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1.
Musculoskelet Surg ; 108(1): 87-92, 2024 Mar.
Article in English | MEDLINE | ID: mdl-37644317

ABSTRACT

Most studies comparing medial pivot to the posterior stabilised (PS) systems sacrifice the PCL. It is unknown whether retaining the PCL in the Medial Congruent (MC) system may provide further benefit compared to the more commonly used PS system. A retrospective review of a single-surgeon's registry data comparing 44 PS and 26 MC with PCL retained (MC-PCLR) TKAs was performed. Both groups had similar baseline demographics. The PS and MC-PCLR groups had similar pre-operative range of motion (ROM) (PS:104º ± 20º vs. MC-PCLR: 101º ± 19º, p = 0.70), Oxford Knee Score (OKS) (PS: 27 ± 6 vs. MC-PCLR: 26 ± 7, p = 0.62), and Knee Society Scoring System (KS) Function Score (KS-FS) (PS: 52 ± 24 vs. MC-PCLR: 56 ± 23, p = 0.49). The pre-operative KS Knee Score (KS-KS) was significantly lower in the PS group (PS: 44 ± 14 vs. MC-PLR: 53 ± 18, p < 0.05). At 12-months post-operation, there was significant improvement in all parameters (p < 0.01). Both groups had similar ROM (PS: 115º ± 13º vs. MC-PCLR: 114º ± 10º, p = 0.98), OKS (PS: 41 ± 5 vs. MC-PCLR: 40 ± 4, p = 0.50), KS-FS (PS: 74 ± 22 vs. MC-PCLR: 77 ± 16, p = 0.78), and KS-KS (PS: 89 ± 10 vs. MC-PCLR: 89 ± 10, p = 0.89). The PS group had significant improvement in all parameters from preoperation to 3-month postoperation (p < 0.05), but not from 3-month to 1-year postoperation (p ≥ 0.05). The MC-PCLR group continued to have significant improvement from 3-month to 1-year postoperation (p < 0.05). Preserving the PCL when using MC may paradoxically cause an undesired additional restrain that slows the recovery process of the patients after TKA. Compared to MC-PCLR, a PS TKA may expect significantly faster improvement at 3 months post operation, although they will achieve similar outcomes at 1-year post operation.


Subject(s)
Arthroplasty, Replacement, Knee , Knee Prosthesis , Osteoarthritis, Knee , Posterior Cruciate Ligament , Humans , Posterior Cruciate Ligament/surgery , Knee Joint/surgery , Osteoarthritis, Knee/surgery , Range of Motion, Articular
3.
Water Sci Technol ; 43(11): 17-23, 2001.
Article in English | MEDLINE | ID: mdl-11443959

ABSTRACT

The use of polyvinyl alcohol (PVA) as a matrix for cell immobilization has been extensively studied in various biological systems. However, its suitability has not been reported in biosorption studies where inactivated cells are used as biosorbents. In this work, PVA and alginate as immobilization matrices (for the biosorption of gold by a fungal biomass) were investigated by examining their physical and chemical properties. Compared to alginate gels, PVA gels were shown to be more resistant to mechanical abrasion, and more stable over a wide pH range. Although the PVA matrix did not affect the equilibrium uptake in gold biosorption studies, the time required to attain a removal of 80% of the initial metal concentration was 1.7 times that of the freely suspended biosorbent. This contrasts with the alginate immobilized biosorbent which required an increase of well over ten times the duration to attain the same removal efficiency. Results indicated that PVA gels conferred a lower mass transfer resistance than alginate gels. Gold biosorption by the PVA-immobilized fungi followed the commonly used Langmuir and Freundlich adsorption isotherm models although the former gave a better fit. The uptake of gold was dependent on the initial gold concentration and the biomass loading. Using a fungal biosorbent and gold ions as the model system, the results demonstrate the potential in the use of the PVA as a cell immobilisation matrix for biosorption studies.


Subject(s)
Alginates/chemistry , Fungi/metabolism , Gold/analysis , Polyvinyl Alcohol/chemistry , Absorption , Adsorption , Biomass , Glucuronic Acid , Hexuronic Acids , Hydrogen-Ion Concentration , Indicators and Reagents , Models, Chemical , Water Pollutants, Chemical/isolation & purification , Water Purification/methods
4.
Biochem Eng J ; 8(1): 51-59, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11356371

ABSTRACT

The characteristics of polyvinyl alcohol (PVA) and calcium alginate as immobilization matrices were examined and compared for the uptake of gold by a fungal biomass. PVA-immobilized biomass showed superior mechanical strength and chemical stability. In addition, PVA beads were also stable under a wider range of pH (1-13). The lower mass transfer resistance in PVA beads was evident from kinetic studies which showed a significantly shorter period of time for the immobilized PVA beads to achieve 80% gold removal as compared with immobilized alginate beads. Calculated rate constants and maximum rates for the uptake of gold by both immobilized PVA and immobilized alginate biosorbent revealed a much more rapid uptake phenomenon by the former. BET analyses also indicated a larger surface area and larger pore size distribution in PVA beads, further indicating a lower resistance to mass transfer. Gold biosorption in the immobilized PVA bead could be modeled by both the Langmuir and Freundlich adsorption isotherms.

