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Biomedical subjects

C Chang

Publications and source records attributed to C Chang.

At least 289 records · Page 16Linked to original sources
PubMed1995

[The cervical ripening score by trans-perineum ultrasound].

OBJECTIVE: To evaluate cervical ripening in pregnancy at term by trans-perineum ultrasound. METHODS: The cervical length, cervical internal os width, cervical echo intensity, cervical position and distance between fetal presentation and vaginal external os were assessed by trans-perineum ultrasound (transducer 3.5MHz) in 100 cases of normal pregnant women at term. RESULTS: On the basis of Bishop score, the results showed, cervical ripening score > or = 9, 14 cases were in labor, mean parturient time 3.9 +/- 3.1 hours; 5 approximately 8 scores, 54 cases were in labor, mean parturient time 20.8 +/- 3.9 hours; < or = 4 scores, 32 cases in which only 21 cases were in labor, mean parturient time 46.9 +/- 3.9 hours. The results were significantly different among the three groups. CONCLUSION: Ultrasonographic cervical ripening score is an objective noninvasive method for assessment of cervical ripening at term.

Adult↗
PubMed1994

Prostatic localization of spontaneous early invasive carcinoma in Lobund-Wistar rats.

Animal models of human prostate cancer are very limited in number but are of obvious importance to develop. Dr. Morris Pollard (M. Pollard, J. Natl. Cancer Inst., 51: 1235-1241, 1973) has reported that Lobund-Wistar rats develop spontaneous metastatic prostatic cancer when they become old (approximately 25% incidence after 25 months). A chemically induced form of the disease has also been described in Lobund-Wistar rats. However, recent reports suggest that most of the chemically induced adenocarcinomas are not prostatic in origin, with most arising in the seminal vesicle, and thereby raise questions about the origin of the spontaneous cancers. We herein report cancer spontaneously arising in the lateral lobes of the prostates in Lobund-Wistar rats. One of 8 rats killed at 16 months of age showed prostatic carcinoma in situ. Two of 39 rats killed at 20 months displayed early invasive adenocarcinomas with no signs of metastases. Because sectioning of the prostates in this study was limited to face sections from a single block for each rat, it is highly probable that the true incidence of dysplasias and carcinomas is underestimated by these data. Dysplastic or neoplastic changes were not seen in either the seminal vesicles or other portions of the prostatic complex. The nuclei of adenocarcinoma cells showed less labeling with antibody to the androgen hormone receptor than did normal cells. These data strongly support the validity of the Pollard model of spontaneous prostate cancer in Lobund-Wistar rats.

Age Factors↗
PubMed1994

Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase.

The mitochondrial (mt) aldehyde dehydrogenase (ALDH2) in liver has been considered to play a major role in the detoxification of alcohol in humans. Using the human ALDH2 cDNA and synthetic oligodeoxyribonucleotides (oligos) as probes, the mouse ALDH2 (mALDH2) gene was isolated and characterized. Nucleotide (nt) sequence analysis revealed an open reading frame (ORF) of 1560 bp encoding a protein of 519 amino acid (aa) residues. The gene is composed of 13 exons and 12 introns and spans approx. 26 kb of the mouse genome. The deduced aa sequence, when compared to the mtALDH2 of human, rat, horse and bovine, revealed 95.8, 99.0, 95.6 and 93.6% aa identity, respectively. Primer extension and rapid amplification of cDNA ends (RACE) experiments showed that the transcription start point (tsp) was 105 bp upstream from the start codon. The promoter region of mALDH2 is devoid of a TATA consensus sequence motif, but putative regulatory elements, including a CAAT box, Sp1-binding site and glucocorticoid-response element (GRE), are present in the promoter region. Northern blot hybridization demonstrated the existence of a high level of mALDH2 mRNA in mouse liver and a low level in mouse kidney.

Aldehyde Dehydrogenase↗
PubMed1994

Induction of translation by the 5'-untranslated region of human androgen receptor mRNA.

