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K Ramsay

Publications and source records attributed to K Ramsay.

10 recordsLinked to original sources
PubMed2002

Facilities for chemical decontamination in accident and emergency departments in the United Kingdom.

OBJECTIVE: To audit the facilities for chemical decontamination, with special reference to cyanide poisoning, in all major accident and emergency departments in the UK. METHOD: A simple postal questionnaire was used to audit planning, premises, equipment, protection for staff, and stocks of specific antidotes to cyanide poisoning. RESULTS: 227 questionnaires from 261 departments (87%) were returned and used in the survey. Of the 227 departments who responded, 151 (66%) had a written plan; 168 (74%) departments had premises for decontamination; 55 (24%) were judged to have satisfactory premises; 146 (64%) departments had a shower or hose for decontamination; 60 (26%) departments had a decontamination trolley suitable for "stretcher" patients; 203 (89%) had some protective equipment for staff but only 77 (34%) had complete protection--that is, goggles, chemical resistant clothing, and breathing apparatus. In the authors' opinion only seven (3%) departments had satisfactory premises and equipment to treat "stretcher" patients and full protection for staff. A further 11 (5%) departments were equipped to manage ambulant patients at a similar level. Some 205 (90%) departments stocked one or more antidotes to cyanide and 77 (34%) stocked all four antidotes. Thirty four (15%) departments held all four antidotes to cyanide and had full protection for staff. Only five (2%) departments had satisfactory premises and equipment to treat "stretcher" patients, full protection for staff, and at least three of four antidotes. CONCLUSIONS: Most departments had some equipment for chemical decontamination. However, there were major inconsistencies in the range of equipment held and these limited its usefulness. Only a small minority of departments was satisfactorily equipped to deal with a serious chemical incident.

Cyanides↗
PubMed1996

Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts. Decreased expression in transformed cells.

We have used an interaction cloning strategy to isolate cDNAs for sequences that interact with protein kinase C (Chapline, C., Ramsay, K., Klauck, T., and Jaken, S. (1993) J. Biol. Chem. 268,6858-6861). In this paper, we report a novel sequence, clone 72, isolated according to this method. Clone 72 has a 4.8-kilobase pair open reading frame; antibodies to clone 72 recognize a >200-kDa protein in cell and tissue extracts. Clone 72 message and protein are detected in a variety of tissues. Immunoprecipitation studies demonstrate that clone 72 is the major >200-kDa binding protein described previously in REF52 fibroblasts (Hyatt, S. L., Liao, L., Aderem, A., Nairn, A., and Jaken, S. (1994) Cell Growth & Differ. 5, 495-502). Expression of clone 72 message and protein are decreased in progressively transformed REF52 cells. Since clone 72 is both a protein kinase C (PKC)-binding protein and substrate, decreased levels of clone 72 may influence both the subcellular location of endogenous PKCs as well as signaling events associated with clone 72 phosphorylation. Our results emphasize that the role of PKCs in carcinogenesis may involve several factors, including the quantity and location of the PKCs isozymes and their downstream targets.

Amino Acid Sequence↗
PubMed1995

35H, a sequence isolated as a protein kinase C binding protein, is a novel member of the adducin family.

