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Biomedical subjects

N E Fink

Publications and source records attributed to N E Fink.

At least 19 recordsLinked to original sources
PubMed1998

Immunohistochemical localisation of a galectin from Bufo arenarum ovary.

Galectins are a group of soluble animal lectins that exhibit specificity for beta-galactosides and conserve sequence homology in the carbohydrate-recognition domain. The galectin from Bufo arenarum ovary showed a strong cross-reaction with the lectin of 14.5 kDa purified from embryos at early blastula stage. In this paper, we studied the immunohistochemical localisation of the galectin of 14.5 kDa from ovary of the toad B. arenarum in adult ovary sections. We also analysed the immunohistochemical localisation of the embryonic lectin during early development using the antiserum anti-ovary galectin. In the ovary, oocytes in the previtellogenic stage showed strong reactivity in the nucleus and the cortex but not in the cytoplasm. Oocytes in the stage of primary vitellogenesis exhibited a similar pattern in the nuclear and cortical areas but showed immunostaining in the cytoplasm. Intense nuclear staining was detected in oocytes in the stage of late vitellogenesis and in mature oocytes, which also presented strong reactions in the yolk platelets that completely covered the cytoplasm. In blastula embryos the staining was found in the blastomeres, the yolk platelets and the blastocoele. Each lectin localisation is discussed in relation to potential biological roles in the corresponding tissues.

Animals↗
PubMed1998

Red blood cell osmotic fragility in Bufo arenarum exposed to lead.

The effects on red blood cells of a single sublethal dose of Pb of 100 mg kg-1 administrated to adult Bufo arenarum were studied. The blood d-aminolevulinic acid dehydratase (d-ALAD) activity, the red blood cell (RBC) osmotic fragility (OF), and the hematocrit (Hct) were measured in control and lead poisoned toad. The enzyme d-ALAD is considered as a specific biomarker for human and animals lead exposure. In Bufo, lead also provoked a significant decrease in the d-ALAD activity without changes in the Hct. OF test was used to compare the impact of Pb on the extent of the RBC hemolysis produced by osmotic stress. Experimental data (absorbance of solubilized hemoglobin and [NaCl]) were fitted to the Orcutt et al. equation (1995) that allows a precise characterization of the parameters involved in OF. In blood from injected toads, the OF resulted significantly reduced. These changes were interpreted as a consequence of alterations in the composition and conformation of the RBC membrane due to Pb, as it was described for human erythrocytes.

Animals↗
PubMed1998

Evaluation and additional recommendations for preparing a whole blood control material.

OBJECTIVE: The assessment of an easy to prepare and low cost control material for Hematology, available for manual and automated methods. MATERIAL AND METHOD: Aliquots of stabilized whole blood were prepared by partial fixation with aldehydes; the stability at different temperatures (4.20 and 37 degrees C) during periods of up to 8-9 weeks and aliquot variability with both methods were controlled. RESULTS: Aliquot variability with automated methods at day 1, expressed as CV% (coefficient of variation) was: white blood cells (WBC) 2.7, red blood cells (RBC) 0.7, hemoglobin (Hb) 0.6, hematocrit (Hct) 0.7, mean cell volume (MCV) 0.3, mean cell hemoglobin (MCH) 0.6, mean cell hemoglobin concentration (MCHC) 0.7, and platelets (PLT) 4.6. The CV (coefficient of variation) percentages obtained with manual methods in one of the batches were: WBC 23, Hct 2.8, Hb 4.5, MCHC 5.9, PLT 41. Samples stored at 4 degrees C and 20 degrees C showed stability, only a very low initial hemolysis being observed, whereas those stored at 37 degrees C deteriobed a rapidly (metahemoglobin formation, aggregation of WBC and platelets, as well as alteration of erythrocyte indexes). CONCLUSIONS: It was confirmed that, as long as there is no exposure to high temperatures during distribution, this material is stable, allowing assessment, both external and internal, for control purposes, with acceptable reproductivity, both for manual and automatic methods.

