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Biomedical subjects

J McNally

Publications and source records attributed to J McNally.

At least 37 records · Page 2Linked to original sources
PubMed1993

In vitro assays for the study of erythrocyte invasion by malarial parasites.

In vitro assays for the study o f erythrocyte invasion by merozoites are available for several primate and rodent malarial species. These assays are essential means by which potential anti-merozoite vaccine candidates are identified. John Dalton, John McNally and Susan O'Donovan describe the various types of invasion assays that are in current use, outline the procedures for performing these assays and add some pointers on interpretation of data derived from them.

Journal Article↗
PubMed1992

Prospective, randomized study comparing amoxycillin-clavulanic acid and cefamandole for the prevention of wound infection in high-risk patients undergoing elective biliary surgery.

The efficacy of amoxycillin-clavulanic acid for prevention of postoperative wound infection was compared with that of cefamandole in 150 patients at risk for infected bile while undergoing elective biliary surgery in a prospective, randomized study. The two groups were comparable for age, sex, risk factors, operative procedures and positive bile cultures. Similar numbers of patients had an uncomplicated postoperative course (amoxycillin-clavulanic acid 70%; cefamandole 73%). Four patients in each group developed wound infection. The incidence of postoperative pneumonia, urinary tract infection and number of days (+/- SD) in hospital (amoxycillin-clavulanic acid 10.1 +/- 4.7; cefamandole 9.7 +/- 5.6) were similar. The efficacy of amoxycillin-clavulanic acid and cefamandole in preventing wound sepsis in high-risk patients undergoing biliary surgery was similar. Economic considerations may favour the use of amoxycillin-clavulanic acid.

Adolescent↗
PubMed1992

Plasmodium berghei and Plasmodium chabaudi chabaudi: development of simple in vitro erythrocyte invasion assays.

Erythrocyte invasion assays are described for two species of rodent malaria, namely Plasmodium berghei and P.c. chabaudi. These invasion assays are simple, are carried out using a candle jar and allow a number of assays to be performed simultaneously. Our results demonstrate that both rodent malaria species show an in vitro preference for reticulocytes although the preference of P. c. chabaudi for these cells is not as marked as that of P. berghei. The details of our invasion assays and our results obtained are discussed.

Animals↗
PubMed1991

Effect of inadequate antivenin stores on the medical treatment of crotalid envenomation.

The case of a 27-y-old male with a serious Crotalus atrox envenomation is presented. His medical care was compromised by the lack of readily available polyvalent Crotalidae antivenin. An investigation of antivenin stocking by health care facilities in Arizona was undertaken. Failure to stock sufficient quantities of antivenin to initiate treatment of a single patient with a severe envenomation was found in 43.5% of urban hospitals, 41.2% of rural hospitals within 25 miles of another hospital, 52.9% of rural hospitals greater than 25 miles from another hospital, and 41.7% of Indian Health Service hospitals. Current antivenin stocking was related to antivenin use during the previous year. Reliance on recent antivenin use to guide current antivenin stocking leaves many hospitals with insufficient antivenin stores and may seriously compromise the medical care of patients suffering from rattlesnake envenomations.

Adult↗
PubMed1990

Does exposure to rubella virus generate endocrine autoimmunity?

Rubella virus is a possible environmental agent which may be involved in triggering autoimmunity to pancreatic islet cells, leading to Type 1 diabetes. Autoantibody responses were determined in 239 10-year-old girls who received live attenuated rubella vaccine, of whom 61 (26%) had no pre-existing rubella immunity. Islet cell antibodies (ICA greater than 5 Juvenile Diabetes Foundation (JDF) units) were present in seven (2.9%) girls before vaccination, and they appeared in three more 6 weeks after vaccination (4.2%). However, the ICA levels were low in all cases and of the three girls who developed ICA greater than 5 JDF units 6 weeks post-vaccination, none had detectable ICA 18 months later. IgG-insulin autoantibodies were present in 17 (7.1%) girls before vaccination, and their prevalence decreased after vaccination (5.4%). Thyroid antibodies (thyroglobulin and microsomal) were present in 2% and 1%, respectively, of the girls before vaccination and none appeared afterwards. Thus, rubella vaccination did not elicit widespread endocrine autoantibody production and viral triggering of endocrine autoimmunity in susceptible subjects remains an open question.

