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X J Ma

Publications and source records attributed to X J Ma.

At least 37 records · Page 2Linked to original sources
PubMed1998

Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast.

Histone H4 can be acetylated at N-terminal lysines K5, K8, K12, and K16, but newly synthesized H4 is diacetylated at K5/K12 in diverse organisms. This pattern is widely thought to be important for histone deposition onto replicating DNA. To investigate the importance of K5/K12 we have mutagenized these lysines in yeast and assayed for nucleosome assembly. Assaying was done in the absence of the histone H3 N terminus, which has functions redundant with those of H4 in histone deposition. Nucleosome assembly was assayed by three methods. Because nucleosome depletion may be lethal, we examined cell viability. We also analyzed nucleosome assembly in vivo and in vitro by examining plasmid superhelicity density in whole cells and supercoiling in yeast cell extracts. All three approaches demonstrate that mutagenizing K5 and K12 together does not prevent cell growth and histone deposition in vivo or in vitro. Therefore, K5/K12 cannot be required for nucleosome assembly in yeast. It is only when the first three sites of acetylation-K5, K8, and K12-are mutagenized simultaneously that lethality occurs and assembly is most strongly decreased both in vivo and in vitro. These data argue for the redundancy of sites K5, K8, and K12 in the deposition of yeast histone H4.

Acetylation↗
PubMed1997

[The expression of Quox-1 gene homologous sequence in the development of early human embryos].

By using the b2 fragment of Quox-1 gene as probe, we have confirmed that the Quox-1 gene homologous sequence exists in the human genome according to the results of Southern blot. Studies on the expression of Quox-1 homologous sequence in early human embryos from 26 to 37 days by means of immunohistochemistry technigue with Quox-1 protein antibodies showed the spatiotemporal expression patterns: in 26 days embryo Quox-1 homologous sequence was expressed in many places including neural tube, but 30 days later, tits expression sites were limited to notochord, digestive epithelium, myotome, cardiac muscle cell and periderm. The functions in control and regulation of Quox-1 gene homologous sequence during the early development of human embryo were discussed.

Animals↗
PubMed1996

A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae.

In a genetic screen for second-site mutations that are lethal in combination with a deletion of the amino terminus of histone H3, we have uncovered three new gene products that regulate the Saccharomyces cerevisiae Swe1 kinase. The Swe1 protein kinase phosphorylates tyrosine residue 19 of Cdc28 and inhibits its activity. One histone synthetic-lethal gene, HSL1, encodes a putative protein kinase that has high sequence and functional homology to fission yeast cdr1/nim1, an inhibitory kinase of wee1. Another gene, HSL7, is a novel negative regulator of Swe1 function. Sequences similar to Hsl7 exist in Caenorhabditis elegans and humans. In addition, we have isolated a dosage-dependent suppressor, OSS1, of hsl1 and hsl7. OSS1 is important for the transcriptional repression of SWE1 and CLN2 in G2. Mutations in HSL1 and HSL7 therefore cause hyperactivity of the Swe1 kinase, which in turn decreases mitotic Cdc28 kinase activity. Moreover, HSL5 is identical to CDC28, further suggesting that it is the decreased Cdc28 kinase activity in these hsl mutants that causes lethality in the histone mutant background. Because neither HSL1 nor HSL7 is essential in yeast, and histone transcription is unaffected by the hsl5/cdc28 mutation, it is unlikely that synthetic lethality results from reduced transcription of HSL1 and HSL7 caused by histone mutations, or from reduced histone transcription when Cdc28 kinase activity is compromised. We suggest that these cell cycle regulators function in a pathway upstream of both histones H3 and H4, thereby modulating histone function in the cell cycle.

Amino Acid Sequence↗
PubMed1996

[Venous protection of acute leukemia treatment with amsacrine].

Amsacrine (AMSA) was a high effective medicine of acute leukemia treatment. But it could lead to severe phlebitis with venous drip. 44 patients were treated 71 courses with AMSA. After we used fasting venous drip and diluting high concentration AMSA, occurrence of phlebitis remarkably decreased and patients of phlebitis could be cured with early comprehensive nursing.

Acute Disease↗
PubMed1995

Putative mechanism for guinea pig ileum contraction by N-formyl peptides. A comparative study of N-formyl and N-acetyl peptides with the N-terminal sequence of the calpain small subunit.

