An EBV-transformed owl monkey B-lymphocyte cell line

Scammell, Jonathan G.; Reynolds, Philip D.; Elkhalifa, Mohamed; Tucker, J. Allan; Moore, Charleen M.

doi:10.1007/s11626-997-0028-z

Cited by 14 publications

(7 citation statements)

References 12 publications

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“…A transformed female B lymphoblast cell line CRL-2312 of A. nancymae was obtained from the American Type Culture Collection (Scammell et al 1997). We identified this cell line as derived from A. nancymae in view of its karyotypic attributes (chromosome morphology and diploid number) corresponding to karyotype I (Brumback et al 1971;Ma et al 1976;Hershkovitz 1983;Groves 2001).…”

Section: Methodsmentioning

confidence: 99%

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

et al. 2004

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We mapped chromosomal homologies in two species of Chiropotes (Pitheciini, Saki Monkeys) and one species of Aotus (Aotinae, Owl Monkey) by multi-directional chromosome painting. Human chromosome probes were hybridized to Chiropotes utahicki, C. israelita and Aotus nancymae metaphases. Wooly Monkey chromosome paints were also hybridized to Owl Monkey metaphases. We established Owl Monkey chromosome paint probes by flow sorting and reciprocally hybridized them to human chromosomes. The karyotypes of the Bearded Saki Monkeys studied here are close to the hypothesized ancestral platyrrhine karytoype, while that of the Owl Monkey appears to be highly derived. The A. nancymae karyotype is highly shuffled and only three human syntenic groups were found conserved coexisting with 17 derived human homologous associations. A minimum of 14 fissions and 13 fusions would be required to derive the A. nancymae karyotype from that of the ancestral New World primate karyotype. An inversion between homologs to segments of human 10 and 16 suggests a link between Callicebus and Chiropotes, while the syntenic association of 10/11 found in Aotus and Callicebus suggests a link between these two genera. Future molecular cytogenetic work will be needed to determine whether these rearrangements represent synapomorphic chromosomal traits.

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Section: Methodsmentioning

confidence: 99%

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

et al. 2004

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“…We report here that the hsp90-associated immunophilin, FKBP51, is overexpressed in squirrel monkeys and is responsible for the low binding affinity of the squirrel monkey GR. (12,13). HL, SML, OML, and B95-8 cells were grown in suspension cultures in RPMI 1640 media supplemented with 10% FBS, 4 mm glutamine, 50 U/mL penicillin G, and 0.05 mg/mL streptomycin.…”

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confidence: 99%

Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP51¹

Reynolds¹,

Ruan²,

Smith³

et al. 1999

The Journal of Clinical Endocrinology & Metabolism

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Squirrel monkeys are neotropical primates that have high circulating cortisol to compensate for expression of glucocorticoid receptors (GRs) with reduced affinity. The low binding affinity of squirrel monkey GR does not result from substitutions in the receptor, because squirrel monkey GR expressed in vitro exhibits high affinity. Rather, squirrel monkeys express a soluble factor that, in mixing studies of cytosol from squirrel monkey lymphocytes (SML) and mouse L929 cells, reduced GR binding affinity by 11-fold. In an effort to identify this factor, the cellular levels of components of the GR heterocomplex in SML and human lymphocytes (HL) were compared. The immunophilin FKBP51 was 13-fold higher in SML than in HL cytosol; FKBP52 in SML was 42% of that in HL cytosol. A role for changes in immunophilins, causing glucocorticoid resistance in neotropical primates, is supported by the following: the changes in FKBP51 and FKBP52 were observed in cells from other neotropical primates with glucocorticoid resistance; the elevated level of FKBP51 was reflected in an abundance of FKBP51 in heat shock protein 90 complexes in SML; when cytosols of SML and L929 cells were mixed, the decrease in GR binding was associated with incorporation of FKBP51 into GR heterocomplexes; the effect of SML cytosol on GR binding was reproduced with cytosol from COS cells expressing squirrel monkey FKBP51; and both the effect of SML cytosol on GR binding and the incorporation of FKBP51 into GR heterocomplexes were blocked by FK506. Regulation of GR binding by FKBP51 represents a previously unrecognized mechanism for regulating glucocorticoid sensitivity. (J Clin Endocrinol Metab 84: [663][664][665][666][667][668][669] 1999) G LUCOCORTICOIDS play an essential role in regulating many developmental and physiological processes (1). The actions of glucocorticoids are mediated by the glucocorticoid receptor (GR), a member of the steroid hormone receptor superfamily (2). The GR protein is made up of an aminoterminal transactivation domain, a central DNA-binding domain, and a carboxyterminus that includes the ligandbinding domain and sequences involved in interaction with heat shock proteins (hsps) (3). In the unliganded state, the GR resides in the cytoplasm associated with hsps and other chaperone proteins, forming a multiprotein complex (4). The ordered association of chaperone complexes with the GR is critical in establishing a receptor conformation optimally responsive to hormone (4).Our recent studies have focused on the mechanisms of glucocorticoid insensitivity in species of neotropical primates. Squirrel monkeys, cotton-top tamarins, and owl monkeys have markedly elevated plasma cortisol levels, but they show no signs of glucocorticoid excess (5, 6). They have been proposed as models for the in vivo study of glucocorticoid sensitivity (3, 5). Chrousos et al. (5) demonstrated a greater than 20-fold higher apparent dissociation constant for the GR in squirrel monkey mononuclear leukocytes than in human cells, suggesting that a dec...

