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Biomedical subjects

W Xia

Publications and source records attributed to W Xia.

At least 73 records · Page 4Linked to original sources
PubMed1999

[Determination on chemical constituents of Curcuma L. produced in China].

OBJECTIVE: To provide some valuable information for the research on species systematization and quality standardization of Curcuma drugs. METHODS: Colorimetry, TLC-colorimetry and water vapour distillation were used to determine the contents of curcuminoids, curcumin and essential oils of 34 samples of Curcuma produced in China. RESULTS AND CONCLUSION: The contents of curcuminoids and curcumin are different upto an extent of over 100 times among the varieties of Curcuma, and those of essential oils to an extent of 6 times. But there is little difference in the samples of the same species from different producing areas. There is also an obvious correlativity between the contents of curcuminoids and essential oils in the varieties of curcuma.

Curcuma↗
PubMed1999

[Evaluation of the risk of vertebral fracture predictable with quantitative tibial ultrasound velocity test in postmenopausal women].

OBJECTIVE: To investigate predicting value of increased risk of vertebral fracture associated with reduction of tibial ultrasound velocity (SOS) test in postmenopausal women. METHODS: 193 menopausal women aged(54.4 +/- 7.3) years were included in our study. Post menopausal period of these subjects were (16.0 +/- 7.8) years. These participants received tibial ultrasound speed (SOS) test, DEXA for lumbar 2-4, femoral neck wards triangle and trochant, as well as SPA for 1/3 and 1/10 of distal forearm. Vertebral fracture was determined by radiograph of lateral lumbar and thoracic spine. RESULTS: 54 subjects were found at least one vertebral deformation, and no vertebral deformation was found in other 139 subjects. Tibial SOS was significantly lower in subjects with than without vertebral fracture [(3,651.9 +/- 188.3) vs (3,731.3 +/- 140.8), P < 0.01], The similar results were also found in BMD. The analysis of logistic regression showed: odds ratio (OR) of SOS to vertebral fracture was 1.86(P < 0.01) when 1 standard deviation of SOS changed. It was lower than OR of BMD by DEXA(2.25-3.28, all P < 0.001), and similar with OR of BMD by SPA (1.50-1.96). CONCLUSIONS: Low SOS was associated with presence of vertebral fracture in postmenopausal women. SOS could predict the risk of vertebral fracture, 86% of the risk of vertebral fracture increased when 1 standard deviation of SOS reduced.

Aged↗
PubMed1998

Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi.

Progressive cerebral deposition of the amyloid beta-protein (Abeta) is believed to play a pivotal role in the pathogenesis of Alzheimer's disease (AD). The highly amyloidogenic 42-residue form of Abeta (Abeta42) is the first species to be deposited in both sporadic and familial AD. Mutations in two familial AD-linked genes, presenilins 1 (PS1) and 2 (PS2), selectively increase the production of Abeta42 in cultured cells and the brains of transgenic mice, and gene deletion of PS1 shows that it is required for normal gamma-secretase cleavage of the beta-amyloid precursor protein (APP) to generate Abeta. To establish the subcellular localization of the PS1 regulation of APP processing to Abeta, fibroblasts from PS1 wild-type (wt) or knockout (KO) embryos as well as Chinese hamster ovary (CHO) cells stably transfected with wt or mutant PS1 were subjected to subcellular fractionation on discontinuous Iodixanol gradients. APP C-terminal fragments (CTF) were markedly increased in both endoplasmic reticulum- (ER-) and Golgi-rich fractions of fibroblasts from KO mice; moreover, similar increases were documented directly in KO brain tissue. No change in the subcellular distribution of full-length APP was detectable in fibroblasts lacking PS1. In CHO cells, a small portion of APP, principally the N-glycosylated isoform, formed complexes with PS1 in both ER- and Golgi-rich fractions, as detected by coimmunoprecipitation. When the same fractions were analyzed by enzyme-linked immunosorbent assays for Abetatotal and Abeta42, Abeta42 was the major Abeta species in the ER fraction (Abeta42:Abetatotal ratio 0.5-1.0), whereas absolute levels of both Abeta42 and Abeta40 were higher in the Golgi fraction and the Abeta42:Abetatoal ratio was 0.05-0.16 there. Mutant PS1 significantly increased Abeta42 levels in the Golgi fraction. Our results indicate PS1 and APP can interact in the ER and Golgi, where PS1 is required for proper gamma-secretase processing of APP CTFs, and that PS1 mutations augment Abeta42 levels principally in Golgi-like vesicles.

