Biomedical subjects

S Upadhye

Publications and source records attributed to S Upadhye.

4 recordsLinked to original sources

PubMed2001

Approach to learning disability.

Learning disabilities (LD) is one of the important causes of poor academic performance in school going children. Learning disabilities are developmental disorders that usually manifest during the period of normal education. These disabilities create a significant gap between the true potential and day to day performance of an individual. Dyslexia, dysgraphia and dyscalculia denote the problem related to reading, writing and mathematics. Perinatal problems are certain neurological conditions, known to be associated with LD; however, genetic predisposition seems to be the most probable etiological factors. Evaluation of a child suspected to be having LD consists of medical examination, vision and hearing test analysis of school performance. The psycho-behaviour assessment and education testing are essential in the process of diagnosis. The experienced persons in the field of LD should interpret the results of such tests. With Individualized Remedial Education Plan (IEP) most children learn to cope up with disability and may get integrated in a regular steam.

Adolescent↗

PubMed1995

Interaction of peptide substrates of fibroblast collagenase with divalent cations: Ca2+ binding by substrate as a suggested recognition signal for collagenase action.

To correlate structural data on substrates of human fibroblast collagenase with their interaction with the enzyme, we have studied: Ac-PLG-s-LLG-O-ethyl ester (I), Dnp-PLGLWA(d-Arg)-NH2 (II), AcGPEGLRVG-O-ethyl ester (III) and Succ-GPLGP-O-amidomethylcoumaryl ester (IV). Peptides I and II represent collagenase cleavage sequences in collagen, peptide III is a mimic for the cleavage site in alpha 2-macroglobulin and peptide IV represents a non-substrate model. Kinetic data showed that peptides I, II and III were substrates of the enzyme. In contrast, peptide IV was not acted upon by the enzyme. Circular dichroism data on the peptides showed that the peptides assume ordered structures in water and trifluoroethanol. In the latter solvent, peptides I and III bound Ca2+ and Zn2+ while peptide II bound Ca2+ but not Zn2+. Peptide IV did not bind either cation in this solvent. Together with the kinetic data, the results suggest that the collagenase cleavage segments in collagen and non-collagen substrates of collagenase could interact with Ca2+ and the enzyme to form a ternary complex. This, in turn, would imply a cofactor role for Ca2+ in collagenase action in addition to the solely structural role ascribed so far to this cation.

Amino Acid Sequence↗

PubMed1992

Search for peptide immunogens of the beta-subunit of human chorionic gonadotropin (hCG) capable of eliciting hormone specific and neutralizing antisera. Identification of an undecapeptide eliciting hCG-specific antisera.

The work reported herein describes our attempts to identify peptide immunogens of the beta-subunit of the pregnancy-specific placental hormone, human chorionic gonadotropin (hCG), capable of eliciting hormone specific and neutralizing antisera. Hydrophilicity profiles of the beta-subunits of hCG and the homologous pituitary hormone, human luteinizing hormone (hLH) were compared and two sequences which are hydrophilic but unique to hCG-beta were identified. They are 6-12 and 109-119 of hCG-beta. Results of the studies with the undecapeptide 109-119 of hCG-beta are reported in this paper. The undecapeptide amide was synthesized using the p-(acyloxy) benzhydrylamine resin and antisera to the peptide were elicited in rabbits using the peptide-diphtheria toxoid conjugate. The peptide is highly immunogenic as both the rabbits responded with high titers of antibodies to the peptide. The antipeptide antibodies bound to hCG but not to hLH showing thereby that the region 109-119 of hCG-beta is a unique determinant of hCG. However, the antibodies were found not to neutralize the biological activity of hCG.

Amino Acid Sequence↗

PubMedDate not supplied

Efficacy of intravenous ketoprofen for pre-emptive analgesia.

AIM: To determine whether intravenous ketoprofen is effective as pre-emptive analgesia for breast surgery. DESIGN: Randomised, controlled, double blind study. PATIENTS AND METHODS: 50 patients undergoing breast surgery under general anaesthesia randomised to receive either 100 mg intravenous ketoprofen 30 minutes before (Group I), or immediately after surgical incision (Group II). Postoperatively, pain scores (Visual Analogue Scale, VAS) and time to rescue analgesic were recorded by an independent, blinded observer. The study was terminated when rescue analgesic was required (VAS > or =4 or demand for analgesic). STATISTICAL ANALYSIS: Continuous variables were analysed by the unpaired 't' test, discrete variables with the chi square test, and survival curves by the log-rank test. RESULTS: Pain scores were significantly lower in Group I till 10 hours after surgery. The number of patients requiring analgesia at 4, 6, 8 and 10 hours was significantly lower in group I (0% vs. 47% [P <0.0001], 0% vs. 44% [P <0.003], 0% vs. 80% [P <0.0001], 0% vs. 100% [P <0.0001] respectively). The mean time for rescue analgesic was 15.47 -/+ 2.87 hours in group I versus 4.22 -/+ 2.55 hours in group II (P <0.0001). CONCLUSION: Pre-emptive analgesia with Intravenous ketoprofen (100mg) produces better postoperative pain-relief in patients undergoing breast surgery.

Adult↗