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“…An amount of 4–5 mL whole blood was sampled from a cynomolgus monkey, followed by the isolation of lymphocyte cells. The B-lymphocyte cell line was established according to Scammell et al [ 41 ].…”

Section: Methodsmentioning

confidence: 99%

Analysis of 10,000 ESTs from lymphocytes of the cynomolgus monkey to improve our understanding of its immune system

Wang

Lin

et al. 2006

BMC Genomics

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BackgroundThe cynomolgus monkey (Macaca fascicularis) is one of the most widely used surrogate animal models for an increasing number of human diseases and vaccines, especially immune-system-related ones. Towards a better understanding of the gene expression background upon its immunogenetics, we constructed a cDNA library from Epstein-Barr virus (EBV)-transformed B lymphocytes of a cynomolgus monkey and sequenced 10,000 randomly picked clones.ResultsAfter processing, 8,312 high-quality expressed sequence tags (ESTs) were generated and assembled into 3,728 unigenes. Annotations of these uniquely expressed transcripts demonstrated that out of the 2,524 open reading frame (ORF) positive unigenes (mitochondrial and ribosomal sequences were not included), 98.8% shared significant similarities (E-value less than 1e-10) with the NCBI nucleotide (nt) database, while only 67.7% (E-value less than 1e-5) did so with the NCBI non-redundant protein (nr) database. Further analysis revealed that 90.0% of the unigenes that shared no similarities to the nr database could be assigned to human chromosomes, in which 75 did not match significantly to any cynomolgus monkey and human ESTs. The mapping regions to known human genes on the human genome were described in detail. The protein family and domain analysis revealed that the first, second and fourth of the most abundantly expressed protein families were all assigned to immunoglobulin and major histocompatibility complex (MHC)-related proteins. The expression profiles of these genes were compared with that of homologous genes in human blood, lymph nodes and a RAMOS cell line, which demonstrated expression changes after transformation with EBV. The degree of sequence similarity of the MHC class I and II genes to the human reference sequences was evaluated. The results indicated that class I molecules showed weak amino acid identities (<90%), while class II showed slightly higher ones.ConclusionThese results indicated that the genes expressed in the cynomolgus monkey could be used to identify novel protein-coding genes and revise those incomplete or incorrect annotations in the human genome by comparative methods, since the old world monkeys and humans share high similarities at the molecular level, especially within coding regions. The identification of multiple genes involved in the immune response, their sequence variations to the human homologues, and their responses to EBV infection could provide useful information to improve our understanding of the cynomolgus monkey immune system.

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An EBV-transformed owl monkey B-lymphocyte cell line

Cited by 14 publications

References 12 publications

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP51¹

Analysis of 10,000 ESTs from lymphocytes of the cynomolgus monkey to improve our understanding of its immune system

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An EBV-transformed owl monkey B-lymphocyte cell line

Cited by 14 publications

References 12 publications

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

Multi-directional chromosome painting maps homologies between species belonging to three genera of New World monkeys and humans

Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP511

Analysis of 10,000 ESTs from lymphocytes of the cynomolgus monkey to improve our understanding of its immune system

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Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP51¹