Hematology↗
PubMed1998

Hematological parameters in Bufo arenarum injected with sublethal dose of lead acetate.

Lead has been recognized as a high risk toxic for most organisms including human. The effects of Pb in non-mammalian vertebrates are poorly known, particularly in anuran amphibians. The purpose of this study was to determine the effect of this metal on some hematological parameters of adult Bufo arenarum. It was found that all parameters remained unaltered within normal ranges, with the exception of reticulocyte counts which was significantly increased compared to the in controls (3.7% vs. 0.2%). It is suggested that the selective change found in reticulocyte count might be considered as an early response of a biomarker to sublethal exposition of Bufo arenarum to lead.

Animals↗
PubMed1997

Patient's view of dialysis care: development of a taxonomy and rating of importance of different aspects of care. CHOICE study. Choices for Healthy Outcomes in Caring for ESRD.

Quality assessment efforts to enhance public accountability in dialysis care and to support provider efforts to improve care have lacked patient input. To develop brief patient evaluation or satisfaction surveys suitable for busy clinical settings, knowing patients' priorities can be helpful in deciding which aspects of care should be tracked. We conducted a study to identify salient attributes of dialysis care and to rank the importance of these attributes from the perspective of dialysis patients. We analyzed the content of patient focus group transcripts to characterize dialysis care from the patients' perspective. We then surveyed 86 patients to determine how patients would rank the importance of each aspect to quality of dialysis care. The 18 broad aspects of care identified in the focus group included: (1) care provided by nephrologists, (2) care provided by other physicians (nonnephrologists), (3) care provided by dialysis center nurses, (4) care provided by social workers and psychologists, (5) care provided by dieticians, (6) clergy, (7) care provided by technicians and physician assistants/nurse practitioners, (8) care provided by dialysis center staff in general, (9) supplies, (10) treatment choice and effectiveness, (11) patient education and training, (12) self-care, (13) dialysis machines, (14) unit environment and policies, (15) cost containment, (16) billing, (17) cost of care, and (18) health outcomes. Items ranked in the top 10 by both groups of patients included issues related to nephrologists, other doctors, nurses, and patient education and training. Compared with hemodialysis patients, peritoneal dialysis patients gave higher ratings to hospital doctors' and nurses' attention to cleanliness when working with access sites, how correct the nephrologist's instructions to patients are, whether emergency room doctors check with nephrologists, the amount of information patients get about their diet, and how well nurses answer patients' questions. Patients value certain aspects of dialysis care highly, and these aspects differed in some respects for the relatively small number of hemodialysis and peritoneal dialysis patients studied. Construction of brief questionnaires for quality assessment and assurance requires thoughtful consideration of what questions to include. Knowing patients' priorities regarding the most important aspects of care that have high potential for dissatisfaction may be helpful to continuous quality improvement of end-stage renal disease care.

Adult↗
PubMed1997

[External assessment of analytic quality in hematology: a necessity in Latin America].