Androgens and androgen receptor (AR) play important roles in sexual differentiation and prostatic cancer cell proliferation. To investigate the regulation of AR expression, a 2-kilobase pair 5'-flanking region of human AR gene including a 0.6-kilobase pair 5'-untranslated region (5'-UTR) was ligated to a chloramphenicol acetyltransferase (CAT) gene and characterized by CAT assay after transfection into HeLa cells. The results revealed that AR 5'-UTR was absolutely needed for the induction of CAT activity, but could not function as an enhancer for the AR transcription. A further study using a 180 base pairs (+21 to +202 including a stem-loop secondary structure at +109 to +129) within the AR 5'-UTR demonstrated that this region was sufficient to induce more CAT activity without changing the CAT mRNA expression. Taken together, these results strongly suggested that 5'-UTR of AR mRNA plays an essential role in the induction of AR translation, which may represent the first reported translational induction mechanism in the steroid receptor superfamily.

Base Sequence↗
PubMed1994

Human NKR-P1A. A disulfide-linked homodimer of the C-type lectin superfamily expressed by a subset of NK and T lymphocytes.

In rodents, the NKR-P1 family of glycoproteins are preferentially expressed on NK cells and have been implicated in NK cell function. In this study, we describe the characterization and cloning of a human homologue. Human (h)NKR-P1A cDNA was cloned from a NK cell cDNA library by expression in COS7 cells with the use of the DX1 mAb. hNKR-P1A is a type II membrane glycoprotein with characteristic properties of the C-type lectin superfamily. Comparison of the predicted amino acid of human NKR-P1A with rat and mouse NKR-P1 indicates 46% homology. NKR-P1A is on human chromosome 12, the syntenic of mouse chromosome 6, where the murine NKR-P1 genes are located. All rat NK cells express NKR-P1; however, hNKR-P1A is present on only a subset of human NK cells. Although rodent T cells only infrequently express NKR-P1, hNKR-P1A is present on approximately 25% of adult peripheral blood T cells, including both CD4+ and CD8+ T cells, and is expressed preferentially on adult T cells with a "memory" antigenic phenotype. The anti-hNKR-P1A mAb failed to affect lysis of NK-sensitive targets; however, the spontaneous cytotoxicity mediated by certain NK cell clones against the murine P815 cell target was blocked by anti-hNKR-P1A mAb. Our findings demonstrate that NKR-P1A is a human homologue of the rodent NKR-P1 genes and suggest that this molecule may be involved in NK cell function.

Amino Acid Sequence↗
PubMed1994

Human and rat TR4 orphan receptors specify a subclass of the steroid receptor superfamily.

We have identified a member of the steroid receptor superfamily and cloned it from human and rat hypothalamus, prostate, and testis cDNA libraries. The open reading frame between first ATG and terminator TGA can encode 615 (human) and 596 (rat) amino acids with calculated molecular mass of 67.3 (human) and 65.4 (rat) kDa. The amino acid sequence of this protein, called TR4 orphan receptor, is closely related to the previously identified TR2 orphan receptor. The high homology between TR2 and TR4 orphan receptor suggests that these two orphan receptors constitute a unique subfamily within the steroid receptor superfamily. These two orphan receptors are differentially expressed in rat tissues. Unlike TR2 orphan receptors, the TR4 orphan receptor appears to be predominantly located in granule cells of the hippocampus and the cerebellum, suggesting that it may play some role(s) in transcriptional regulation in these neurons.

Amino Acid Sequence↗
PubMed1994

Prostromelysin and procollagenase genes are differentially up-regulated in chondrocytes from the knees of rabbits with experimental osteoarthritis.

OBJECTIVE: To determine the relative expressions of matrix metalloprotease (MMP) genes pro-MMP1 and pro-MMP3 in the cartilage of rabbits with experimentally induced osteoarthritis (OA), and to assess the role of the chondrocyte in this process. METHODS: OA was induced in rabbits after partial medial meniscectomy. Rabbits were killed at 4 weeks or 8 weeks, and total cellular RNA was prepared from cartilage and probed by Northern blotting with pro-MMP 32P-labeled complementary DNA. Monolayer chondrocytes were used to assess MMP-inducing activity of chondrocyte factor(s). RESULTS: Pro-MMP messenger RNAs (mRNAs) were up-regulated in experimental OA cartilage; pro-MMP3 mRNA expression exceeded that of pro-MMP1. Conditioned medium from OA-derived chondrocytes up-regulated pro-MMP mRNAs in normal chondrocytes. CONCLUSION: Up-regulation of MMP genes in this OA model may contribute to cartilage degradation. Chondrocytes up-regulate MMP genes via an autocrine pathway.

