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Biomedical subjects

C T Lim

Publications and source records attributed to C T Lim.

At least 73 records · Page 4Linked to original sources
PubMed1989

Meconium peritonitis due to meconium ileus presenting as fetal ascites: a case report.

A case of meconium peritonitis due to meconium ileus is described. The condition was detected antenatally as fetal ascites on ultrasonography. Plain X-ray of abdomen post-natally showed specks of calcification mainly at the flanks, while on ultrasonography specks of high echogenic areas were seen throughout the abdomen which has been described as "snow-storm sign". The aetiology of meconium ileus is briefly discussed.

Adult↗
PubMed1987

A photoaffinity label for the thromboxane A2/prostaglandin H2 receptor in human blood platelets.

A photoactive iodoarylazide derivative (I-APA-PhN3) of the competitive thromboxane A2/prostaglandin H2 (TXA2/PGH2) antagonist 13-azaprostanoic acid is evaluated. Upon photoactivation, the compound was found to inhibit specifically and irreversibly human platelet aggregation induced by the TXA2/PGH2 mimetic U46619. In receptor-binding studies using [3H]U46619, I-APA-PhN3 exhibited an IC50 of 300 nM for inhibition of U46619 binding. Photoactivation of I-APA-PhN3 resulted in an irreversible 58% reduction in specific binding of U46619. This compound and its corresponding ratio-iodinated form will prove to be useful tools for the isolation and purification of the TXA2/PGH2-binding protein in human platelets.

Affinity Labels↗
PubMed1987

Preparation and biological evaluation of a potential photoaffinity label for the prostaglandin H2/thromboxane A2 receptor.

Two aromatic azides (24 and 26) were prepared as potential photoaffinity probes for the PGH2/TXA2 receptor. The compounds are based on the well-characterized PGH2/TXA2 receptor antagonist 13-azaprostanoic acid, with the terminus of its lower side chain replaced with phenoxy (24) or benzyl (26) azide functionality. The two compounds were shown to irreversibly inhibit platelet function after photolysis and resuspension. However, of the two aromatic azides, only the benzyl derivative 26 appeared to be selective for the prostaglandin pathway. The latter compound was also prepared as the aromatic 125I (29) derivative, which may ultimately prove useful as a labeled probe for the identification and isolation of the putative TXA2/PGH2 receptor.

Adenosine Diphosphate↗
PubMed1985

Disulfide-linked and transglutaminase-catalyzed protein assemblies in platelets.

Energy depletion induces the formation of disulfide-linked and transglutaminase-catalyzed protein assemblies in platelets. The disulfide type polymers, formed following incubation at 37 degrees C in the absence of adenosine triphosphate (ATP)-generating precursors, are composed of cytoskeletal proteins and are associated with a decrease of reduced glutathione levels accompanying ATP depletion. The maintenance of ATP and reduced glutathione levels to, respectively, 34% and 47% of their original values is sufficient to prevent the formation of both polymer types. The transglutaminase-type cross-links are formed in the presence of calcium in either "energy-depleted" or thrombin stimulated platelets. 125I-surface-labeled membrane proteins, presumably transmembrane proteins, are incorporated into the transglutaminase-catalyzed cross-linked polymer of thrombin-stimulated platelets. Glycoproteins IIb and IIIa are not essential to the polymer formation, since thrombasthenic platelets treated with thrombin exhibit the same type of labeled polymer. The transglutaminase-catalyzed polymer formation following thrombin stimulation of platelets is inhibited by a calcium channel blocker, an intracellular calcium antagonist, as well as other inhibitors such as indomethacin, dibutyryl cyclic AMP, and prostaglandin E1. Although the evidence points to the formation of transglutaminase-catalyzed cross-linking in the cytoplasmic compartment, additional cross-linking of extruded components cannot be excluded.

Acyltransferases↗
PubMed1981

Purification and properties of human N-acetylgalactosamine-6-sulfate sulfatase.

1. Human N-acetylgalactosamine-6-sulfate sulfatase (EC 3.1.6.-) from human placenta has been purified more than 3000-fold by gel filtration, ion-exchange and substrate affinity chromatography. The enzyme has a molecular weight of 90 000 by gel filtration chromatography and 85 000 by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Enzyme purified from cultured human skin fibroblasts has similar properties. 2. The tritium-labeled chrondroitin 6-sulfate trisaccharide N-acetylgalactosamine 6-sulfate-(beta, 1-4)-glucuronic acid-(beta, 1-3(-N-acetyl[1-3H]galactosaminitol 6-sulfate as substrate demonstrated a Km of 0.12 mM at pH 4.5. Sulfate was hydrolyzed only from the non-reducing terminal of this disulfated trisaccharide. Hyaluronic acid, dermatan sulfate, chondroitin 4-sulfate, heparin and chondroitin 6-sulfate tetrasaccharide were slightly inhibitory, whereas 6-sulfated pentasaccharides and heptasaccharides were strongly inhibitory. The enzyme dose not hydrolyze sulfate from N-acetylglucosamine 6-sulfate.