N-formyl and N-acetyl peptides with the N-terminal sequence of the calpain small subunit were prepared and their spasmogenic activity was examined using guinea pig ileum preparations. Sections of ileum were found to contract in the presence of all N-formyl peptides used (tri- to nonapeptides and tridecapeptide) but failed to contract with N-acetyl peptides, although both N-formyl and N-acetyl peptides have chemotactic activity, indicating that spasmogenic activity and chemotactic activity involve different mechanisms. A formyl peptide antagonist, Boc-Phe-Leu-Phe-Leu-Phe, suppressed contraction by formyl peptides whereas a histamine antagonist, diphenhydramine, suppressed contraction by formyl peptides as well as by histamine. In addition, formyl peptide-induced contractions were noted after an approximately 20-sec time lag, and their profiles were bell-shaped and roughly symmetrical. On the other hand, histamine- and acetylcholine-induced contractions exhibited a much shorter time lag. These data led us to conclude that contraction induced by formyl peptides may not occur as a direct response but may be due to the histamine released from mast cells present in the tissues of the small intestine.

Amino Acid Sequence↗
PubMed1995

Neutrophil chemotactic N-acetyl peptides from the calpain small subunit are also chemotactic for immunocytes.

N-terminal peptides from the calpain small subunit were shown to have dose-dependent chemotactic activity toward several types of leukemia cells: T cell, B cell, monocyte and granulocyte/monocyte line leukemia cells. In order to prove that chemotaxis is mediated via receptors, a fluorescein-labeled probe was prepared from one of the N-terminal peptides and its interaction with peripheral leukocytes was estimated by means of flow cytometry, resulting in staining not only of neutrophils but also of most of the monocytes and more than half of the T and B lymphocytes. The results indicate that calpain-derived N-terminal peptides may be involved in defense mechanisms, inducing chemotaxis of immunocytes as well as that of neutrophils.

Amino Acid Sequence↗
PubMed1993

Neutrophil responses induced by formyl and acetyl peptides with the N-terminal sequence of the calpain small subunit.

A series of formylated and acetylated peptides with the amino terminal sequence of the small subunit of human calpains were prepared and their neutrophil activating potency was examined. Formyl peptides showed dose-dependent superoxide generation and elastase/myeloperoxidase releasing activity in addition to chemotactic activity whereas acetyl peptides showed only chemotactic activity and neither superoxide generation nor degranulation activity was detected. These results imply that acetyl peptides from the calpain small subunit might be moderate neutrophil chemotactic factors which do not produce bacteriocidal and cytotoxic effects.

Acetylation↗
PubMed1992

Nutritional regulation of nucleosomal structure at the chicken malic enzyme promoter in liver.

Transcription of the chicken malic enzyme gene in the liver is stimulated by feeding and inhibited by starvation. Concomitant with the increase in transcription caused by refeeding, chromatin structure around the transcription start site of the malic enzyme gene is modified in the liver. Digestion of chromatin in isolated nuclei with DNase I revealed four feeding-induced DNase I hypersensitive sites (-220, -170, -130 and -70 bp) near the malic enzyme promoter. Similarly, digestion of chromatin with restriction endonucleases detected enhanced cleavage within this region when birds were refed. Micrococcal nuclease detected the presence of nucleosomes over this region in the starved state, but not in the fed state. After food was withdrawn from fed birds, nucleosomes were reformed in this region within 6 h. The speed and magnitude of the changes in nucleosomal structure in this region suggest that they did not require DNA replication.

Animals↗
PubMed1991

Triiodothyronine stimulates and cyclic AMP inhibits transcription of the gene for malic enzyme in chick embryo hepatocytes in culture.

In chick embryo hepatocytes in culture, insulin and triiodothyronine (T3) increase malic enzyme activity and the abundance of malic enzyme mRNA by at least 50-fold, and glucagon or cAMP blocks this effect. Steps regulated by these hormones were defined by measuring transcriptional activity with the nuclear run-on assay and multiple fragments of the malic enzyme gene as probes. T3 alone caused a significant increase in transcription within 1 h, with a maximal increase of 30-40-fold occurring by 24 h. When T3 was added with insulin, 80% of the maximum rate was reached in 1 h. Insulin alone had no effect on transcription of the malic enzyme gene; it amplified the response to T3 in the first few hours after adding T3 but did not alter T3's maximal effect. Cyclic AMP for 1 h completely inhibited the increase in transcription caused by T3. The size and speed of the responses of the malic enzyme gene to T3 and cAMP suggest regulation of transcription initiation. T3-stimulated transcription of the malic enzyme gene did not require ongoing protein synthesis despite the fact that inhibitors of protein synthesis inhibited the T3-stimulated accumulation of its mRNA. T3 may directly activate transcription of this gene via its receptor. The pattern of DNase I hypersensitivity of the malic enzyme gene in chick embryo hepatocytes was the same as that in fed chick liver. Insulin, T3, and cAMP had no effect on that pattern. In chick embryo hepatocytes in culture, factors involved in regulation of transcription by insulin, T3, and cAMP may be bound to DNA independently of hormonal treatment.