Animals↗
PubMed1994

An in vitro model for the effects of androgen on neurons employing androgen receptor-transfected PC12 cells.

Androgen alters neurite outgrowth, synaptic organization, and cell survival in various portions of the brain and spinal cord. However, examination of the specific effects of androgen on neurons in vivo has been difficult. Previously, an in vitro model for the effects of estrogen on neurons was developed and characterized, using an estrogen receptor (ER)-transfected PC12 rat pheochromocytoma cell line. This model demonstrated estrogenic regulation of neurite outgrowth, spine formation, and gap junction formation. Similarly, an in vitro model for the effects of androgen on neurons is now described. Wild-type cells (PC12-WT) were stably transfected with an expression vector coding for the full-length cDNA for the human androgen receptor (AR). Resultant clones were isolated, screened for incorporation of vector and expression of AR mRNA and protein, and analyzed for morphologic responses to androgen. PC12-WT, NE09 (ER-negative, AR-negative), SER8 (ER-positive, AR-negative), and AR8 (ER-negative, AR-positive) cells were exposed to 10 ng/ml nerve growth factor (NGF), along with 0-10(-7) M dihydrotestosterone (DHT) for 2 days. AR8 cells demonstrated an androgen dose-dependent increase in mean neurite length, branch order, and neurite field area, whereas neurite branch segment length and soma area were not affected by androgen. PC12-WT, NE09, and SER8 cells exhibited no alterations in cell morphology with DHT exposure. Because of the synergistic effects of DHT and NGF, the regulation of NGF receptor mRNA by DHT was evaluated; however, no significant induction of either trkA or p75 mRNA expression by androgen was documented. The results suggest that in AR-positive PC12 cells, androgen acts additively with NGF to increase neurite outgrowth; but androgen effects are mediated specifically through branching and arborization. These responses are similar to developmental studies of androgen effects in vivo. Thus, androgen appears to induce an inherent neural morphologic program in AR-containing cells, which increases the receptive field of these cells, increasing the likelihood for interneural communication, although not promoting communication itself. These cell lines will provide a unique in vitro system for studying mechanisms of androgen-neuron interactions.

Androgens↗
PubMed1994

Immunocytochemical identification of androgen receptor in mouse osteoclast-like multinucleated cells.

Expression of androgen receptor (AR) in mouse osteoclast-like multi-nucleated cells (OCs) was examined with immunocytochemical techniques. Murine OCs were obtained by co-culturing mouse osteoblastic cells and bone marrow cells. Three preparations of polyclonal anti-AR antibody which were raised in rabbit against different parts of the human AR were employed for the experiments. Specific staining for AR was demonstrated in the nuclei and the perinuclear area of mouse OCs. This is the first report demonstrating the presence of AR in osteoclast-like cells.

Animals↗
PubMed1994

31P-magnetic resonance spectroscopy of the rabbit masseter muscle.