Alzheimer Disease↗
PubMed1998

Adenovirus 5 E1A-mediated tumor suppression associated with E1A-mediated apoptosis in vivo.

Disruption of apoptotic pathways is a major factor in the multistep process of tumorigenesis, whereas induction of apoptosis can be important for tumor suppression and cancer therapy. The adenovirus type 5 E1A gene provides a useful tool to study the function of tumor suppression and apoptosis. E1A has been shown to induce apoptosis in different systems in vitro. However, this activity has not been well characterized in vivo. Therefore, the effect of this activity and the link to the in vivo biological function are not clear. To answer these questions, we introduced E1A into murine melanoma cells and characterized the biological features both in vitro and in vivo. Expression of the E1A gene does not affect the proliferation rate of tumor cells in vitro, but inhibits tumor growth in vivo. The in vitro analysis indicated that the E1A-expressing tumor cells are sensitive to serum depletion-induced apoptosis. Importantly, E1A-mediated apoptosis was also identified in vivo, suggesting this activity contributed to the tumor suppressive function. The in vivo apoptotic pattern was unique: most of the apoptotic cells were around the periphery of the tumors, implicating the interaction of these cells with stress stimuli in vivo. In addition, E1A also rendered the tumor cells susceptible to the cytotoxicity of other anticancer agents, a feature useful for improving the efficacy of cancer therapy. The results provide a functional link between in vitro activity and in vivo effects.

Adenovirus E1A Proteins↗
PubMed1998

Secondary structure of an antibacterial peptide Abp3 studied by two-dimensional proton-NMR.

An antibacterial peptide Abp3, an analogue of cecropin B, was investigated by two-dimensional proton-NMR at pH 5.0 in aqueous solution with 15% (v/v) hexafluoroisopropanol. The peptide, which consists of 35 amino acids, was synthesized chemically. Most resonances of the main-chain and side-chain protons were assigned. Several medium range NOE connectivities were observed, showing two separate alpha-helices with one amphiphilic in N-terminal domain (residues 5-21) and the other hydrophobic in C-terminal domain (residues 25-35) and a hinge region between them. The J coupling constants and the chemical shifts in these sections also supported the conclusion.

Amino Acid Sequence↗
PubMed1998

Subcellular distribution and turnover of presenilins in transfected cells.

The mechanisms by which mutations in presenilin-1 (PS1) and presenilin-2 (PS2) result in the Alzheimer's disease phenotype are unclear. Full-length PS1 and PS2 are each processed into stable proteolytic fragments after their biosynthesis in transfected cells. PS1 and PS2 have been localized by immunocytochemistry to the endoplasmic reticulum (ER) and Golgi compartments, but previous studies could not differentiate between the full-length presenilin proteins and their fragments. We carried out subcellular fractionation of cells stably transfected with PS1 or PS2 to determine the localization of full-length presenilins and their fragments. Full-length PS1 and PS2 were principally distributed in ER fractions, whereas the N- and C-terminal fragments were localized predominantly to the Golgi fractions. In cells expressing the PS1 mutant lacking exon 9 (DeltaE9), we observed only full-length molecules that were present in the ER and Golgi fractions. The turnover rate was considerably slower for the DeltaE9 holoprotein, apparently due to decreased degradation within the ER. Our results suggest that that full-length presenilin proteins are primarily ER resident molecules and undergo endoproteolysis within the ER. The fragments are subsequently transported to the Golgi compartment, where their turnover rate is much slower than that of the full-length presenilin in the ER.

Animals↗
PubMed1998

Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo.