5.
J Biol Chem ; 275(32): 24807-17, 2000 Aug 11.
Article in English | MEDLINE | ID: mdl-10818108

ABSTRACT

CD38 is a type II transmembrane glycoprotein found on both hematopoietic and non-hematopoietic cells. It is known for its involvement in the metabolism of cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate, two nucleotides with calcium mobilizing activity independent of inositol trisphosphate. It is generally believed that CD38 is an integral protein with ectoenzymatic activities found mainly on the plasma membrane. Here we show that enzymatically active CD38 is present intracellularly on the nuclear envelope of rat hepatocytes. CD38 isolated from rat liver nuclei possessed both ADP-ribosyl cyclase and NADase activity. Immunofluorescence studies on rat liver cryosections and isolated nuclei localized CD38 to the nuclear envelope of hepatocytes. Subcellular localization via immunoelectron microscopy showed that CD38 is located on the inner nuclear envelope. The isolated nuclei sequestered calcium in an ATP-dependent manner. cADPR elicited a rapid calcium release from the loaded nuclei, which was independent of inositol trisphosphate and was inhibited by 8-amino-cADPR, a specific antagonist of cADPR, and ryanodine. However, nicotinic acid adenine dinucleotide phosphate failed to elicit any calcium release from the nuclear calcium stores. The nuclear localization of CD38 shown in this study suggests a novel role of CD38 in intracellular calcium signaling for non-hematopoietic cells.


Subject(s)
Adenosine Diphosphate Ribose/analogs & derivatives , Antigens, CD , Antigens, Differentiation/metabolism , Calcium Signaling/physiology , Cell Nucleus/metabolism , Liver/metabolism , NAD+ Nucleosidase/metabolism , Nuclear Envelope/enzymology , ADP-ribosyl Cyclase , ADP-ribosyl Cyclase 1 , Adenosine Diphosphate Ribose/metabolism , Animals , Antigens, Differentiation/analysis , Antigens, Differentiation/isolation & purification , Cell Nucleus/ultrastructure , Cyclic ADP-Ribose , Kinetics , Liver/ultrastructure , Membrane Glycoproteins , Microscopy, Immunoelectron , Multienzyme Complexes/metabolism , NAD+ Nucleosidase/analysis , NAD+ Nucleosidase/isolation & purification , NADP/metabolism , Nuclear Envelope/ultrastructure , Rats
6.
Arch Biochem Biophys ; 373(1): 35-43, 2000 Jan 01.
Article in English | MEDLINE | ID: mdl-10620321

ABSTRACT

CD38 is a 42- to 45-kDa type II transmembrane glycoprotein with the ability to synthesize cADPR, a metabolite with potent calcium mobilizing properties independent of IP(3). We report here the primary characterization and localization of CD38 in the plasma membrane fraction of rat hepatocyte. Western blot analysis of a partially purified plasma membrane fraction with a panel of polyclonal antibodies against CD38 detected a 42- to 45-kDa protein band which is characteristic of CD38. ADP-ribosyl cyclase activity was found to be present in the plasma membrane fraction, indicating the presence of functionally active CD38. Subfractionation of the plasma membrane to the sinusoidal and bile canalicular membrane fractions showed the presence of ADP-ribosyl cyclase activity in both fractions with the sinusoidal membrane fraction having a 10-fold higher specific activity than the bile canalicular membrane fraction. Immunohistochemical staining with the same panel of polyclonal antibodies showed exclusive differential spatial localization to both the nuclei and sinusoidal domain of the plasma membrane. It is possible that the different spatial distribution of CD38 in the rat hepatocyte might be responsible for its myriad of previously known functional roles.


