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1.
J Foot Ankle Surg ; 51(3): 365-8, 2012.
Article in English | MEDLINE | ID: mdl-22342112

ABSTRACT

Kaposi's sarcoma is divided into 5 subtypes primarily differentiated by clinical presentation and typical at-risk population. We report the unique case of a 74-year-old Latin American woman who presented with a violaceous lesion on the dorsum of her right second digit, which was diagnosed as Kaposi's sarcoma but was not easily placed into a discrete subtype. We discuss the factors that usually predispose people to this infection and the lack of those factors in our patient, as well as the subsequent treatment of our patient. The patient remained in complete remission at 4 years follow-up.


Subject(s)
Bone Neoplasms/diagnosis , Hispanic or Latino , Sarcoma, Kaposi/diagnosis , Aged , Bone Neoplasms/surgery , Diagnosis, Differential , Female , Follow-Up Studies , HIV Infections , Humans , Sarcoma, Kaposi/surgery , Toes
2.
Foot Ankle Int ; 30(6): 500-5, 2009 Jun.
Article in English | MEDLINE | ID: mdl-19486626

ABSTRACT

BACKGROUND: Although cryosurgery has been used to treat certain conditions, its efficacy for the treatment of heel pain has not been established. The objective of this retrospective case series was to investigate both short- and long-term changes in heel pain after cryosurgery. MATERIALS AND METHODS: A sample of 137 feet (n = 137) was analyzed over a 24-month period after cryosurgery. The mean age was 56 years and the mean BMI was 33. Subjects in our analysis included only those who had failed 6 months of conservative care prior to cryosurgery. Pain was measured using a Numeric Pain Scale (NPS, zero to 10) at 3 weeks and 24 months. Statistics were calculated using SPSS version 12.0 (Chicago, IL). RESULTS: A total of 106 subjects had successful pain relief and 31 subjects failed to gain relief; the success and failure rates were 77.4% and 22.6%, respectively. Mean pain before cryosurgery was 7.6, after cryosurgery at three weeks was 1.6 (p < 0.0005), and after cryosurgery at 24 months was 1.1 (p < 0.0005). CONCLUSION: In subjects who achieved successful pain relief, the significantly lower mean pain score at 3 weeks and 24 months, compared to the initial pain score prior to cryosurgery, suggests that cryosurgery was successful in resolving both short- and long-term heel pain.


Subject(s)
Cryosurgery , Fasciitis, Plantar/surgery , Heel , Adult , Aged , Body Mass Index , Comorbidity , Diabetes Mellitus, Type 2/epidemiology , Female , Humans , Male , Middle Aged , Osteoarthritis/epidemiology , Pain Measurement
3.
FEBS Lett ; 484(2): 159-63, 2000 Nov 03.
Article in English | MEDLINE | ID: mdl-11068052

ABSTRACT

Liver X receptors (LXRs) are nuclear receptors that regulate the metabolism of cholesterol and bile acids. Despite information on the specificity of their natural ligands, oxysterols, relatively little is known about the ligand binding site in LXRs. The helix 3 region in the ligand binding domain (LBD) of peroxisome proliferator-activated receptors (PPARs) has been implicated in ligand entry. Sequence alignment of LXRs, farnesoid X receptor (FXR), and PPARs identified the corresponding helix 3 region in the LXRbeta LBD. Residues F268 and T272, which are conserved in all the aligned sequences and only in LXRs and FXR, respectively, were replaced with alanine. The effects of these mutations on ligand binding and receptor activation were examined using an in vitro ligand binding assay and a cell based reporter assay, respectively. The LXRbeta mutant F268A did not bind ligand. In contrast, conversion of T272 to alanine has no effect on ligand binding. By transiently expressing a chimeric receptor containing Escherichia coli tetracycline repressor (TetR) and LXRbeta LBD and a reporter with a TetR binding site, we show that mutant F268A lost the ability to activate transcription of the reporter, whereas mutant T272A still has an activity similar to that of the wild-type LXRbeta. These data, consistent with the findings in the in vitro ligand binding assay and our 3D modeling, are the first study that identifies a residue critical for ligand binding in LXRbeta.


Subject(s)
Phenylalanine/metabolism , Receptors, Cytoplasmic and Nuclear/metabolism , Amino Acid Sequence , Animals , Binding Sites , CHO Cells , Cricetinae , DNA-Binding Proteins , Ligands , Liver X Receptors , Models, Molecular , Molecular Sequence Data , Mutagenesis , Orphan Nuclear Receptors , Phenylalanine/genetics , Protein Conformation , Receptors, Cytoplasmic and Nuclear/chemistry , Receptors, Cytoplasmic and Nuclear/genetics , Recombinant Fusion Proteins/metabolism , Sequence Homology, Amino Acid , Transcription Factors/chemistry , Transcriptional Activation
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