Mapping of tryptic phosphopeptides of heat shock factor 1 (HSF1) from non-stressed or moderately heat-stressed HeLa cells, labeled in vivo by [32P]orthophosphate, revealed four major phosphopeptides A to D. Heat stress drastically increased phosphopeptide signals. To identify target peptides and amino acids and to correlate phosphorylation and transactivation function, phosphopeptide maps were produced of LexA-human HSF1 chimeras and mutant derivatives thereof, and transactivation activities of original and mutant chimeras were compared. LexA-HSF1 chimeras were previously shown to be regulated identically to HSF1, except that they transactivate promoters with LexA-binding sites instead of hsp promoters. The patterns of phosphopeptides of LexA-HSF1 and endogenous HSF1 were similar. Analysis of single residue substitutions suggested that phosphopeptide C is peptide VKEEPPSPPQSPR (297-309) phosphorylated on Ser-307 but not Ser-303. Substitution of Ser-307 but not Ser-303 caused deregulation of factor activity. Mapping of several constitutively active chimeras associated unphosphorylated peptide C with the transcriptionally active HSF1 conformation, suggesting that dephosphorylation of this peptide (at Ser-307) may either be an integral step in the activation process or serve to maintain the active conformation of HSF1. Exploiting this correlation, indirect evidence was obtained that activation domains of HSF1 interact with the distantly located regulatory domain to maintain the factor in an inactive state.

Amino Acid Sequence↗
PubMed1998

Comparison of anion-exchange and ion-modified reversed-phase liquid chromatography for the determination of S-sulfocysteine.

A dual Hg-Au amalgam electrode is used to detect S-sulfocysteine (SSC) in this study. There exist two main components in the acetonitrile (ACN) rat brain extracts, namely, Cl- and GSSG (oxidized glutathione), that are active in our detection system (GSH is not extracted in ACN). Two strong anion-exchange columns from different companies were used to separate the samples under different conditions, but SSC and Cl- were not separated at the optimum detection pH of 5.2. The signal from Cl- was greatly decreased by lowering the potential at the downstream electrode, though it cannot be completely eliminated. While a silver cartridge removed Cl- from micromoles to several millimoles without any negative effect on the SSC signal in aqueous standards, a large negative peak which interferes with SSC detection was unfortunately introduced when a silver cartridge was applied to brain tissue samples. However, SSC and Cl- in the samples are successfully separated by ion-modified reversed-phase LC in acetate buffer at the optimum detection pH (5.2). The separation conditions are 20 mM acetic acid, 2% methanol, 0.5 mM cetyltrimethylammonium p-toluene sulfonate (CTMA) (pH 5.2). Most importantly, the sensitivity of SSC under the optimum separation conditions is not sacrificed. The detection limit is 8 nM (20 microl injected).

Animals↗
PubMed1998

Additive effects of PS1 and APP mutations on secretion of the 42-residue amyloid beta-protein.

Humans harboring missense mutations in the presenilin 1 (PS1) gene undergo progressive cerebral deposition of the 42-residue amyloid beta-protein (A beta 42) at an early age and develop severe Alzheimer's disease. A beta 42 is selectively elevated in the conditioned media of cells expressing mutant but not wild-type PS1, indicating that presenilin mutations alter APP processing. Here we analyze the effects of various PS1 mutant constructs on the cellular production of A beta 42. A construct expressing only the PS1 N-terminal endoproteolytic fragment with the mutation Y115H causes no significant increase in A beta 42, whereas a full-length PS1 construct with the same mutation does. This result suggests that the pathogenic effect of mutant presenilins is produced by the full-length molecule even though only a minor proportion of total PS1 occurs as holoprotein in tissues and cell lines. We demonstrate that the effects of two different PS1 mutations are additive when engineered into the same PS1 molecule. Therefore, two mutations alter gamma-secretase processing of APP more than one and the PS1 mutations described to date do not cause the maximum possible PS1-mediated rise in A beta 42. When a PS1 mutation was expressed in cells carrying the APPV717I mutation, A beta 42 rose dramatically to become the predominant secreted A beta species, an observation of interest for transgenic modeling of AD. Our results are consistent with the hypothesis that presenilin is a major regulator of the proteolytic processing of APP by gamma-secretases.

Age of Onset↗
PubMed1998

A detergent-insoluble membrane compartment contains A beta in vivo.

