that the region is part of a single replicon.

1987 ◽  
Vol 7 (1) ◽  
pp. 450-457 ◽  
Author(s):  
E H Brown ◽  
M A Iqbal ◽  
S Stuart ◽  
K S Hatton ◽  
J Valinsky ◽  
...  
Keyword(s):  
B Cell ◽  
Cell Line ◽  
Gene Cluster ◽  
Cell Lines ◽  
Heavy Chain ◽  
Dna Content ◽  
Immunoglobulin Heavy Chain ◽  
S Phase ◽  
C Value ◽  
Murine Erythroleukemia

We measured the temporal order of replication of EcoRI segments from the murine immunoglobulin heavy-chain constant region (IgCH) gene cluster, including the joining (J) and diversity (D) loci and encompassing approximately 300 kilobases. The relative concentrations of EcoRI segments in bromouracil-labeled DNA that replicated during selected intervals of the S phase in Friend virus-transformed murine erythroleukemia (MEL) cells were measured. From these results, we calculated the nuclear DNA content (C value; the haploid DNA content of a cell in the G1 phase of the cell cycle) at the time each segment replicated during the S phase. We observed that IgCH genes replicate in the following order: alpha, epsilon, gamma 2a, gamma 2b, gamma 1, gamma 3, delta, and mu, followed by the J and D segments. The C value at which each segment replicates increased as a linear function of its distance from C alpha. The average rate of DNA replication in the IgCH gene cluster was determined from these data to be 1.7 to 1.9 kilobases/min, similar to the rate measured for mammalian replicons by autoradiography and electron microscopy (for a review, see H. J. Edenberg and J. A. Huberman, Annu. Rev. Genet. 9:245-284, 1975, and R. G. Martin, Adv. Cancer Res. 34:1-55, 1981). Similar results were obtained with other murine non-B cell lines, including a fibroblast cell line (L60T) and a hepatoma cell line (Hepa 1.6). In contrast, we observed that IgCh segments in a B-cell plasmacytoma (MPC11) and two Abelson murine leukemia virus-transformed pre-B cell lines (22D6 and 300-19O) replicated as early as (300-19P) or earlier than (MPC11 and 22D6) C alpha in MEL cells. Unlike MEL cells, however, all of the IgCH segments in a given B cell line replicated at very similar times during the S phase, so that a temporal directionality in the replication of the IgCH gene cluster was not apparent from these data. These results provide evidence that in murine non-B cells the IgCH, J, and D loci are part of a single replicon.

scholarly journals Identification of a novel member of the Rab8 family from the rat basophilic leukaemia cell line, RBL.2H3

1996 ◽  
Vol 109 (6) ◽  
pp. 1265-1274 ◽  
Author(s):  
J. Armstrong ◽  
N. Thompson ◽  
J.H. Squire ◽  
J. Smith ◽  
B. Hayes ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Line ◽  
Northern Blot Analysis ◽  
Intracellular Localization ◽  
Transient Transfection ◽  
The Novel ◽  
Leukaemia Cell ◽  
Marked Contrast ◽  
Epitope Tag ◽  
Leukaemia Cell Line

We describe the cloning of a cDNA from the rat basophilic leukaemia cell line (RBL.2H3) encoding a novel member of the Rab family of small GTP binding proteins. The novel clone, which we call Rab8b, is most highly related to the Rab8 family with substantial divergence in the variable C-terminal domain. Northern blot analysis reveals highest levels of expression of Rab8b in the spleen, testis and brain, which is in marked contrast to the tissue distribution of Rab8. The Rab8b cDNA was modified to introduce a c-myc epitope tag at the extreme N terminus of the protein, and transient transfection studies were performed to analyse the intracellular localization of Rab8b by confocal microscopy. Transient expression of the c-myc/Rab8b fusion protein in both PC12 and RBL.2H3 cells shows staining of both the plasma membrane and ill-defined vesicular structures, and in the case of RBL.2H3 cells appears to induce striking outgrowths of the plasma membrane.

Sign in / Sign up

Export Citation Format

Share Document