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The following are some of the methods used in our laboratory to achieve our project goals.


If you have any questions or concerns about the techniques described here please refer to our Publications for more details.
You can also contact us by E-mail -
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The Amniochorion Organ Explant Culture:
Fetal membranes were harvested after the separating from the placenta. Membranes were cleansed of all blood and decidua using sterile heparinized saline. Using a sterile cotton gauze membranes were further wiped to remove all the adhering decidua. Membranes were cut into 5 mm circles using a biopsy punch, washed in sterile HBSS x3 and placed in an organ explant system in media consisting of Dulbecco's Modified Eagles medium (DMEM) : F12 Ham mixture (1:1) with antibiotics, 15% FBS and 2mM Glutamine (all reagents from Sigma Chemicals, St. Louis, MO). Media and the fetal bovine serum used in our system contained the lowest endotoxin levels commercially available. Cultures were incubated at 37oC in an atmosphere of 5% CO2 and room air, and the medium was changed on a daily basis. Microscopic examination by phase-contrast microscopy was performed frequently and visible evidence of contamination or tissue death was recorded. Membranes were maintained in organ culture for ten days. During this time viability was confirmed by active metabolism as documented by continued release of metabolites into the media, constitutive GAPDH mRNA production, and evidence of viability as determined by phosphatidylcholine test which measured phospholipase activity. Hematoxylin-Eosin staining done at various time points indicated good tissue morphology. Reverse transcriptase-polymerase chain reaction (RT-PCR) was performed using specific primers for GAPDH (Glyceraldehyde 3 phosphate dehydrogenase) on respective samples collected and frozen each day. GAPDH expression was noticed in the fetal membranes throughout a ten day period in culture. In situ hybridization performed on paraformaldehyde/PBS fixed tissue showed uniform message for GAPDH in amnion and chorion cells up to ten days. In situ hybridization performed with the sense strand for GAPDH provided a negative reaction indicating the specificity of the antisense strand for GAPDH mRNA. To study the response of the membrane in the culture system, tissue samples were stimulated with various doses of endotoxin (E.coli O55:B5) at the end of a 48 hr incubation period. The 48 hr preincubation time was chosen because genes of interest (cytokines) were induced by the physical manipulation in preparation for culture. A return to the base line value of gene expression was achieved over this 48 hr period.
Sigma Chemical
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Testing of tissue viability of amniochorionic membrane in culture:
Amniochorionic membrane in culture were tested for tissue viability by looking for expression of message for GAPDH (house keeping gene). Message expression was studied using RT-PCR (method described in detail below). Hematoxylin-Eosin staining were performed on respective samples at different time points and the tissue morphology analyzed under light microscopy. The release of PLC (phospholipase C) and its hydrolytic reaction with PNPC (p-nitrophenylphosphorylcholine) assayed as an indicator of tissue viability. The method of Sheikhnejad and Srivastava modified for amniochorionic tissue by Ohno et al were used. Normal and stimulated tissues were collected and stored at -70oC. The tissue was homogenized with 1 ml of 0.25mol/L Tris.HCl (pH 7.2) and the homogenate will be centrifuged at 1000g for 10min. Supernatant will be stored at 4oC. The activity of PLC was assayed using PNPC as a substrate. The PNPC solution (20 mol./L) is made in 0.25 mol/L Tris.HCl pH 7.2 containing 1% BSA (w/v) The assay mixture containing 0.3 ml of the substrate and 0.15 ml of the supernatant was incubated at 30oC for 30 min, and the absorbance is measured at 405 nm during incubation. The activity of PLC is expressed in U/mg protein (One unit of the enzyme activity equals 1 micromole of the substrate hydrolyzed per minute).68,103
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Reverse transcriptase-polymerase chain reaction (RT-PCR):
We extract RNA using TRIzol reagent (Superscript Kit, GIBCO-BRL, Grand Island, NY) . DNAse digestions were performed with RNAse free DNAse and the concentration of the precipitated RNA were measure by spectrophotometry. The expression patterns of cytokine mRNA were determined by RT-PCR. For the PCR, we use primers from our previous experiments whose specificity to amplify the required gene sequence has been proven by southern blotting , restriction analysis and sequencing of the PCR products. All new primers planned to be used in our studies are tested for specificity using southern blot hybridization, sequencing of the PCR product and by restriction digestion analysis. Total RNA (0.5 µg) was submitted to random hexamer primed (Superscript Kit, GIBCO-BRL, Grand Island, NY) first strand cDNA synthesis followed by 30 cycles of PCR in a Perkin-Elmer Cetus thermocycler (Perkin-Elmer Cetus Norwalk, CT). PCR products were analyzed on 2% agarose gels and visualized using ethidium bromide. A 1kb DNA ladder (GIBCO-BRL) is used as a molecular weight marker. Representative samples from each batch of experiments were subjected to RT-PCR without reverse transcriptase enzyme to rule out DNA contamination and possible amplification of genomic DNA.