Ordered assembly of the amyloid-beta protein (A beta) into amyloid fibrils is a critical step in Alzheimer's disease (AD). To release the amyloidogenic peptide A beta from the Alzheimer amyloid precursor protein (APP), two secretases act sequentially: first, beta-secretase cleaves close to the membrane within the ectodomain and then gamma-secretase cuts within the transmembrane domain. The sites of gamma-secretase cleavage are after residues 40 or 42 of A beta. Except in those rare cases of AD caused by a mutation, levels of secreted A beta are not elevated; thus, the secretory pathway may be unaffected, and factors other than the extracellular concentration of A beta may contribute to the aggregation properties of the peptide. A beta is also present in intracellular compartments. The two gamma-secretase cleavage products, A beta42 and A beta40, were found in different compartments: A beta42 in the endoplasmic reticulum (ER)/intermediate compartment, and A beta40 in the trans-Golgi network (TGN). The cellular compartments that harbor A beta are target sites for therapeutic intervention. Here we report that in the brain, the principal compartment in which A beta resides is a detergent-insoluble glycolipid-enriched membrane domain (DIG). Also present in the DIG fractions are the endoproteolytic fragments of presenilin-1 (PS1) and APP. The presence of these proteins, which all contribute to the generation of A beta, indicates that the DIG fraction is probably where the intramembranous cleavage of APP occurs.

Alzheimer Disease↗
PubMed1998

[Ultrasound bone measurement of the tibia: comparison with vertebral dual-energy X-ray absorptiometry and appendicular single photon absorptiometry].

OBJECTIVE: Ultrasonic techniques have been used to assess the mechanical properties of bone. Recently, a new ultrasonic bone instrument, which measured the SOS (speed of sound) at the tibial shaft, has been introduced (Sound Scan 2000, Myriad Ultrasound Systems Ltd.). The aim of this work was to investigate the correlation of tibial SOS with bone mineral density (BMD). METHODS: The tibial SOS was measured in 213 healthy women (aged 22-83 years) and 56 female primary osteoporosis with vertebral fractures (aged 53-82 years). Values of SOS were compared with BMD assessed by dual energy x-ray absorptiometry (DEXA) at spine and hip sites and single photon absorptiometry (SPA) at the distal forearm. RESULTS: Tibial SOS correlated more closely with the BMD of lumbar, hip and forearm (r = 0.387-0.928, P < 0.001). The tibia SOS values and the BMD values measured by the DEXA and SPA were negatively correlated to age and years since menopause. In particular, they were obviously lower in the group of 50 years old. The tibial SOS of vertebral fracture group was significantly lower than that of well-matched non-fracture-group (n = 104, aged 51-84 years). CONCLUSIONS: Tibial SOS was significantly correlated with BMD measured by DEXA or SPA respectively and able to discriminate patients with vertebral fracture from the age-matched controls.

Absorptiometry, Photon↗
PubMed1997

Cross-reactivity of C219 anti-p170(mdr-1) antibody with p185(c-erbB2) in breast cancer cells: cautions on evaluating p170(mdr-1)

BACKGROUND: Increased expression of the multidrug resistance gene (MDR-1)-encoded P-glycoprotein (p170[mdr-1]) is a major cause of tumor cell multidrug resistance. p170(mdr-1) functions as a drug-efflux pump to reduce the cellular accumulation of specific drugs. MDA-MB-435 human breast cancer cells that have been transfected with oncogene c-erbB2 complementary DNA (435.eb cells) express high levels of the transmembrane glycoprotein p185(c-erbB2) and exhibit increased resistance to the chemotherapeutic agent paclitaxel via p170(mdr-1)-independent mechanisms. We have recently discovered that the widely used monoclonal antibody C219, which is specific for p170(mdr-1), may cross-react with p185(c-erbB2) in 435.eb cells. In this study, we have investigated the nature of this cross-reactivity. METHODS: Immunoprecipitation experiments involving the use of breast cancer cells that express different levels of p185(c-erbB2) were performed, and C219 was used for western blot analysis of immunoprecipitated proteins. Immunohistochemical analyses were performed on acetone-fixed slides of human breast cancer cells. Peptide sequence comparisons and enzyme-linked immunosorbent assays were performed to determine the molecular basis of C219 cross-reactivity with p185(c-erbB2). RESULTS: The cross-reactivity of C219 with p185(c-erbB2) was demonstrated by both western blot and immunohistochemical analyses. Peptide sequence comparisons revealed that C219 recognizes an epitope in p170(mdr-1) (C219 epitope) that shares sequence homology with p185(c-erbB2). Enzyme-linked immunosorbent assays demonstrated that C219 recognizes synthetic peptides derived from both the C219 epitope in p170(mdr-1) and the C219 epitope-homologous region in p185(c-erbB2). CONCLUSIONS: The anti-p170(mdr-1) monoclonal antibody C219 cross-reacts with p185(c-erbB2) through a peptide sequence in p185(c-erbB2) that is homologous to the C219 epitope in p170(mdr-1).

