A major single-stranded DNA binding protein from ovaries of the frog, Xenopus laevis, is lactate dehydrogenase

Kaiserman, H. B.; Odenwald, Ward F.; Stowers, Deborah J.; Poll, E. H. A.; Benbow, Robert M.

doi:10.1016/0167-4781(89)90165-6

Cited by 8 publications

(2 citation statements)

References 26 publications

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“…Sperm-specific LDH, which exists only in testis, plays important role in the immune system (Gupta and Chaturvedi 2000). In addition to enzymatic activity, LDH has the DNA binding property Grosse et al 1986;Sharief et al 1986;Kaiserman et al 1989). Moreover, LDH is localized in nucleus of several cells .…”

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confidence: 99%

Lactate dehydrogenase enhances immunoglobulin production by human hybridoma and human peripheral blood lymphocytes

Takenouchi

Sugahara

2003

Cytotechnology

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Lactate dehydrogenase (LDH) derived from rabbit muscle enhanced IgM production by human-human hybridoma HB4C5 cells 12.4-fold at 320 g/ml under serum-free conditions. LDHs from pig muscle and pig heart also accelerated IgM production 8.4-and 6.4-fold, respectively. The immunoglobulin production stimulating activity of LDH was not accompanied by activation of cell proliferation. LDH from rabbit muscle facilitated IgM and IgG production by human peripheral blood lymphocytes. This means LDH stimulates immunoglobulin production not only by the specified hybridoma cell line, but also by unspecified immunoglobulin producers. LDH from rabbit muscle enhanced IgM production of transcription-suppressed HB4C5 cells treated with actinomycin D. The immunoglobulin production-stimulating factors (IPSFs) effect of LDH was slightly weakened by sodium fluoride (translation inhibitor) treatment of HB4C5. Moreover, the amount of intracellular IgM of monensin-treated HB4C5 cells was obviously enhanced by LDH. This result means that the IPSF effect of LDH is irrelevant to the post-translation activity of target cells. It is expected from these findings that LDH from rabbit muscle accelerates the translation step to enhance immunoglobulin productivity. The immunoglobulin production-stimulating activity of LDH was inhibited by colchicine, endocytosis inhibitor. This fact suggests that it is necessary for LDH to be taken by target cells to act as an IPSF.

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Section: Introductionmentioning

confidence: 99%

Lactate dehydrogenase enhances immunoglobulin production by human hybridoma and human peripheral blood lymphocytes

Takenouchi

Sugahara

2003

Cytotechnology

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“…Protein interactions with double-stranded and single-stranded DNA are the key element in the complex schemes of the replication, recombination or repair of the genetic material (Kaiserman et al 1989). It is well recognized that a large number of heterotropic DNA-protein interactions governs these dynamic processes (van der Knapp et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Application of capillary electrophoresis for DNA-protein binding tests

Kaźmierczak

Kaźmièrczak

2003

Acta Physiol Plant

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The combination of affinity chromatography and capillary electrophoresis (CE-SDS) has been found to be a useful tool to analyse populations of proteins which specifically bind to ssor dsDNA. Proteins were extracted from tissue, cytosol or nuclei of meristems ofPisum sativum seedlings and separated on cellulose column functionalized with ss-, dsDNA (calf thymus) and ssDNA (P. sativum) at 2M concentration of sodium chloride. Electropherograms of the crude protein extracts show two fractions of proteins specific for dsDNA (calf thymus) and three fractions specific for ssDNA (calf thymus). Four and five fractions of proteins specific for ssDNA (P. sativum) were identified in the material isolated from cytosolic and nuclear extracts, respectively. Both ds-and ssDNA (calf thymus) form complexes with ca. 4.0 % of the total amount of proteins, while ssDNA (P. sativum) binds to ca. 11.0 % of cytosolic and 5.0 % of nuclear proteins.List of abbreviations: CE -capillary electrophoresis; DSB -double-stranded DNA-binding protein ds -double-stranded; ss -single-stranded; SSBsingle-stranded DNA-binding protein

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Expression of mitochondrial genes and DNA-repair-related nuclear genes is altered in xeroderma pigmentosum fibroblasts

Xia

Werner

Popanda

et al. 1994

J Cancer Res Clin Oncol

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Differential hybridization was used to detect repair defects in xeroderma pigmentosum (XP) that are not amenable to current analyses. cDNA libraries were constructed from cytoplasmic RNA of normal and XP fibroblast strains (complementation groups A and D) and analyzed for differential gene expression. More than 40,000 lambda gt10 cDNA clones were differentially screened with in vitro transcripts made from cDNA in the pBluescript vector. Six differential clones were detected in the libraries of the XP group A and D strains which caused stronger or weaker signals when probed with transcripts from XP strains than with those from the normal strains. Two clones coded for mitochondrial genes: mitochondrial 16 S rRNA and ATPase 6L. Overexpression of mitochondrial genes in XP may indicate that functions of the ATP-generating system are impaired since such functions are intensified whenever they become insufficient, for example as a consequence of DNA damage. It is tempting to assume that abnormal mitochondria are one of the causes for the neurological malfunctions in XP. Furthermore, densitometric analysis of Northern blots revealed that mRNA of lactate dehydrogenase, chain M, was less abundant in four XP group A strains (extent of reduction: 70%) and in two XP group D strains (extent of reduction: 58%). Enzyme activity was also diminished. In addition, mRNA of the gene for glyceraldehyde-3-phosphate dehydrogenase was less expressed in the same XP group A and D fibroblast strains investigated (reduction in both complementation groups: 50%). Both glycolytic enzymes have nuclear functions apart from their role in sugar metabolism. Lactate dehydrogenase, chain M, is identical to a helix-destabilizing protein; it is closely associated with chromatin and unfolded DNA, suggesting a role in DNA synthesis and transcription. The 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase is involved in transcription and was shown to be identical to uracil-DNA glycosylase, a base-excision repair enzyme. We presume that the nuclear functions of these glycolytic enzymes may be thwarted in the XP strains investigated and may account for malfunctions in XP, particularly for neurological disturbances.

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A major single-stranded DNA binding protein from ovaries of the frog, Xenopus laevis, is lactate dehydrogenase

Cited by 8 publications

References 26 publications

Lactate dehydrogenase enhances immunoglobulin production by human hybridoma and human peripheral blood lymphocytes

Lactate dehydrogenase enhances immunoglobulin production by human hybridoma and human peripheral blood lymphocytes

Application of capillary electrophoresis for DNA-protein binding tests

Expression of mitochondrial genes and DNA-repair-related nuclear genes is altered in xeroderma pigmentosum fibroblasts

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