Perkin-Elmer Cetus
GIBCO-BRL, Life Technologies
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Quantitative Competitive Polymerase Chain Reaction:
Quantitative Competitive PCR (QPCR) was achieved using the CLONTECH PCR MIMIC Construction Kit (CLONTECH, Palo Alto, CA). In this competitive PCR assay one set of primers is used to amplify both the target gene cDNA and another neutral DNA fragment (MIMIC DNA). The neutral DNA fragment competes with the target cDNA fragment for the same primers and acts as an internal standard. This protocol uses a non-homologous DNA fragment engineered to contain the desired gene template primers and thus is recognized by a pair of gene specific primers. Serial dilutions of the PCR MIMICs are added to PCR amplification reactions containing constant amounts of experimental cDNA samples. A constant amount of the cDNA is then coamplified with known concentrations of the competitor DNA for 30 cycles. This MIMIC utilizes the same primer as the target cDNA but yields a PCR product of different size. Following PCR, the products were resolved by 1.6% agarose gel electrophoresis and visualized on an ethidium bromide stained gel. A visual comparison is made of the intensities of the bands produced by the target gene and the PCR MIMIC.
Clonetech
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Densitometry of QPCR products:
Quantitation of PCR products was achieved by gel band spot densitometry using the Alpha Ease software program (AlphaInnotech Corporation, San Leandro, CA). Integrated density values for two matching bands (MIMIC and target genes) were obtained and the densitometric ratio was calculated. This value was multiplied by the known concentration of the MIMIC to get the approximate (~) number of molecules. Since the molar concentrations of the MIMIC are known, the relative levels of expression of target mRNA can be estimated (# fold increase/decrease).
AlphaInnotech Corporation
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Paraffin sections for in situ hybridization and immunocytochemistry:
6 µm tissue sections were floated on to the surface of chrome-alum gelatin coated slides and fixed at 42oC overnight. Slides for in situ hybridization was deparaffinized by two, 10 min incubations with xylene and stored in cold absolute ethanol until processing. For immunocytochemistry, the sections were deparaffinized with 2 changes of xylene, rehydrated with descending grades of alcohol and equilibrated with PBS pH 7.4.
Fisher Scientific
Daigger
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In situ hybridization:
In situ hybridization was performed using biotinylated oligonucleotides. The same antisense (3') oligonucleotides used for PCR were used as the hybridization probe. The sense strand (5') were used as a negative control for the specificity of hybridization.
The hybridization solution were prepared by mixing 50% v/v deionized formamide, 2x Denhardt's solution, 2x SSC, 0.1% SDS, 0.1 M Tris pH 8.0 and 20 mm vanydyl ribonucleoside complexes (GIBCO-BRL). Slides stored in ethanol were incubated with hybridization solution and prehybridized in hybridization solution for 1 hr at room temperature. Biotinylated probes were added to the hybridization solution to a final concentration of 0.5 µg/ml. Hybridization was done at 450-550C for 16-18 hrs in a humidified chamber followed by washing with 0.1X SSC at room temperature for 15 min. After blocking endogenous alkaline phosphatase activity, hybridization was detected using streptavidin-alkaline phosphatase followed by incubation with nitroblue tetrazolium-4-bromo-5-chloro-3- indolylphosphate (In situ hybridization detection kit, GIBCO-BRL) in alkaline buffer solution pH 9.5. Sections were washed in deionized water and mounted with Gelmount (Biomedia Corp. Foster City, CA). Photo microscopy of the sections showing reactions will be performed.