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1997

Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease.

Mutations in the presenilin 1 (PS1) and presenilin 2 (PS2) genes increase the production of the highly amyloidogenic 42-residue form of amyloid beta-protein (Abeta42) in a variety of cell lines and transgenic mice. To elucidate the molecular mechanism of this effect, wild-type (wt) or mutant PS1 and PS2 genes were stably transfected into Chinese hamster ovary cells expressing endogenous or transfected beta-amyloid precursor protein (APP). By immunoprecipitation/Western blot analysis, APP was consistently found to coimmunoprecipitate with PS1 or PS2 proteins. Several distinct PS1, PS2, or APP antibodies precipitated PS-APP complexes that were detectable by blotting with either APP or PS antibodies. Importantly, complex formation could be detected at endogenous protein levels in nontransfected cells. In various Chinese hamster ovary cell lines, the amounts of APP coprecipitated by PS antibodies were proportional to the expression levels of both APP and PS. APP-PS complexes also were recovered from human 293 and HS683 cells. Full maturation of APP was not required for the interaction; most APP molecules complexed with PS were solely N-glycosylated. Treatment of cells with brefeldin A or incubation at 20 degrees C did not block complex formation, suggesting that the association between APP and PS occurs in part in the endoplasmic reticulum. Complex formation was detected for both wt and mutant PS and APP proteins. Deletion of the APP C-terminal domain did not abrogate complex formation, suggesting that the interaction does not occur in the cytoplasmic domains of the proteins. Our results demonstrate that wt and mutant PS1 and PS2 proteins form complexes with APP in living cells, strongly supporting the hypothesis that mutant PS interacts with APP in a way that enhances the intramembranous proteolysis of the latter by a gamma-secretase cleaving at Abeta42.

Alzheimer Disease↗
PubMed1997

Skeletal and CNS defects in Presenilin-1-deficient mice.

Presenilin-1 (PS1) is the major gene responsible for early-onset familial Alzheimer's disease (FAD). To understand the normal function of PS1, we have generated a targeted null mutation in the murine homolog of PS1. We report that PS1-/- mice die shortly after natural birth or Caesarean section. The skeleton of homozygous mutants is grossly deformed. Hemorrhages occur in the CNS of PS1 null mutants with varying location, severity, and time of onset. The ventricular zone of PS1-/- brains is markedly thinner by embryonic day 14.5, indicating an impairment in neurogenesis. Bilateral cerebral cavitation caused by massive neuronal loss in specific subregions of the mutant brain is prominent after embryonic day 16.5. These results show that PS1 is required for proper formation of the axial skeleton, normal neurogenesis, and neuronal survival.

Alzheimer Disease↗
PubMed1997

Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins.

Mutations in the presenilin 1 (PS1) and presenilin 2 (PS2) genes cause the most common and aggressive form of early onset familial Alzheimer's disease. To elucidate their pathogenic mechanism, wild-type (wt) or mutant (M146L, C410Y) PS1 and wt or mutant (M239V) PS2 genes were stably transfected into Chinese hamster ovary cells that overexpress the beta-amyloid precursor protein (APP). The identity of the 43-45-kDa PS1 holoproteins was confirmed by N-terminal radiosequencing. PS1 was rapidly processed (t1/2 = 40 min) in the endoplasmic reticulum into stable fragments. Wild-type and mutant PS2 holoproteins exhibited similar half lives (1.5 h); however, their endoproteolytic fragments showed both mutation-specific and cell type-specific differences. Mutant PS1 or PS2 consistently induced a 1.4-2.5-fold increase (p < 0.001) in the relative production of the highly amyloidogenic 42-residue form of amyloid beta-protein (Abeta42) as determined by quantitative immunoprecipitation and by enzyme-linked immunosorbent assay. In mutant PS1 and PS2 cell lines with high increases in Abeta42/Abetatotal ratios, spontaneous formation of low molecular weight oligomers of Abeta42 was observed in media, suggesting enhanced Abeta aggregation from the elevation of Abeta42. We conclude that mutant PS1 and PS2 proteins enhance the proteolysis of beta-amyloid precursor protein by the gamma-secretase cleaving at Abeta residue 42, thereby promoting amyloidogenesis.