Antigens, Viral↗
PubMed1990

Topical anaesthesia for repair of minor lacerations.

One hundred traumatic skin wounds were sutured under topical anaesthesia using a solution of lignocaine, adrenaline, and cocaine, and the effectiveness of the anaesthesia produced was assessed on a behavioural scale. The procedure was tolerated well by 63 patients, poorly by 11, and in 26 the response was uncertain. The response correlated well with age and with the field of anaesthesia measured from the wound margin. No toxic reactions were observed.

Administration, Topical↗
PubMed1988

The action of the protein kinase C inhibitor, staurosporine, on human platelets. Evidence against a regulatory role for protein kinase C in the formation of inositol trisphosphate by thrombin.

The ability of several putative inhibitors of protein kinase C (PKC) to block dioctanoylglycerol (DC8)-induced phosphorylation of a 47 kDa protein (a recognized substrate for PKC) in human platelets was investigated. Staurosporine (1 microM) caused complete inhibition of phosphorylation, whereas the other reagents were either inactive (polymyxin B) or gave only partial inhibition (C-1, H-7, tamoxifen). Staurosporine (1 microM) fully inhibited the phosphorylation of the 47 kDa protein in platelets challenged with thrombin, but also inhibited the phosphorylation of a 20 kDa protein which is a substrate for myosin light-chain kinase. The inhibition of both kinases by staurosporine was associated with the inhibition of thrombin-induced secretion of ATP and 5-hydroxytryptamine and a slowing of the aggregation response; staurosporine, however, had no effect on the formation of phosphatidic acid and inositol phosphates induced by thrombin. Staurosporine also reversed the inhibitory action of phorbol esters on thrombin-induced formation of phosphatidic acid. These data are consistent with a role for these two kinases in secretion and aggregation (although there must be additional control signals, since aggregation was only slowed, not inhibited), but suggest that neither kinase is involved in the regulation of phosphoinositide metabolism. This latter conclusion contradicts previous observations that the activation of PKC by phorbol esters or membrane-permeable diacylglycerols alters the apparent activity of both phospholipase C and inositol trisphosphatase. Possible explanations for this discrepancy are discussed.

Adenosine Triphosphate↗
PubMed1987

The primary structure of rat ribosomal protein L7. The presence near the amino terminus of L7 of five tandem repeats of a sequence of 12 amino acids.

The covalent structure of rat ribosomal protein L7 was determined in part from the sequence of nucleotides in a recombinant cDNA and in part from the sequence of amino acids in portions of the protein. The complementary analyses supplemented and confirmed each other. Ribosomal protein L7 contains 258 amino acids and has a molecular weight of 30,040. The protein has an unusual and striking structural feature near the NH2 terminus: five tandem repeats of a sequence of 12 residues. Rat L7 appears to be related to ribosomal protein L7 from the moderate halophile Vibrio costicola and perhaps to L30 from Bacillus stearothermophilus, to L7 from the moderate halophile NRCC 41227, and to L22 from Nicotinia tobaccum chloroplast. In addition, there is a sequence of 24 amino acids in rat protein L7 that may be related to segments of the same number of residues in Escherichia coli ribosomal proteins S10, S15, L9, and L22.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA.