Chondroitinases and Chondroitin Lyases↗
PubMed1976

Apoproteins of human serum high density lipoproteins. Isolation and characterization of the peptides of Sephadex fraction V from normal subjects and patients with abeta-lipoproteinemia.

1. Sephadex fraction V, obtained from human serum high density lipoprotein apoprotein (HDL apoprotein) of normal subjects and of patients with abetalipoproteinemia, was resolved by DEAE-cellulose ion exchange column chromatography into several fractions which were defined in terms of amino acid composition, NH2- and COOH-terminsls, sialic acid content, immunologic and electrophoretic properties, and in vitro activation of purified lipoprotein lipase from rat adipose tissue. 2. Fraction V of HDL apoprotein of both normal and abetalipoproteinemic subjects was found to contain polypeptides corresponding to apolipoproteins C-I, C-II, C-III-1, and C-III-2, which had been described previously in very low-density lipoproteins (VLDL). The content of apo C-III-1 in abetalipoproteinemia-HDL was very low, whereas the percentage, by weight, of apo C-I was about twice as high as that in the normal subjects studied. Furthermore, both normal and abetalipoproteinemia-HDL apoprotein contained a previously unreported peptide which had a molecular weight of about 7 000 and electrophoretic, chemical, and immunological properties distinct from those of the known C apolipoproteins. Of all of the peptides comprising fraction V, only apo C-II activated a purified preparation of rat adipose tissue lipoprotein lipase. This was the case for both normal and abetalipoproteinemic subjects.

Amino Acids↗
PubMed1975

Human brain and placental choline acetyltransferase: purification and properties.

Choline acetyltransferase (EC 2.3.1.6) catalyzes the biosynthesis of acetylcholine according to the following chemical equation: acetyl-CoA + choline in equilibrium to acetylcholine + CoA. In addition to nervous tissue, primate placenta is the only other animal source which contains appreciable acetylcholine and its biosynthetic enzyme. Human brain caudate nucleus and human placental choline acetyltransferase were purified to electrophoretic homogeneity using ion-exchange and blue dextran-Sepharose affinity chromatography. The molecular weights determined by Sephadex G-150 gel filtration and sodium dodecyl sulfate gel electrophoresis are 67000 plus or minus 3000. N-Ethylmaleimide, p-chloromercuribenzoate, and dithiobis(2-nitrobenzoic acid) inhibit the enzyme. Dithiothreitol reverses the inhibition produced by the latter two reagents. The pKa of the group associated with N-ethylmaleimide inhibition is 8.6 plus or minus 0.3. A chemically competent acetyl-thioenzyme is isolable by Sephadex gel filtration. The enzymes from the brain and placenta are thus far physically and biochemically indistinguishable.

Acetyltransferases↗
PubMed1974

A study of the abnormal lipoproteins in abetalipoproteinemia.

The serum lipoproteins of five patients with abetalipoproteinemia (ABL) were separated by ultracentrifugation and then analyzed either intact or after delipidation. In accord with previous findings, all of the patients lacked serum particles with the characteristics of normal low-density lipoproteins (LDL) and of the LDL apoprotein as assessed by immunochemical methods. Each patient exhibited on every examination an abnormal particle, "LDL", which had the flotational properties of LDL, the polypeptide makeup of high-density lipoproteins HDL, the spectral and morphological characteristics of neither LDL nor HDL, and a relatively low content of cholesteryl esters. The HDL were abnormal in having a marked decrease in their total plasma content, an altered proportion of the subclasses HDL2 and HDL3, and a peculiar polypeptide distribution, comprising both normal and additional components, usually not seen in normal controls. The patients also exhibited a decrease of plasma lecithin-cholesterol acyl transferase (LCAT) activity which probably accounted for the low content of cholesteryl esters in both "LDL" and HDL, and in turn for the unusual appearance of "LDL" on electron microscopy. It is concluded that ABL is a disorder affecting all serum lipoprotein classes. Whether the abetalipoproteinemia previously described and noted in the current studies is related to or independent of the abnormalities observed in the other lipoproteins was not established. How the deficiency of LCAT activity, observed in all patients studied, contributed to some of the observed structural lipoprotein abnormalities also remained undetermined.

