Mononuclear cells separated from heparinized fresh venous blood of healthy male bloodclonors by means of Ficoll- Hypaque density gradient centrifugation were subjected to petri dish adhesion and nylon wool-column separation to obtain monocytes and T lymphocytes of high purity, respectively. Antigen- presenting capability of the monocytes, as reflected by T lymphocyte proliferation, was assayed after the monocytes had been preincubated with PPD (purified protein derivative, end concentration12.5 ?g /ml ) and methione enkephalin (M-Enk) in defferent concentrations for 24 hours at 37 ℃ in a humidified incubator containing 5% CO_2. It was shown that the antigen-presenting capability of the monocytes was markedly enhanced by M-Enk when its concentration was from 10 ~(-10) M to 10~(-14) M(close to the normal serum concentration of M-Enk), and this effect of M-Enk could be cancelled if the monocytes had been pretreated with 10~(-6) M naloxone for 30 min before addition of PPD and M-Enk, suggesting that the effect of M-Enk in these concentrations was mediated through the opioid receptors on the monocytes. M-Enk in high concentrations (10~(-4) M-10~(-6)), however, was found to inhibit th'e antigen- presenting capability significantly and this inhibition could not be cancelled by pretreatment of the monocytes with naloxone.

Mononuclear cells obtained from heparinized fresh venous blood of healthy male blood donors by means of Ficoll-Hypaque densitz gradient centrifugation were subjected to petri dish adhesion and nylon-wool-column separation to harvest monocytes (Mon) and T lymphocytes (T) high purity, respectively. APF of Mon, as reflected by ~3H-TdR incorporated T proliferation, was assayed after the Mon had been preincubated with PPD (purified protein derivative, end concentration 9.25 ?g/ml), PPD+ascorbic acid, PPD+cortisol, and PPD+ascorbic acid+cortisol for 24 hours at 37℃, in a humidified incubator containing 5% CO_2. It was shown that APF of the Mon was markedly enhanced by ascorbic acid in a concentration of 3.75mM (P0.05).

Insulin has been found to enhance specific immune function in experimental animals. However, it remains hitherto unnoticed whether the antigen-presenting capability and expression of Ia antigens of the macrophage, known to be essential for the induction of both cell-mediated immunity and humoral immune response to most antigens, could also be influenced by insulin. In the present study, it was demonstrated that insulin, in a concentration of 1.03?10~(-7) mol/L, promoted the antigen-presenting capability of human monocytes significantly. Furthermore, we found that the expression of HLADQ antigen on monocytes was markedly enhanced by insulin while that of HLA-DR determinant was not affected significantly. We suggested, therefore, that the promotion of antigen-presenting capability of human monocytes by insulin may be attributed, at least in part, to its enhancing effect on the expression of HLA-DQ antigen on the monocytes.

When the central nervous system is stimulated, the opioid neuropeptide?-endorphine (?-EP) is liberated into the blood stream. The result of this work showedthat the antigen-presenting capability (APCP) of normal human monocytes (Mon) wasmarkedly enhanced (P0. 05), sug-gesting that the effect of ?-EP was mediated through the opioid receptors on the Mon.

[Objective]To observe the effect of Homoharringtonine on Adjuvant Arthritis Rats.[Methods]Observe the effect of Homoharringtonine on Adjuvant Arthritis Rats’ SP,IL-1? and TNF-?;we take the Adjuvant Arthritis Rats as model and Tripterygium wilfordii polycoside was the positive group.[Results]The Homoharringtonine and Tripterygium wilfordii polycoside group’s level of TNF-?,IL-1? in the serum and synovial membrane decreased instructively,and their dose of SP in the plasma and synovial membrane was suppressed obviously too.[Conclusion]Homoharringtonine has the effect of anti-inflammation,it may treat the Adjuvant Arthritis Rats through reducing the dose of TNF-?,IL-1? in the serum and synovial membrane,inhibiting the secretion and releasing SP in the plasma and synovial membrane.

Cell-cycle deregulation leading to excessive cellproliferation is an important mechanism of human tumorigenesis. CDK6 and CDK4 have been found to be significant regulators of cellcycle, particularly in promoting cell -cycle progress. Moreover, these proteins are usually overly active in most tumors and closely related to tumor development. Recently, research has confirmed CDK4/6 as prospective targets for cancer therapy. However, the mechanism of excessive CDK6 activation leading to tumorigenesis is not completely understood. Therefore, further understanding of the role of CDK4/6 in cell -cycle regulatory pathways and celldifferenti-ation is essential, as well as their overexpression in different types of tumors. This information will elucidate the mechanisms of tumor development and treatment. Therefore, this review intends to discuss the structure and biological function of CDK6, the role and mecha-nism of CDK6 in carcinogenesis, and the clinical application of CDK6 inhibitors.