The covalent structure of rat ribosomal protein L5, which associates with 5 S rRNA in the organelle, was deduced from the sequence of nucleotides in a recombinant cDNA (pL5-6-4) and confirmed from the sequences of amino acids in portions of the protein. Ribosomal protein L5, encoded by pL5-6-4, contains 296 amino acids and has a molecular weight of 34,298. However, a second recombinant cDNA, pL5-8-5, encodes a protein with an additional methionyl residue at position 236 and may be the product of a second active L5 gene. Rat L5 is homologous to yeast YL3 and to Halobacterium cutirubrum HL13, proteins that also bind to 5 S rRNA. No significant structural similarity, however, was found between rat L5 and other 5 S rRNA-binding proteins; not with a second H. cutirubrum protein HL19, nor the Escherichia coli ribosomal proteins, L5, L18, or L25, nor the Xenopus laevis transcription factor IIIA. H. cutirubrum HL19, however, has structural identity with E. coli L5 and seems to be related to yeast YL3 and, hence, may be an evolutionary link between the prokaryotic and eukaryotic 5 S rRNA-binding proteins. A group of ribosomal proteins not known to be associated with 5 S rRNA are also related to rat L5. They include: rat L39, Euglina gracilis chloroplast S7, Saccharomyces cerevisiae L31 and L46, Homo sapiens L32 and, perhaps, several others as well. There is an especially close interrelationship between rat L5, rat L39, yeast L46, human L32, and mouse L32. These results, and others, suggest that ribosomal proteins form an extended family and that L5 may contain in its structure traces of this affinity.

Amino Acid Sequence↗
PubMed1987

The primary structure of rat ribosomal protein L19. A determination from the sequence of nucleotides in a cDNA and from the sequence of amino acids in the protein.

The covalent structure of rat ribosomal protein L19 was inferred from the sequence of nucleotides in a recombinant cDNA and confirmed from the sequence of amino acids in a portion of the protein. Ribosomal protein L19 contains 196 amino acids and has a molecular weight of 26,971. There are indications that a segment of 23 residues in rat L19 is related to sequences of the same length in Escherichia coli ribosomal proteins L30, L18, and S2.

Amino Acid Sequence↗
PubMed1986

Islet-cell antibodies and insulin autoantibodies in association with common viral infections.

The appearance of islet-cell antibodies (ICA) and insulin autoantibodies (IAA) was sought in a prospective study of subjects with acute infections (mumps, rubella, chickenpox, and measles) followed for 6 months. IAA appeared in many patients' serum samples after these acute infections, IgM-IAA being more prevalent than IgG-IAA; there was a particularly high incidence (81%) after chickenpox. ICA were detected in 2 subjects--in 1 after rubella and in the other after measles, but this patient had evidence of previous rubella and a strong autoimmune family history. ICA did not appear after mumps. It is postulated that viral infections may trigger the production of IgM-IAA by a common mechanism involving polyclonal immunocyte activation.

Acute Disease↗
PubMed1984

The primary structure of rat liver ribosomal protein L39.

The covalent structure of the rat liver 60 S ribosomal subunit protein L39 was determined. Fourteen tryptic peptides were purified, and the sequence of each was established by a micromanual procedure; they accounted for all 50 residues of L39. The sequence of the NH2-terminal 32 residues of L39, obtained by automated Edman degradation of the intact protein, provided the alignment of the first seven tryptic peptides. Two peptides, CNI (28 residues) and CNII (22 residues), were produced by cleavage of protein L39 with cyanogen bromide and the sequence of CNII was determined by automated Edman degradation. This sequence established the order of tryptic peptides T8 through T14. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. Protein L39 contains 50 amino acids and has a molecular weight of 7308. There are indications that a portion of rat L39 is related to a fragment of Escherichia coli ribosomal protein S1.

Animals↗
PubMed1984

A family study of the association between insulin dependent diabetes mellitus, autoantibodies and the HLA system.

A family study of the patients attending a paediatric diabetic clinic was undertaken. Seventy-three percent of the index patients and their families provided samples for HLA typing and autoantibody analysis. The HLA types were analysed and correlated with the auto-antibody data. Ways of predicting which siblings are at risk of developing insulin dependent diabetes mellitus (IDDM) were sought. The antigen DR4 carries a higher relative risk and delta value (viz. 27 and 0.93) than any other antigen. The data did not support the notion of heterogeneity of IDDM on the basis of HLA types or autoantibody status. However, the majority of patients with a younger age of onset were DR4/DR4 homozygotes. The presence of ICA was a good marker for siblings at risk of developing IDDM. Some siblings who developed IDDM had ICA and CF-ICA for long periods of time before developing diabetes. The data supported an intermediate model of inheritance for IDDM.