The assurance of analytical quality in a clinical laboratory is achieved through an internal system of quality control complemented by an external evaluation program. Quality assurance provides a foundation for the confidence that is placed in laboratory results and their use in the diagnosis and treatment of diseases. Many laboratories in Latin American countries do not have appropriate systems in place to evaluate and control quality. Given the importance of diagnoses based on hematologic data, the Pan American Health Organization sponsored a course in quality control in hematology during the XI Latin American Congress of Clinical Biochemistry (Mexico, 1993), in which representatives from Argentina, Chile, Cuba, Mexico, Paraguay, Dominican Republic, and Uruguay participated. As part of the course, the following control materials were produced: secondary standard solution of cyanmethemoglobin, stabilized concentrated hemoglobin solution, and preserved human whole blood with pseudoleukocytes. These materials were sent to laboratories in the seven participating countries for use in analytical procedures, and the results were then subjected to an external evaluation to assess individual performance and the comparability of results among the group. The specific tasks carried out were: (1) determination of values for hemoglobin, hematocrit, and red and white blood cell counts by the procedures normally used in each laboratory; (2) recording of the data on special reporting forms; and (3) transmittal of those forms to the coordinator in each country. The results were analyzed with regard to both the procedure used and the participating country. Reference values were established by consensus following application of a statistical method to eliminate outlying values. Comparative analysis of the results showed the coefficients of variation (CV) of the hematocrit (4.5%), red blood cell count (11.0%), and white blood cell count (22.2%) to be higher than those reported from the United States of America and Europe. With regard to analytical procedures, the manual methods yielded larger CV than the automated methods. When analysis of variance (ANOVA) was used on data broken down by country and by procedure, the only statistically significant result was for leukocyte count (P < 0.02). It was concluded that training in the preparation of quality control materials and the subsequent use of these materials in pilot surveys could provide a starting point for establishing continuous internal and external quality assessment systems in hematology. Such systems, together with continuing education for laboratory personnel and the availability of automated instrumentation, will lead to achievement of optimum laboratory quality.

Hematology↗
PubMed1997

Further studies on vertebrate S-type lectins: cross-reactivity between toad and human lectins.

Galectins (S-type or S-Lac lectins) are a well-defined family of beta-galactoside animal lectins characterized by a high sequence homology in the carbohydrate-binding domain. We have previously purified and characterized the S-type lectin from the ovary of the toad Bufo arenarum. In this study, we purified the S-type lectins from Bufo arenarum ovary and human spleen by an improved method which included ion exchange and affinity chromatography. Antibody cross-reactivities between both lectins and some other S-type lectins showed that they share epitopes. Glycosylation studies carried out with detection/differentiation kits suggested that both lectins are not glycosylated.

Animals↗
PubMed1996

The primary structure and carbohydrate specificity of a beta-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis.

The detailed characterization of a galectin from the toad (Bufo arenarum Hensel) ovary in its primary structure, carbohydrate specificity, and overall biochemical properties has provided novel information pertaining to structural and evolutionary aspects of the galectin family. The lectin consists of identical single-chain polypeptide subunits composed of 134 amino acids (calculated mass, 14,797 daltons), and its N-terminal residue, alanine, is N-acetylated. When compared to the sequences of known galectins, the B. arenarum galectin exhibited the highest identity (48% for the whole molecule and 77% for the carbohydrate recognition domain (CRD)) with the bovine spleen galectin-1, but surprisingly less identity (38% for the whole molecule and 47% for the CRD) with a galectin from Xenopus laevis skin (Marschal, P., Herrmann, J., Leffler, H., Barondes, S. H., and Cooper, D. N. W. (1992) J. Biol. Chem. 267, 12942-12949). Unlike the X. laevis galectin, the binding activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccharide and Galbeta1,3GalNAc relative to lactose, was in agreement with that observed for the galectin-1 subgroup and those galectins having "conserved" (type I) CRDs (Ahmed, H., and Vasta, G. R. (1994) Glycobiology 4, 545-549). Moreover, the toad galectin shares three of the six cysteine residues that are conserved in all mammalian galectins-1, but not in the galectins from X. laevis, fish, and invertebrates described so far. Based on the homologies of the B. arenarum galectin with the bovine spleen galectin-1 and X. laevis skin galectin, it should be concluded that within the galectin family the correlation between conservation of primary structure and phylogenetic distances among the source species may not be a direct one as proposed elsewhere (Hirabayashi, J., and Kasai, K. (1993) Glycobiology 3, 297-304). Furthermore, galectins with conserved (type I) CRDs, represented by the B. arenarum ovary galectin, and those with "variable" (type II) CRDs, represented by the X. laevis 16-kDa galectin, clearly constitute distinct subgroups in the extant amphibian taxa and may have diverged early in the evolution of chordate lineages.

Amino Acid Sequence↗
PubMed1996

Purification and partial biochemical characterization of an S-type lectin from blastula embryos of Bufo arenarum.