Gibco-BRL, Life technologies
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Immuno histochemistry:
Rehydrated sections were quenched in 3% hydrogen peroxide in methanol to block endogenous peroxidase activity followed by a rinse in PBS and blocked with 10% FBS in PBS for 10 min to minimize nonspecific antibody binding. Sections were incubated in PBS at room temperature for 30 min in a humidified chamber with primary monoclonal antibody to the cytokine or substance in question at a dilution to be individually determined for each antibody. After washing, biotinylated anti-mouse immunoglobulin (Zymed, San Francisco, CA) and avidin-horse radish peroxidase (Zymed) were added. The chromogenic reaction was developed with a freshly prepared solution of tetra hydrochloride diaminobenzidine and hydrogen peroxide (Zymed). Sections will be slightly counter stained with Harris hematoxylin. The following antibodies were normally utilized in our laboratory as controls in each experiment; antibodies to collagen type IV (Zymed), fibronectin (Zymed), laminin (AMAC, Inc. Westbrook, ME) as a positive control and anti-HLA-DR (DAKO, Denmark), antibody to single stranded DNA were used as negative control for amnion and chorion cells. PBS without primary antibody was used as a reagent control. Photo microscopy of the sections showing reactions were performed.
Zymed laboratories
Calbiochem
OncogeneProducts
Sigma Chemicals
Biosource International
Promega
R & D Systems
Innogenex
Santacruz Biotechnologies
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Zymography :
Media samples frozen during the experiments were subjected to zymography using specific substrates (gelatin and casein) for detecting the presence of gelatinases (MMP2 and MMP9). Media containing 0.2% lactalbumin hydrolysate were used instead of 15% FBS media to avoid any interference from MMPs in FBS. Sodium dodecyl sulfate (SDS), substrate gel electrophoresis (zymography) was carried out by incorporating an appropriate dilution of substrate into standard 10% polyacrylamide gel electrophoresis (PAGE). After electrophoresis each gel was washed two times for 15 min each in 2.5% Triton X-100 (to remove SDS) and then incubated overnight in 500 mM Tris.Hcl, pH 7.4, containing 10mM CaCl2. Each gel was stained with Coomassie blue for 30 min and then destained in 30% methanol-10% acetic acid. Clear bands on a blue background, due to degradation of the entrapped substrate, indicate the presence of substrate-degrading proteinases whose molecular weight can be estimated from the molecular weight standards simultaneously run on the same gel. A second gel run with the same samples were incubated in a buffer containing 10 mM EDTA to document the metalloproteinase nature of these proteinases.
Novex Laboratories
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Quantitation of zymograms for active MMP2:
Human recombinant active MMP2 (Oncogene Research) were used as standard to run zymograms. Different dilutions of standards (range 1 ng - 0.0001 ng) was made and will be subjected to zymography. The bands produced by these standards of known concentrations was used to calculate the concentration of active MMP2 (a 66 kDa band) in AF samples, culture media, and tissue homogenate by densitometry using the Alpha-Ease soft ware program (also see QPCR quantitation).
Oncogene Research Products
AlphaInnotech Corporation
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Bioactivity testing of MMP9:
The presence of bioactive MMP9 in AF was determined using a bioassay specific for the active form of MMP9 only (Amersham Life Sciences). The assay uses a urokinase proenzyme that can be cleaved into an active enzyme by a single proteolytic step. The natural activation sequence in the proenzyme was replaced by protein engineering, with an artificial sequence recognized only by MMP9. Briefly, MMP9 present in the amniotic fluid was captured onto the wells by incubating at 4oC overnight in an anti-MMP9 antibody coated micro titer plate. After washing, the plates will be incubated at 37oC with a substrate protein (an engineered protein which can be cleaved only by active MMP9) and a detection enzyme for 6 hrs. The resulting color was read at 405 nm using an ELISA plate reader. The concentration of active MMP9 was calculated by regression analysis. For this, standards (recombinant human pro-MMP9) at different concentrations are prepared according to manufacturer's instruction. The activation of pro-MMP9 standards to active MMP9 is achieved by treating them with 1mM p-amino phenyl mercuric acetate (APMA). The sensitivity of the assay used in our laboratory is 0.125 ng/ml.