The aim of this study was to look for the chemical constituents from the rhizomes of Dryopteris sublaeta. The fresh plant was extracted twice with boiling water, the extract was concentrated to small volume under reduced pressure at 50 ℃. The concentrated material was partitioned with ether, ethyl acetate and n-butanol. The fraction of ethyl acetate was repeatedly chromatographied over silica gel and Sephadex LH-20 columns. Structures of pure compounds were established on the basis of their physiochemical and spectral data. Nine compounds were obtained and identified as sublaetentin A (1), sublaetentin B (2), sublaetentin C (3), sublaetentin D (4), matteuorienate A (5), matteuorienate C (6), arbutin (7), 3-methoxy-4-hydroxyphenyl-1-O-β-D-glucopyranoside (8) and 3,4-dimethoxyphenyl-1-O-β-D-glucopyranoside (9). Compounds 1-4 are new compounds, the others were isolated from this plant for the first time.

Aim To study the chemical constituents of Dryopteris sublaeta Ching et Hsu. Methods Fresh plant of Dryopteris sublaeta Ching et Hsu was extracted twice with boiling water, concentrated to small volume under reduced pressure at 50 ℃. The concentrated material was partitioned with ether, ethyl acetate, and n-butanol. The fraction of ethyl acetate extract was chromatographed over macroporous adsorption resin (Diaion HP-20) eluted with a mixture of H2O and MeOH in increasing MeOH content.Their fractions from resin were repeatedly chromatographed over Toyopearl HW-40, Sephadex LH-20 and silica gel column chromatography. The compounds were identified on the basis of their physiochemical and spectral data. Results Four compounds were obtained and identified as 3,5-dihydroxy-stilbene-3-O-neohesperidoside ( 1 ), 3,5-dihydroxy-stilbene-3-O-β-D-glucoside ( 2 ), polydotin peceid (3) and 3,5,4'-trihydroxy-bibenzyl-3-O-β-D-glucoside (4). Conclusion Compound 1 is a new compound, the others were isolated from Dryopteris for the first time.

Aim To study the chemical constituents of Dryopteris sublaeta Ching et Hsu. Methods Fresh plant of Dryopteris sublaeta Ching et Hsu was extracted twice with boiling water, the extract was concentrated to small volume under reduced pressure at 50 ℃. The concentrated material was partitioned with ether, ethyl acetate, and n-butanol. The fraction of ether extract was chromatographed over silica gel column. The compounds were identified on the basis of their physiochemical and spectral data. Results Four compounds were obtained and identified as 2 (S)-5,7, 3'-trihydroxy-6,8-dimethy1-5'-methoxyflavanone ( 1 ), matteucinol ( 2 ), desmethoxymatteucinol ( 3 ) and 5,7,2'-trihydroxy-6,8-dimethy1-flavanone (4). Conclusion Compound 1 is a new one, the others were isolated from Dryopteris for the first time.

Background and purpose:Inhibitor of apoptosis-stimulating protein of p53 (iASPP) is one of the ASPP family. It binds to p53 to inhibit the transcriptional activity of p53-target genes and cell apoptosis, which is asso-ciated with tumor formation. Previously, we found a new subtype of iASPP, iASPP splice variant (iASPP-SV), which is a nuclear protein containing 407 amino acid residues and can bind to p53, inhibiting p53 transcriptional activity. However, the relationship of iASPP-SV and breast cancer is still obscure. Therefore, the purpose of this research was to study the role of iASPP-SV on breast cancer tumorigenesis and progression.Methods:5’-rapid ampliifcation of cDNA ends (RACE) was used to identify the 5’-end of iASPP-SV mRNA in MCF-7 cells. HEK 293 cells were transfected with pFLAG-iASPP-SV and pFLAG-iASPP (828). Then Western blot was used to identify whether endogenous iASPP-SV was expressed in HEK 293 cells and 8 types of human tumor cell lines. This study established the stable clones of NIH 3T3 expressing FLAG-iASPP-SV and FLAG-iASPP (828). Cell proliferation assay, colony formation and soft agar colony formation assay were used to identify whether iASPP-SV and iASPP (828) can promote cell proliferation and iASPP-SV is an oncogene. Real-time lfuorescent quantitative polymerase chain reactive (RTFQ-PCR) was used to de-tect the levels of iASPP-SV and iASPP (828) mRNA in primary breast cancers. Luciferase assays were used to identify the relationships between iASPP-SV, iASPP (828), p53 and NF-κB p65.Results:The study identiifed that iASPP-SV was encoded by previously reported NF-κB p65 subunit (RelA)-associated inhibitor (RAI), and endogenously expressed in many human cancer cell lines. Analysis of cell proliferation, colony formation assay and soft agar assay for colony formation identiifed that similarly to iASPP (828), iASPP-SV promoted tumor cell proliferation and acted as an onco-gene. RTFQ-PCR result showed that the median values of iASPP-SV and iASPP (828) in breast cancers with wild-type p53 were more signiifcantly over-expressed than those of mutant p53. Luciferase assays showed that iASPP-SV and iASPP (828) could suppress NF-κB p65 transcriptional activity. Thus iASPP family may participate in the regulation of p53 and NF-κB activity, which imply that iASPP perhaps shows pro- or anti-survival activities when it interacts with different proteins.Conclusion:These ifndings indicate that iASPP-SV may be a potential target for breast cancer thera-py.