Amyloid beta-Peptides↗
PubMed1997

Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers.

In the course of its activation by heat and other stresses, the inactive monomer of human heat shock transcription factor 1 (HSF1) is converted to a DNA-binding homotrimer and is hyperphosphorylated. At least four Ser/Thr residues in HSF1 appeared to be inducibly phosphorylated during heat shock. Ser/Thr protein kinase inhibitors inhibited, and protein phosphatase inhibitor calyculin A and phorbol ester enhanced, hsp70-CAT reporter gene expression but not heat shock element DNA binding activity in HeLa cells undergoing a moderate heat shock. Calyculin A (5-20 nM) caused hyperphosphorylation of HSF1, the extent of which was comparable to that produced by moderate to severe heat shock. Upon recovery from a 42 degrees C/30 min-heat shock, HSF1 trimers disassembled quantitatively within 2 h. Calyculin A interfered with the dissociation of HSF1 trimers. Thus, hyperphosphorylation increases the effective half-life of the HSF1 trimer, which may prolong factor activity subsequent to heat shock. Hyperphosphorylation also dramatically stimulated the transactivation function of HSF1: exposure to calyculin A of cells induced to form inactive HSF1 trimers resulted in the conversion of the inactive to active trimers. Given that deletion of certain sequences renders HSF1 constitutively active, these results suggested that the activation of HSF1 trimers by calyculin A was a consequence of hyperphosphorylation of HSF1 rather than of a downstream factor.

Biopolymers↗
PubMed1997

The tumor suppression activity of E1A in HER-2/neu-overexpressing breast cancer.

The HER-2/neu proto-oncogene is frequently amplified or overexpressed in human breast and ovarian cancers, and is significantly correlated with shorter survival. We have previously reported that the adenovirus type 5 early region 1A (E1A) gene product can repress HER-2/neu overexpression by repressing HER-2/neu promoter activity, and suppress the tumorigenic potential of HER-2/neu-overexpressing ovarian cancer cells. To examine E1A tumor suppressor function in breast cancer, we transduced E1A in vitro by adenovirus into both HER-2/neu-overexpressing and low expressing human breast cancer cell lines. In HER-2/neu-overexpressing cells, E1A greatly inhibited tumor cell growth in vitro. However, in HER-2/neu low expressing cancer cell lines, E1A had no significant effect on cell growth in culture medium. To test the therapeutic efficacy of E1A, we used both adenovirus-mediated and cationic liposome-mediated E1A gene delivery systems in an orthotopic breast cancer animal model. An advanced breast cancer model was established by inoculation of HER-2/neu-overexpressing human breast cancer cells in mammary fat pad and treated by local injections of either replication-deficient adenovirus expressing E1A, Ad.E1A(+) or a liposome-E1A DNA complex. As controls, mice bearing tumors were also treated with Ad.E1A(-) which is virtually the same adenovirus as Ad.E1A(+) except that E1A is deleted, a liposome-E1A frame-shift mutant DNA complex, or just PBS. In mice bearing a HER-2/neu-overexpressing breast cancer cell line, E1A delivered either by adenovirus or liposome significantly inhibited tumor growth and prolonged mouse survival compared with the controls. In fact, 60-80% of E1A-treated mice lived longer than 2 years versus only 0-20% of control mice (P<0.05). Western blot analysis showed that E1A protein was expressed in tumor tissue and immunohistochemical analysis showed that HER-2/neu p185 protein expression was suppressed. Taken together, our results indicated that both adenovirus and cationic liposome delivery systems were effective in transfering E1A gene for tumor suppression in a HER-2/neu-overexpressing breast cancer model.

Adenovirus E1A Proteins↗