Amersham Pharmacia
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ELISA: Enzyme linked immunosorbent assay:
The release of cytokines, MMPs and TIMPs of interest into the culture medium can be quantitated using ELISA. The assay procedure involved a multiple-site two step sandwich immunoassay using oligoclonal antibodies(several monoclonal antibodies directed against different epitopes of each specific cytokine). These assays were performed in our laboratory with commercially available kits. Manufacturers instructions were followed for each kit to perform ELISA. Standard curves are developed using duplicate samples of known quantities of recombinant proteins. Sample concentrations were determined by relating the absorbance obtained to the standard curve by linear regression analysis. Colorimetric absorption were read at 450 nm using an Inc Star Automatic microplate reader. Reference filters were chosen based on the assay performed. The assay reagents are generally obtained from the following sources.
R&D systems
Promega corporation
Biosource International
Amersham Pharmacia
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LM-PCR for DNA laddering:
Genomic DNA samples were isolated from representative tissue samples using NucleoBond nucleic acid purification protocols (Clontech Laboratories, Palo Alto, CA). Tissue samples (20 mg) were homogenized and digested in buffer containing proteinase K (0.25 mg/ml) for 2 hours at 50oC. After purification on an AX anion exchange resin DNA was precipitated with isopropanol and washed in ethanol for purification. Purified DNA was resuspended in Tris.EDTA (pH 8.0) buffer by overnight shaking at room temperature. Spectrophotometry was performed to quantitate the DNA.
      Genomic DNA was subjected to a ligation reaction with dephosphorylated adaptors (composed of a 12-mer and a 24-mer) to the ends of the DNA fragments. Human cells undergoing apoptosis were expected to contain nucleosomal fragments (ladders) with 5'-phosphorylated blunt ends which will bind only to the 24-mer. The unbound 12-mers were released by heating the reaction. The 5' protruding ends were filled in using thermostable DNA polymerase. The ligated 24-mer were then used as primers in PCR in which the fragments with adaptors on both ends were exponentially amplified (Clontech Laboratories, Palo Alto, CA). For this, 0.5µg of genomic DNA was mixed with dephopsphorylated oligonucleotide. The reaction was performed at 55oC for 10 minutes allowing the mixture to cool to 10oC over 60 minutes followed by incubation at 10oC for 10 minutes. T4 DNA ligase (200 U) was added and ligations incubated at 16oC for 12 - 16 hours. Ligated DNA (150 ng) was used for PCR assay (100 µl volume) with 24 bp linker primer and thermostable DNA polymerase (Clontech Laboratories, Palo Alto, CA). Samples were amplified for 35 cycles of 1 minute at 94oC and 3 minutes at 72oC and a final extension of 15 minutes at 72oC. To verify the standard amount of DNA (150 ng) in each sample, ligated DNA was subjected to PCR with En-2 (conserved single copy gene) primer. The samples were amplified for 26 cycles of PCR; 1 minute 94oC , 1 minute 70oC and 1 minute 72oC. This PCR yielded a product of 290 bp with equal intensities in all samples tested. The LM-PCR products were then analyzed on an ethidium bromide stained 1.2% agarose gel.
Clontech Laboratories
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Terminal deoxynucleotidyl transferase (TdT) mediated biotinylated DNA fragment end labeling:
Amniochorionic membrane fixed in Histochoice was processed in a tissue processor. Paraffin embedded tissues were applied to chrome-alum gelatin coated slides (6µ thickness) and fixed overnight. Deparaffinization was performed in xylene and dehydration was performed in graded alcohol. Tissue sections were treated with 20 µg/ml of proteinase K for 20 minutes at room temperature. Endogenous peroxidase activity was blocked in 3% hydrogen peroxide in absolute methanol for 5 minutes and slides were washed well in Tris buffered saline. Sections were then incubated with biotin labeled dNTPs for 1.5 hours catalyzed by terminal deoxynucleotidyl transferase (TdT) (CalBiochem, Cambridge, MA). After stopping the reaction, sections were treated with streptavidin-horse raddish peroxidase conjugate for 30 minutes and the color was developed using diamniobenzidine, hydrogen peroxide/urea mixture in water (CalBiochem, Cambridge, MA). The sections were then mounted using Gelmount (Zymed, San Francisco, CA). Controls were carried out with each experiments in which terminal deoxynucleotidyl transferase was omitted from the labeling reaction.
CalBiochem
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