1. S-type lectin from Bufo arenarum embryos at blastula stage was purified by affinity chromatography. The molecule is a dimer with equal-sized monomers and the apparent subunit molecular weight was found to be 14.5 kDa. 2. Analytical isoelectric focusing of the pure lectin showed an acidic pI of 4.7. 3. Inhibition of the hemagglutination by mono- and oligosaccharides revealed a specificity for sugars bearing a beta-galactoside configuration. 4. Crossreactivity studies between the blastula lectin and the one purified earlier from adult ovary performed by immunodotting, ELISA and immunoblotting showed that these lectins share many epitopes.

Animals↗
PubMed1996

Galectin-1 from bovine spleen: biochemical characterization, carbohydrate specificity and tissue-specific isoform profiles.

Selected biochemical properties, including the charge heterodispersity profile and carbohydrate specificity, of bovine galectin-1 were determined in detail. The lectin was purified through an improved purification protocol that yielded 35-40 mg/kg of wet tissue with a specific activity of 1.7-2 x 10(4) mg-1.ml. The galectin is a homodimer of approximately 14.5 kDa subunits with E(280)mg/ml of 0.65 ml.mg-1.cm-1. When stored in the presence of its carbohydrate ligand, the lectin's binding activity remained stable in a non-reducing environment even at room temperature. The optimal pH for binding to the ligand was 6.5-8.0. The overall carbohydrate specificity of the bovine galectin-1 isolated from spleen is similar to that of the galectin isolated from heart and to other mammalian galectins that exhibit "conserved" (Type I) carbohydrate recognition domains (CRDs) [Ahmed, H. and Vasta, G.R. (1994) Glycobiology 4, 545-549], but differs from those from Xenopus laevis and rat intestine domain I. The fluorescence of 4-methylumbelliferyl alpha-D-galactopyranoside was quenched on binding to bovine spleen galectin-1. Scatchard plots of data obtained at 5, 15, and 30 degrees C showed that the galectin has two sugar exothermic binding sites with association constants of 3.4 x 10(5), 1.0 x 10(5), and 0.3 x 10(5), respectively. Chemical modification studies indicated that histidine, tryptophan, carboxylic acid, and arginine, but not lysine or tyrosine, are involved in the binding to the carbohydrate ligand. On isoelectric focusing, the spleen galectin-1 appeared as six isoforms ranging from pI4.56-4.88 with main components at pI 4.63 (34.0%), 4.73 (42.6%), and 4.88 (16.6%). The galectin-1 isolated from heart yielded a quali- and quantitatively different profile with four isoforms ranging from pI 4.53-4.73, those with pIs of 4.56, 4.63, and 4.73 being common to the spleen homolog. Edman degradation of selected peptides purified from the spleen galectin-1 digest revealed amino acid sequences identical to those obtained for the heart galectin-1. This suggests that although point mutations in the subunit primary structure may not be the likely source of isolectins, as observed for X. laevis, tissue-specific co- or post-translational modifications may be the possible cause of the differences in the galectin isoform profile between bovine spleen and heart.

Amino Acid Sequence↗
PubMed1996

[Soluble beta-galactoside-binding lectins].

Animal lectins are classified on the basis of structural and functional studies in two types: the C-type, characterized by their dependence on calcium ions and the S-type which are not calcium-dependent, but thiol-dependent. In this late one, a group has been extensively studied as the S-Lac type. They are extracted with saline buffers added with lactose in presence of thiol agents, and constitute a family of structurally related protein which contain a series of conserved amino acids. They specifically bind to complementary glicoconjugates, and their biosynthesis and localization are developmentally regulated. Their role could be related to several biological activities in different organs.

Amino Acid Sequence↗
PubMed1995

Efficacy of ofloxacin vs cefazolin and tobramycin in the therapy for bacterial keratitis. Report from the Bacterial Keratitis Study Research Group.