Dynamic biochemical changes in the masseter muscle were studied in 14 New Zealand adult male rabbits by 31P-nuclear magnetic resonance (NMR) spectroscopy. NMR spectra were obtained during rest and electrical stimulation of the muscle in the anaesthetized animal at 33 recording sessions. Electrical stimulation was applied by a pair of copper wires placed separately with hypodermic needles into the muscle. NMR spectra were acquired with a 2 x 3 cm, double-turn, copper transmit/receive coil. Sixteen spectra were averaged over 30 s to obtain averaged spectra continuously during a 30-min recording. The spectra were processed automatically using a non-linear 'least-squares' fitting program on the spectrometer. A Lorentzian line shape was assumed for the peaks, and values of peak height, area and chemical shifts were generated. Each averaged spectrum consisted of five peaks: inorganic phosphate (Pi), creatine phosphate (PCr), and three peaks related to ATP. Data were analysed as to absolute changes in Pi and PCr, in the ratio of Pi/PCr, and the shift of Pi to PCr to estimate pH. Several protocols were used in which ranges of frequency, intensity and duration of electrical stimulation were tested. The protocol for detailed studies involved stimulating the muscle twice at 5 Hz for 3 min separated by a 3-min rest period, then stimulating twice at 50 Hz for 3 min separated by a rest period. During contraction of the muscle, there was a significant increase in the Pi/PCr ratio (p < 0.05) as compared to the resting level. The ratio reached a plateau over a 3-min contraction using 5-Hz stimulation, then increased significantly more with the 50-Hz stimulation but decayed during the 3 min. Sustained stimulation with 50 Hz for 15-45 min evoked an initial sharp change in Pi/PCr, which then reached a steady plateau that remained over the entire stimulation. These findings indicate that the rabbit masseter muscle is relatively fatigue resistant in maintaining a steady-state equilibrium in the relation of Pi to PCr.

Adenosine Triphosphate↗
PubMed1994

Presence of hepatitis B surface antigen (HBsAg)-specific cytotoxic T cells in asymptomatic HBsAg carriers.

To investigate whether there is any evidence of an immune stimulation against hepatitis B virus surface antigen (HBsAg) in asymptomatic HBsAg carriers, proliferative and cytotoxic responses to HBsAg were measured in their peripheral blood lymphocytes. Although the majority of asymptomatic carriers had no proliferative response to HBsAg, 3 (25%) of 12 carriers showed significant T cell proliferation against HBsAg. In addition, using HBsAg-expressing autologous lymphoblastoid cell line (LCL) as target cells, HBsAg-specific cytotoxic activity was found in 2 of 3 asymptomatic HBsAg carriers who had a proliferative response against HBsAg. Furthermore, 6 cytotoxic T lymphocyte (CTL) clones were isolated from 1 asymptomatic carrier. The epitope recognized by 2 CTL clones was mapped to the major HBsAg residues 158-172. These CTL clones were able to produce interferon-gamma, tumor necrosis factor-alpha, or granulocyte-macrophage colony-stimulating factor. These findings demonstrate the presence of HBsAg-specific, major histocompatibility complex class I-restricted CTL in asymptomatic HBsAg carriers.

Adult↗
PubMed1994

Phenotypic mixing between different hepadnavirus nucleocapsid proteins reveals C protein dimerization to be cis preferential.

Hepadnaviruses encode a single core (C) protein which assembles into a nucleocapsid containing the polymerase (P) protein and pregenomic RNA during viral replication in hepatocytes. We examined the ability of heterologous hepadnavirus C proteins to cross-oligomerize. Using a two-hybrid assay in HepG2 cells, we observed cross-oligomerization among the core proteins from hepatitis B virus (HBV), woodchuck hepatitis virus, and ground squirrel hepatitis virus. When expressed in Xenopus oocytes, in which hepadnavirus C proteins form capsids, the C polypeptides from woodchuck hepatitis virus and ground squirrel hepatitis virus, but not duck hepatitis B virus, can efficiently coassemble with an epitope-tagged HBV core polypeptide to form mixed capsids. However, when two different core mRNAs are coexpressed in oocytes the core monomers show a strong preference for forming homodimers rather than heterodimers. This holds true even for coexpression of two HBV C proteins differing only by an epitope tag, suggesting that core monomers are not free to diffuse and associate with other monomers. Thus, mixed capsids result from aggregation of different species of homodimers.

Animals↗
PubMed1994

A critical role for chromatin in mounting a synergistic transcriptional response to GAL4-VP16.

The role of chromatin in mounting a synergistic transcriptional response to GAL4-VP16 was investigated. Strong synergy was observed when chromatin templates were used in vitro. The synergy was severely reduced when naked DNA templates were transcribed. In vivo synergy was strong when nonreplicating templates were used. However, the use of replicating templates, which involved transient disruptions of chromatin, led to strong reductions in synergy. In both of these low-synergy responses, transcription levels were high. We infer that strong synergy has a requirement for chromatin that may be understood in terms of the competition between multiple activator molecules and histone cores for promoter DNA.

