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1.
Eur J Ophthalmol ; 18(4): 609-13, 2008.
Article in English | MEDLINE | ID: mdl-18609483

ABSTRACT

PURPOSE: Diabetic macular edema (DME) causes visual loss in diabetic patients. Multifocal electroretinograms (mfERGs) have been used to assess macular function pre- and postvitrectomy for DME. METHODS: A standard three-port pars plana vitrectomy with peeling of inner limiting membrane was performed in 25 eyes of 21 patients (13 male, 8 female) with DME. For each patient, visual acuity examination, measure of retinal thickness (using optical coherence tomography), and mfERGs were performed before and 1 week, 1 month, 3 months, and 6 months after vitrectomy. RESULTS: Mean postoperative visual acuity was significantly improved (p<0.05, t test), with mean increase of 0.17 logMAR units; mean retinal thickness was significantly (p<0.001) decreased after surgery (from 537 microm to 298 microm). The increase of normalized amplitude of central ring was not significant; the mean P1 wave-amplitude increased from 0.33 to 0.40 mV; mean P1 wave-implicit time decreased 2.88 ms. We divided the patients into two groups: Group 1 (13 eyes), in which the visual recovery was less than 0.20 logMAR, and Group 2 (12 eyes), in which the visual recovery was greater than 0.20 logMAR. ERG results were statistically significantly different between the groups (p<0.025), when we consider the response recorded from the central ring. In Group 2 there is a marked reduction in implicit time of both ERGs waves, which was statistically significant for N1 wave (p=0.01). The changes of parameters of mfERG observed 6 months after surgery were consistent with those recorded just 1 week after surgery. CONCLUSIONS: Multifocal electroretinogram can be useful to predict functional prognosis in patients with diabetes who underwent vitrectomy for diabetic macular edema.


Subject(s)
Diabetic Retinopathy/physiopathology , Diabetic Retinopathy/surgery , Electroretinography , Macula Lutea/physiopathology , Macular Edema/physiopathology , Macular Edema/surgery , Vitrectomy/methods , Aged , Epiretinal Membrane/surgery , Female , Humans , Male , Middle Aged , Postoperative Period , Prognosis , Visual Acuity/physiology
2.
Fertil Steril ; 63(5): 1114-7, 1995 May.
Article in English | MEDLINE | ID: mdl-7720927

ABSTRACT

OBJECTIVE: To describe a patient with severe ovarian hyperstimulation syndrome (OHSS) demonstrating a beneficial result of reduction in abdominal ascites with a chest tube placed for bilateral pleural effusions. DESIGN: Case report. SETTING: Academic hospital. PATIENT: A 28-year-old white female with primary infertility on hMG (Pergonal; Serono Laboratories, Randolph, MA) therapy. INTERVENTIONS: Intravenous fluids, lasix, and albumin were administered for correction of laboratory abnormalities, including hemoconcentration, hypoalbuminemia, and leukocytosis. A chest tube was placed for treatment of pleural effusions. MAIN OUTCOME MEASURES: Laboratory values of hematologic measures and electrolytes. Resolution of pleural effusions and abdominal ascites as determined by chest roentgenogram and physical examination. RESULTS: Treatment of OHSS with intravenous fluids, lasix, and albumin corrected the hemoconcentration, hypoalbuminemia, and leukocytosis associated with OHSS. Placement of a chest tube corrected the pleural effusions and abdominal ascites. CONCLUSION: This case report demonstrates a beneficial result of reduction in abdominal ascites by a chest tube placed for pleural effusions.


Subject(s)
Ascites/surgery , Drainage , Ovarian Hyperstimulation Syndrome/surgery , Pleural Effusion/surgery , Adult , Chest Tubes , Female , Fluid Therapy , Humans , Infertility, Female/therapy , Menotropins/adverse effects , Ovarian Hyperstimulation Syndrome/chemically induced
3.
Membr Biochem ; 5(2): 109-17, 1984.
Article in English | MEDLINE | ID: mdl-6323916

ABSTRACT

The epinephrine-induced inotropic effect of the myocardium can be attributed to phosphorylation of the sarcolemmal protein calciductin, as this event is accompanied by a 3.5-fold increase in ATP-independent, voltage-dependent CA2+ uptake by isolated sarcolemmal vesicles. This can be considered as the in vitro equivalent of the Ca2+ slow channel. Ca2+ uptake under these conditions is linear, with the degree of calciductin phosphorylation and inhibitor studies indicate the properties of the unphosphorylated channels are similar to those of the fully activated state. Calciductin has been purified and shows great similarities to phospholamban, a protein modulator of the sarcoplasmic reticulum Ca2+ pump. This raises the interesting possibility that calciductin and phospholamban are identical, although they serve different purposes in the sarcolemma and sarcoplasmic reticulum membranes.


Subject(s)
Calcium/metabolism , Ion Channels/metabolism , Muscle Proteins/metabolism , Myocardium/metabolism , Animals , Calcium-Binding Proteins/metabolism , Dogs , Myocardial Contraction , Phosphorylation , Sarcolemma/metabolism , Sarcoplasmic Reticulum/metabolism
4.
Biochim Biophys Acta ; 728(1): 83-91, 1983 Feb 09.
Article in English | MEDLINE | ID: mdl-6830774

ABSTRACT

Membrane-bound phosphorylatable proteolipids were reported to play a role in the regulation of transmembrane Ca2+ fluxes by catecholamines. A generally applicable purification procedure is described by which such proteolipids as the cardiac sarcoplasmic reticulum phospholamban is purified by solvent extraction followed by high pressure liquid chromatography on microparticulate silica. Phospholamban is thereby purified with a yield of 3.37 mg from 100 mg of sarcoplasmic reticulum proteins, significantly higher than that obtained by any of the previously reported procedures. It appeared homogeneous upon dodecyl sulfate-polyacrylamide gel electrophoresis where it is stained by Coomassie blue and detected by autoradiography. The same procedure is applicable to cardiac sarcolemmal calciductin. Both proteolipids exhibit the same Mr 11 000 and pI 3.7 upon two-dimensional gel electrophoresis. Their amino acid compositions are very similar if not identical. This raises the intriguing possibility that phospholamban and calciductin are identical though they obviously belong to different membranes.


Subject(s)
Calcium-Binding Proteins/isolation & purification , Membrane Lipids/isolation & purification , Membrane Proteins/isolation & purification , Muscle Proteins/isolation & purification , Myocardium/analysis , Proteolipids/isolation & purification , Sarcolemma/analysis , Sarcoplasmic Reticulum/analysis , Amino Acids/analysis , Animals , Chromatography, High Pressure Liquid/methods , Dogs , Electrophoresis, Polyacrylamide Gel
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