PURPOSE: To compare ofloxacin solution with a combination of fortified antibiotic cefazolin sodium and tobramycin sulfate solutions in the treatment of bacterial keratitis. METHODS: Patients under care at any one of 28 participating clinical centers who had an eye with suspected bacterial keratitis were randomly allocated in a double-masked manner to treatment with 0.3% ofloxacin solution or a combination of the fortified antibiotics (1.5% tobramycin and 10.0% cefazolin solutions). MAIN OUTCOME MEASURES: Time to healing defined as complete re-epithelization, accompanied by a nonprogressive stromal infiltrate for two consecutive visits. Secondary outcome measures included patient symptoms and signs of infection and adverse reactions to study medications. Only patients with a positive bacterial corneal culture were included in most analyses. RESULTS: A positive bacterial corneal culture was obtained in 140 (56%) of the 248 enrolled patients. The time to healing was similar among the 73 patients receiving ofloxacin and the 67 patients receiving fortified antibiotics (P = .70). By 7 days after study entry, the keratitis in 37% of the ofloxacin group and 38% of the fortified antibiotics group had healed. By 28 days, keratitis in 89% of the ofloxacin group and 86% of the fortified antibiotics group had healed. Two patients receiving ofloxacin and one receiving fortified antibiotics discontinued study medication because of lack of efficacy. Patients receiving ofloxacin reported substantially less burning and stinging on instillation than the patients receiving fortified antibiotics (P < .001). Five of six patients among the 140 with positive bacterial cultures who had study medications discontinued because of ocular side effects were in the fortified antibiotics group; an additional three patients, all in the fortified antibiotics group, among the remaining 108 receiving study medications had ocular side effects. CONCLUSIONS: The efficacy of ofloxacin solution in treating bacterial keratitis is equivalent to that of the fortified cefazolin and tobramycin solutions. The reduced frequency of ocular toxic effects and the relative ease of preparation of ofloxacin are additional considerations.

Adult↗
PubMed1995

Patient-reported symptoms associated with graft reactions in high-risk patients in the collaborative corneal transplantation studies. Collaborative Corneal Transplantation Studies Research Group.

The Collaborative Corneal Transplantation Studies (CCTS) were designed to evaluate the effect of donor-recipient histocompatibility matching and cross-matching on the survival of corneal transplants in high-risk patients. We now report on the role of symptoms in the detection of corneal allograft reactions in the CCTS and on the relationship between symptom reporting and graft survival. The 456 patients transplanted in the CCTS were followed for a minimum of 2 years or until graft failure. The follow-up protocol included 11 scheduled examinations in the first year, four examinations during the second year, and examinations every 6 months thereafter. Interim examinations were performed in response to patient-reported symptoms. At every examination, patients were asked specifically if they had redness, sensitivity to light, loss of vision, or pain (RSVP). Of the 456 patients transplanted, 62% had at least one graft reaction. Patients diagnosed with reactions at scheduled visits in the first postoperative year were 2.5 times more likely to report symptoms than those without reactions. Reports of red eye and vision loss were strongly associated with allograft reaction. However, these symptoms were neither highly sensitive nor specific for reaction (sensitivity = 46%, specificity = 70% at 6 months). The severity of reaction influenced the reporting of symptoms: 69% of patients with severe reactions reported symptoms versus 48% of patients with mild reactions (p < 0.001). The only patient characteristic associated with reliable symptom reporting was age, with younger patients with reactions being more likely to report symptoms.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1994

Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution.