Abetalipoproteinemia↗
PubMedDate not supplied

Characterization of the surface biocompatibility of the electrospun PCL-collagen nanofibers using fibroblasts.

The effect of nanofiber surface coatings on the cell's proliferation behavior was studied. Individually collagen-coated poly(epsilon-caprolactone) (PCL) nanofibers (i.e., Collagen-r-PCL in the form of a core-shell structure) were prepared by a coaxial electrospinning technique. A roughly collagen-coated PCL nanofibrous matrix was also prepared by soaking the PCL matrix in a 10 mg/mL collagen solution overnight. These two types of coated nanofibers were then used to investigate differences in biological responses in terms of proliferation and cell morphology of human dermal fibroblasts (HDF). It was found that coatings of collagen on PCL nanofibrous matrix definitely favored cells proliferation, and the efficiency is coating means dependent. As compared to PCL, the HDF density on the Collagen-r-PCL nanofiber membrane almost increased linearly by 19.5% (2 days), 22.9% (4 days), and 31.8% (6 days). In contrast, the roughly collagen-coated PCL increased only by 5.5% (2 days), 11.0% (4 days), and 21.0% (6 days). SEM observation indicated that the Collagen-r-PCL nanofibers encouraged cell migration inside the scaffolds. These findings suggest that the Collagen-r-PCL nanofibers can be used as novel functional biomimetic nanofibers toward achieving excellent integration between cells and scaffolds for tissue engineering applications.

Biocompatible Materials↗
PubMedDate not supplied

Changes in flexural properties of composite restoratives after aging in water.

This study evaluated the changes in flexural properties of microfill (Filtek A110 [AO]), minifill (Filtek Z100 [ZO] and Z250 [ZT]), poly-acid modified (F2000 [FT]), and flowable (Filtek Flowable [FF]) composites after aging in water. The flexural strength and modulus of the composites were determined after one week and one month of aging in water at 37 degrees C. Samples were prepared and tested according to ISO specifications. Data was analyzed using ANOVA/Scheffe's test and independent samples t-test at significance level 0.05. Mean flexural strength (n=7) ranged from 66.61 to 147.21 and 68.74 to 142.69 MPa at one week and one month, respectively. Mean flexural modulus (n=7) at one week and one month ranged from 3.45 to 11.30 and 4.76 to 13.02 GPa, respectively. ZO and ZT were significantly stronger than AO, FT and FF and FF was significantly stronger than AO & FT at both time periods. At one week and one month, AO and FF were significantly more flexible than the ZO, ZT and FT. In addition, ZO and FT were significantly stiffer than ZT. With the exception of AO, a significant increase in flexural modulus was observed with all composites. Although flexural strength of FT and FF was significantly increased with aging in water, the flexural strength of ZT was significantly decreased.

Analysis of Variance↗
PubMedDate not supplied

Effect of food-simulating liquids on the shear punch strength of composite and polyacid-modified composite restoratives.

This study evaluated the effects of food-simulating liquids on the shear punch strength of two composites (Tetric Ceram [TC], Vivadent; Esthet X [EX], Dentsply), a conventional (Compoglass [CG], Vivadent) and a posterior polyacid-modified (Dyract Posterior [DP], Dentsply) composite. Thirty-two specimens (10-mm in diameter and 1.6-mm thick) of each material were made, randomly divided into four groups of eight and conditioned for one week as follows--Group 1 (control): air at 37 degrees C; Group 2: distilled water at 37 degrees C; Group 3: 75% ethanol-water solution at 37 degrees C and Group 4: heptane at 37 degrees C. After conditioning, the specimens were restrained within the test apparatus and subjected to shear punch strength testing using a 3.2 mm diameter punch at a crosshead speed of 0.5 mm/minute. The shear punch strength of the specimens was computed and the data was subjected to ANOVA/Scheffe's tests at significance level 0.05. The effect of food-simulating liquids on shear strength was found to be material dependent. All materials with the exception of EX were significantly weakened by ethanol solution. For DP, a significant increase in strength was observed after conditioning in water. EX was significantly stronger than TC and DY after conditioning in air, water and ethanol solution. The shear punch strength of EX and CG was significantly higher than DY after conditioning in heptane.

Analysis of Variance↗