Chromatin↗
PubMed1994

Identification of 3',5'-cyclic adenosine monophosphate response element and other cis-acting elements in the human androgen receptor gene promoter.

Androgen and androgen receptor (AR) play an important role in sexual differentiation and prostate proliferation. To investigate AR gene transcriptional regulation, a 2.3-kilobase AR gene promoter region was isolated, sequenced, and characterized. Chloramphenicol acetyltransferase (CAT) assay and sequence homology search of AR gene promoter among human, rat, and mouse revealed some potential cis-acting elements, including a GC box, a suppressor region, and a purine-rich element. Deletion analysis and gel retardation assay using a 50-base pair (bp) double-strand purine-rich element showed that this purine-rich element can bind to specific proteins in nuclear extract of LNCaP and HeLa cells and may be essential for AR gene transcription. Furthermore, to investigate the effect of cAMP on AR gene transcription, we treated LNCaP and HeLa cells with 10 mM (Bu)2cAMP after transfection with CAT gene reporter plasmids linked to the AR gene promoter. This treatment induced several folds of CAT activity in LNCaP cells only, and the induction was further confirmed at AR mRNA level by Northern blot analysis and reverse transcription-polymerase chain reaction assay. Deletion analysis of the AR gene promoter showed that a region between 530 bp and 380 bp upstream of AR gene transcription initiation site, which includes one potential cAMP response element (CRE), is responsible for cAMP induction. Gel retardation analysis using this CRE (AR/CRE1) showed that AR/CRE1 can bind to specific proteins in nuclear extract of LNCaP cells, which appears to form a different binding complex compared to somatostatin/CRE.

Animals↗
PubMed1994

Expression of multiple oncogenes in human esophageal carcinomas.

To study the oncogenesis of human esophageal carcinoma, the expression of a variety of oncogenes was studied in 10 esophageal carcinoma cell lines and 16 pairs of tumor and nontumor tissues removed from patients with esophageal carcinoma. Northern blot analyses using 11 different oncogene probes revealed that 5 oncogenes, i.e. c-myc, c-H-ras, c-sis, c-raf, and c-fos, were expressed. Among them, a variant c-sis mRNA transcript of 2.7 kilobase (kb) was expressed in 7 of 10 cell lines and in 9 of 16 tumor tissues. Furthermore, an overexpression and an amplification of c-myc gene was observed in some cell lines. These results suggest that multiple oncogene expression may be required for the induction, maintenance, and progression of esophageal carcinoma. The expression of a 2.7-kb transcript, of c-sis and overexpression of c-myc gene may play some role in the carcinogenesis of esophageal carcinoma.

Carcinoma, Squamous Cell↗
PubMed1994

Demonstration of bioequivalence between ventasol syrup and ventolin syrup in humans and in dogs.

Ventasol syrup, a new locally produced salbutamol formulation, was compared with the standard salbutamol formulation, ventolin syrup, for determination of oral bioequivalence in stable asthmatic human subjects and in dogs. On separate occasions, each subject received a single 10 ml oral dose of each formulation containing 4 mg salbutamol. In the human subjects, statistically similar peak plasma concentrations of salbutamol were obtained (196 +/- 7 ng/ml for ventasol syrup and 185 +/- 6 ng/ml for ventolin syrup) 3 hours after oral administration of the formulations. From the ratio of the AUCo-infinity for the formulations (1.04), a relative oral bioavailability of 104%, indicating equivalent total salbutamol output, was also obtained in the human subjects. Similarly, in the dogs, the formulations produced statistically equivalent peak plasma concentrations of salbutamol (259 +/- 24ng/ml for ventasol syrup and 285 +/- 29ng/ml for ventolin syrup) 3 hours after oral administration. Also, from the ratio of the AUCo-infinity for the formulations (1.02), a relative oral bioavailability of 102%, indicating similar total salbutamol output, was obtained in the dogs. From these results, it is concluded that oral bioequivalence between ventasol syrup and ventolin syrup was demonstrated in human subjects and in dogs.

Adult↗