In recent years, the significant contributions from molecular research studies on animal lectins have elucidated structural aspects and provided clues not only to their evolution but also to their multiple biological functions. The experimental evidence has suggested that distinct, and probably unrelated, groups of molecules are included under the term "lectin." Within the invertebrate taxa, major groups of lectins can be identified: One group would include lectins that show significant homology to membrane-integrated or soluble vertebrate C-type lectins. The second would include those beta-galactosyl-specific lectins homologous to the S-type vertebrate lectins. The third group would be constituted by lectins that show homology to vertebrate pentraxins that exhibit lectin-like properties, such as C-reactive protein and serum amyloid P. Finally, there are examples that do not exhibit similarities to any of the aforementioned categories. Moreover, the vast majority of invertebrate lectins described so far cannot yet be placed in one or another group because of the lack of information regarding their primary structure. (See Table 1.) Animal lectins do not express a recombinatorial diversity like that of antibodies, but a limited diversity in recognition capabilities would be accomplished by the occurrence of multiple lectins with distinct specificities, the presence of more than one binding site, specific for different carbohydrates in a single molecule, and by certain "flexibility" of the binding sites that would allow the recognition of a range of structurally related carbohydrates. In order to identify the lectins' "natural" ligands, we have investigated the interactions between those proteins and the putative endogenous or exogenous glycosylated substances or cells that may be relevant to their biological function. Results from these studies, together with information on the biochemical properties of invertebrate and vertebrate lectins, including their structural relationships with other vertebrate recognition molecules, are discussed.

Animals↗
PubMed1994

Risk factors for corneal graft failure and rejection in the collaborative corneal transplantation studies. Collaborative Corneal Transplantation Studies Research Group.

PURPOSE: To evaluate comprehensively the magnitude of suspected risk factors for corneal graft failure from any cause, failure from rejection, and immunologic reaction in patients at high risk for graft failure after corneal transplantation. METHODS: The records of the 457 participants in the Collaborative Corneal Transplantation Studies were reviewed. All participants had at least two quadrants of stromal vascularization and/or a history or previous graft rejection. Patients were followed for 2 to 5 years. Characteristics of the patient, study eye, donor, donor-recipient histocompatibility, and surgical procedure were examined for their association with the graft outcomes of failure from any cause, rejection failure, and immunologic reaction. Multivariate survival analysis techniques were used to estimate rates of graft outcome events and to estimate the magnitude of risk factors. RESULTS: Many apparent risk factors did not maintain their association with graft outcomes after adjustment for other risk factors. Young recipient age, the number of previous grafts, history of previous anterior segment surgery, preoperative glaucoma, quadrants of anterior synechiae, quadrants of stromal vessels, a primary diagnosis of chemical burn, and blood group ABO incompatibility were among the strongest risk factors identified for graft failure. Donor and corneal preservation characteristics had little influence on graft outcome. CONCLUSIONS: Risk of graft failure varies substantially, even within a high-risk population. The number of risk factors present should be considered by the patient and surgeon when contemplating transplantation and planning follow-up.

Adolescent↗
PubMed1992

Reproducibility of HLA-A, B, and DR typing using peripheral blood samples: results of retyping in the collaborative corneal transplantation studies. Collaborative Corneal Transplantation Studies Group (corrected)

Recipients enrolled in the Collaborative Corneal Transplantation Studies were retyped as part of a quality assurance program. Because the observed percentage of HLA-DR homozygosity on original typing was more than twice as high as expected from CCTS allele frequencies, the sample selected for retyping was heavily weighted with patients whose original typing identified fewer than two DR antigens. Retyping was performed in a different laboratory from the laboratory performing the original typing. For the 129 patients who were retyped, agreement between the original and retyping laboratories was 88% for HLA-A, 79% for HLA-B, and 55% for HLA-DR. When criteria was relaxed to consider only discrepancies involving readily identifiable antigens, the agreement improved to 95% for HLA-A, 91% for HLA-B, and 59% for HLA-DR. Identification of a second HLA-DR antigen on retyping when only one DR antigen had been identified on original typing was by far the most common form of disagreement. There were no significant differences in the amount of disagreement among the laboratories. Of special interest is that 50% of the discrepancies involved DR3, DR5, and/or DR6, which have structural similarities. Based on the results of the project, we recommend: (1) replicate testing for all DR typing; and (2) retyping using a second source of antiserum for all subjects having DR blanks.

Corneal Transplantation↗