Animals↗
PubMed1991

A differentiation stage-specific factor interacts with mouse carbonic anhydrase form I gene and a conserved sequence in mammalian beta-globin genes.

We have identified in mouse erythroleukemic (MEL) cells a novel factor which binds to the 3' flanking region of beta-globin genes. Upon induction, this DNA binding factor disappears as beta-globin gene transcription increases. The factor protects 20-30 base pairs (bp) of a sequence which is tightly conserved in beta-globin genes including chicken, human, mouse and rabbit. A very similar sequence binds the factor in the mouse carbonic anhydrase form I gene, whose transcription diminishes upon induction of MEL cells. The factor, or a closely related form, is detected in nonerythroid cells and binding sites have been detected in other genes, including c-myb and immunoglobulin heavy chain-enhancer. We suggest that this factor could play a role in determining the timing of gene expression in several differentiating cell types.

Animals↗
PubMed1991

Calpain and kininogen mediated inflammation.

On the basis of previous findings that N-acetyl nonapeptide from the human calpain I large subunit has chemotactic activity for neutrophils, more than 30N-acetyl and unmodified peptides which have N-terminal amino acid sequences of the large and small subunits of calpains I and II were synthesized and their chemotactic activity was estimated. In addition to the above N-acetyl nonapeptide from the calpain I large subunit, an unmodified nonapeptide from the calpain II large subunit and several N-acetyl peptides of different lengths from the small subunit showed chemotactic activity. Furthermore, when calpain was incubated with either high molecular weight or low molecular weight kininogen, kinin liberation occurred with simultaneous inhibition of calpain by kininogen. These data suggest that chemical mediators generated from the calpain-kininogen system may participate in migration and accumulation of neutrophils to the inflammatory locus.

Amino Acid Sequence↗
PubMed1990

Nutritional regulation and tissue-specific expression of the malic enzyme gene in the chicken. Transcriptional control and chromatin structure.

Refeeding starved chicks causes a 25- to 50-fold increase in the level of malic enzyme mRNA in liver. To define the regulated steps, we measured transcriptional activity of the malic enzyme gene using the nuclear run-on assay and a variety of DNA probes specific to the malic enzyme gene. Refeeding starved chicks stimulated transcription of the malic enzyme gene in liver by 40- to 50-fold. An increased transcription rate was detectable at 1.5 h, was maximal at 3 h, and remained high at 24 h of refeeding. The level of nuclear precursor RNA for malic enzyme assessed by hybridization with intron-specific probes was high in liver of refed birds, and barely detectable in that of starved birds. These results indicate that nutritional regulation of the level of malic enzyme mRNA is transcriptional. Low levels of malic enzyme mRNA in brain, kidney, and heart correlated well with low rates of transcription of the malic enzyme gene in these tissues. In contrast to liver, neither the rate of transcription nor the steady-state level of malic enzyme mRNA was affected by refeeding starved birds. A series of DNase I-hypersensitive sites were located within 4000 base pairs upstream of the transcription start site of the malic enzyme gene in liver. The DNase I-hypersensitive region extending from the start of transcription to 400 base pairs upstream was much more pronounced in the refed state than in the starved state. This change in DNase I hypersensitivity followed the same time course as increased transcription of the malic enzyme gene. This DNase I-hypersensitive region also was present at low intensity in kidney and heart independently of nutritional state. The three constitutive DNase I-hypersensitive sites further upstream were present in liver but not in kidney or heart.

Animal Nutritional Physiological Phenomena↗
PubMed1990

Neutrophil chemotactic activity of N-terminal peptides from the calpain small subunit.

On the basis of previous findings that N-acetyl nonapeptide from the human calpain I large subunit has chemotactic activity for neutrophils, a series of peptides with the N-terminal sequence of the calpain small subunit were synthesized and their chemotactic activity was examined. Potent activity was found in N-acetyl tetra, hepta, octa, nona and a larger peptide of 13 residues, although N-acetyl tripeptide showed only weak activity and N-acetyl penta and hexa peptides showed almost no activity. Since the small subunit is identical in calpains I and II, the results indicate that both calpains could be precursor proteins of chemotactic factors for neutrophils.

Amino Acid Sequence↗