Adolescent↗
PubMed1983

The primary structure of rat liver ribosomal protein L37. Homology with yeast and bacterial ribosomal proteins.

The covalent structure of the rat liver 60 S ribosomal subunit protein L37 was determined. Twenty-four tryptic peptides were purified and the sequence of each was established; they accounted for all 111 residues of L37. The sequence of the first 30 residues of L37, obtained previously by automated Edman degradation of the intact protein, provided the alignment of the first 9 tryptic peptides. Three peptides (CN1, CN2, and CN3) were produced by cleavage of protein L37 with cyanogen bromide. The sequence of CN1 (65 residues) was established from the sequence of secondary peptides resulting from cleavage with trypsin and chymotrypsin. The sequence of CN1 in turn served to order tryptic peptides 1 through 14. The sequence of CN2 (15 residues) was determined entirely by a micromanual procedure and allowed the alignment of tryptic peptides 14 through 18. The sequence of the NH2-terminal 28 amino acids of CN3 (31 residues) was determined; in addition the complete sequences of the secondary tryptic and chymotryptic peptides were done. The sequence of CN3 provided the order of tryptic peptides 18 through 24. Thus the sequence of the three cyanogen bromide peptides also accounted for the 111 residues of protein L37. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. There is a disulfide bridge between half-cystinyl residues at positions 40 and 69. Rat liver ribosomal protein L37 is homologous with yeast YP55 and with Escherichia coli L34. Moreover, there is a segment of 17 residues in rat L37 that occurs, albeit with modifications, in yeast YP55 and in E. coli S4, L20, and L34.

Amino Acid Sequence↗
PubMed1982

The primary structure of the acidic phosphoprotein P2 from rat liver 60 S ribosomal subunits. Comparison with ribosomal 'A' proteins from other species.

The primary structure of rat liver ribosomal protein P2 was deduced from the sequence of the peptides. Ten peptides were obtained by cleavage of P2 with trypsin. The peptides, which accounted for the 111 residues of P2, were isolated by high voltage electrophoresis and chromatography on cellulose thin layer sheets, and the partial or complete sequence was determined by micromanual or solid-phase procedures using 4-N,N-dimethylaminoazobenzene 4'-isothiocyanate and phenylisothiocyanate. In a similar manner, the sequence of 14 peptic peptides was determined. The sequence of the NH2-terminal 30 residues of P2 was obtained by automatic Edman degradation in a sequenator. The ordering of the tryptic peptides was aided by determination of the partial or complete sequence of fragments generated with chymotrypsin, or Armillaria mellea protease, or by secondary cleavage of peptic peptides with trypsin. The carboxyl-terminal sequence was obtained from a cyanogen bromide fragment and from hydrolysis with carboxypeptidase. The sequence of protein P3 was also determined. P3 differs from P2 only in that it lacks the carboxyl-terminal 8 residues, and hence, it is likely to be a proteolytic product of P2. Rat liver ribosomal protein P2 is homologous with yeast YP A1, with Artemia salina eL12, and with Halobacterium cutirubrum L20. It is likely that rat liver P2 is also homologous with the prokaryotic ribosomal "A" proteins, Escherichia coli L7/L12, Micrococcus lysodeikticus MA1, and Bacillus subtilis L9, but that during evolution, a transposition of a portion of the molecule occurred.

Amino Acid Sequence↗
PubMed1982

Pretreatment behavioral profiles associated with subsequent psychosocial adjustment in radiation therapy patients: a prospective study.

A clinically derived system of judging cancer patients' engagement, reality testing and degree of arousal during a pretreatment consultation was found predictive of psychosocial problems or no problems reported by sixty cancer patients one month after starting radiation therapy. Independent ratings of psychosocial problems by the treating oncologists, nurses and radiation therapists three months after starting treatment were also found significantly associated with the pretreatment composite. Disease, treatment and demographic factors were not predictive of psychosocial problems and were not associated with the pretreatment clinical composite. Follow-up observations at six months and eighteen to twenty-four months of forty-four and twenty-four of the original patients available for study revealed there was no continuing association between their pretreatment clinical composites and psychosocial problem ratings.

Adult↗