Subject(s)
Antigens, CD , Antigens, Differentiation/metabolism , Cell Membrane/enzymology , Cell Membrane/immunology , Liver/enzymology , Liver/immunology , NAD+ Nucleosidase/metabolism , ADP-ribosyl Cyclase , ADP-ribosyl Cyclase 1 , Amino Acid Sequence , Animals , Antibodies , Antigens, Differentiation/chemistry , Antigens, Differentiation/immunology , Cell Nucleus/enzymology , Cell Nucleus/immunology , Immunohistochemistry , Isoenzymes/chemistry , Isoenzymes/immunology , Isoenzymes/metabolism , Male , Membrane Glycoproteins , NAD+ Nucleosidase/chemistry , NAD+ Nucleosidase/immunology , Protein Processing, Post-Translational , Rats , Rats, Wistar
7.
Brain Res ; 821(1): 17-25, 1999 Mar 06.
Article in English | MEDLINE | ID: mdl-10064783

ABSTRACT

CD38 is a 42-kDa type II transmembrane glycoprotein that has been shown to catalyze the synthesis and hydrolysis of cyclic ADP-ribose, a metabolite with well-known calcium mobilizing properties independent of IP3. In this report, characterization and localization of CD38 in the porcine and rat eyes were carried out. Western blot analysis of a purified microsomal eye extract detected a single 42-kDa protein band characteristic of CD38. Subcellular fractionation studies indicate the presence of ADP-ribosyl cyclase and NADase activities in the nuclear, membrane and microsomal fractions. Immunohistochemical staining of the rat retina showed the expression of CD38 in three distinct layers: the ganglion cell layer, inner nuclear layer and the pigmented epithelium. In the lens, the lenticular epithelium and lens cells were also immunoreactive for CD38 while in the ciliary body, both the pigmented and non-pigmented epithelium also showed the presence of CD38. For the first time, the presence of CD38/ADP-ribosyl cyclase was detected in the vertebrate eye.


Subject(s)
Antigens, CD/analysis , Antigens, Differentiation/analysis , Eye/immunology , NAD+ Nucleosidase/analysis , Rats/immunology , Swine/immunology , ADP-ribosyl Cyclase , ADP-ribosyl Cyclase 1 , Animals , Blotting, Western , Eye/enzymology , Immunohistochemistry , Membrane Glycoproteins , Microscopy, Confocal , Microsomes/enzymology , Microsomes/immunology
8.
Biochem Mol Biol Int ; 44(4): 841-50, 1998 Apr.
Article in English | MEDLINE | ID: mdl-9584998

ABSTRACT

Purification and characterization of CD38/ADP-ribosyl cyclase in the rat lung tissue was performed with microsomes solubilized in Triton X-100 and the ADP-ribosyl cyclase was then purified using sequential column chromatography. Partially purified rat lung ADP-ribosyl cyclase was analyzed by immunoblotting using an antibody raised against a recombinant rat CD38 and showed the presence of monomer (42 kDa) and dimer (85 kDa) under non-reducing conditions but under reducing conditions, only the monomer was detected. Both the monomer and dimer could be eluted out in a stable manner from SDS-PAGE and the enzymatic activity was retained by the two different forms of CD38/ADP-ribosyl cyclase. Immunohistochemical staining showed the presence of CD38 on the bronchial epithelium and the alveoli.


Subject(s)
Antigens, CD , Antigens, Differentiation/isolation & purification , Antigens, Differentiation/metabolism , Lung/enzymology , NAD+ Nucleosidase/isolation & purification , NAD+ Nucleosidase/metabolism , ADP-ribosyl Cyclase , ADP-ribosyl Cyclase 1 , Animals , Bronchi/enzymology , Cell Nucleus/enzymology , Centrifugation , Cytoplasm/enzymology , Electrophoresis, Polyacrylamide Gel , Epithelial Cells/enzymology , Immunohistochemistry , Membrane Glycoproteins , Microsomes/enzymology , Pulmonary Alveoli/enzymology , Rabbits , Rats
9.
Ann Acad Med Singap ; 23(1): 94-7, 1994 Jan.
Article in English | MEDLINE | ID: mdl-8185280

ABSTRACT

We reviewed 357 patients with carpal tunnel syndrome who had surgical decompression of the carpal tunnel between January 1989 and April 1991. The male to female ratio was 1:6. In 40 patients, there was bilateral involvement. Only 38.5% of the patients complained of numbness or sensory disturbance in the median nerve distribution of the hand. Tinel and Phalen sign tests were positive in about two-thirds of the patients. Electromyographic studies were performed in 329 patients. The commonest surgical procedure was a simple release of the flexor retinaculum at the wrist. Nearly all the patients reported improved symptoms.


Subject(s)
Carpal Tunnel Syndrome/surgery , Adult , Aged , Aged, 80 and over , Carpal Tunnel Syndrome/physiopathology , Electromyography , Female , Humans , Male , Middle Aged
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