We recently cloned a partial cDNA (35H) for a protein kinase C (PKC) binding protein from a rat kidney cDNA library and demonstrated that it is a PKC substrate in vitro (Chapline, C., Ramsay, K., Klauck, T., and Jaken, S. (1993) J. Biol. Chem. 268, 6858-6861). Additional library screening and 5' rapid amplification of cDNA ends were used to obtain the complete open reading frame. Amino acid sequence analysis, DNA sequence analysis, and Northern analysis indicate that 35H is a unique cDNA related to alpha-and beta-adducins. Antisera prepared to the 35H bacterial fusion protein recognized two polypeptides of 80 and 90 kDa on immunoblots of kidney homogenates and cultured renal proximal tubule epithelial cell extracts. The 35H-related proteins were similar to alpha- and beta-adducins in that they were preferentially recovered in the Triton X-100-insoluble (cytoskeletal, CSK) fraction of cell extracts and were predominantly localized to cell borders. Phorbol esters stimulated phosphorylation of CSK 35H proteins, thus emphasizing that sequences isolated according to PKC binding activity in vitro are also PKC substrates in vivo. The phosphorylated forms of the 35H proteins were preferentially recovered in the soluble fraction, thus demonstrating that phosphorylation regulates their CSK association and, thereby, their function in regulating cytoskeletal assemblies. We have isolated another PKC binding protein partial cDNA (clone 45) from a rat fibroblast library with substantial homology to alpha-adducin. Antisera raised against this expressed sequence recognized a protein of 120 kDa, the reported size of alpha-adducin, on immunoblots of renal proximal tubule epithelial cell extracts. A 120-kDa protein that cross-reacts with the clone 45 (alpha-adducin) antisera coprecipitated with 35H immunecomplexes, indicating that alpha-adducin associates with 35H proteins in vivo. Taken together, these results indicate that 35H is a new, widely expressed form of adducin capable of forming heterodimers with alpha-adducin. We propose naming this adducin homologue gamma-adducin.

Amino Acid Sequence↗
PubMed1994

Protein kinase C isozymes in progressively transformed rat embryo fibroblasts.

The role of individual protein kinase C (PKC) isoforms in progressive transformation of a rat embryo fibroblast cell line (REF52 cells) has been evaluated. Normal (REF A) cells were transfected with SV40 to produce the partially transformed REF B cell line. REF B cells are morphologically transformed but have only limited capacity for growth in soft agar. Message and protein levels for PKC-alpha and PKC-delta were similar in REF A and B cells, indicating that expression of SV40 large T did not directly influence the amounts of PKCs. However, PKC-alpha localization was influenced. PKC-alpha was associated with focal contacts of REF A but not REF B cells, indicating that changes in location rather than content are an early event in REF52 cell transformation. Clones of REF B cells were selected for growth in soft agar (REF C cells). Levels of PKC-delta, but not PKC-alpha or epsilon, were increased in several of these clones, suggesting that increased PKC-delta content may facilitate anchorage-independent growth. In other studies, we have determined that PKCs interact with their binding proteins/substrates through their regulatory domains (RD; L. Liao et al., Biochemistry, 33: 1229-1233, 1994). These results predict that RDs could potentially inhibit PKC signaling by competing with endogenous wild-type PKCs for binding protein/substrate interactions. Overexpression of the RD of PKC-delta inhibited growth in soft agar of one representative REF C clone, whereas overexpression of the RD of PKC-alpha promoted growth in soft agar. These results suggest that RD expression may be a useful approach for dominant negative PKC inhibitors with potential isozyme specificity.

Animals↗
PubMed1993

Interaction cloning of protein kinase C substrates.

We have previously used an overlay assay technique to detect proteins that interact with protein kinase C (PKC) (Hyatt, S. L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as substrates. Therefore, we used the overlay assay approach to screen a rat kidney lambda gt11 cDNA library to isolate and identify additional PKC substrates. Two clones have now been characterized. 35A is the rat homologue of the myristoylated alanine-rich C kinase substrate (MARCKS)-related F52 cDNA, whereas 35H is a partial cDNA with substantial homology to the 3' end of beta-adducin. Both cDNAs encode proteins that bind phosphatidyl-serine (PS) and are substrates for PKC. Phosphorylation decreased both PS and PKC binding activities. Both proteins contain high density positive charge domains similar to that found in the major PKC substrate MARCKS. These results demonstrate that PKC interactions with certain substrate proteins are of sufficiently high affinity to facilitate their isolation via interaction cloning.

Amino Acid Sequence↗
PubMed1979

Clinical comparison of maphenide and silver sulphadiazine.

A series of 645 consecutive burn injuries are analysed. There were 175 patients in the control group, 156 in the Maphenide (Sulfamylon) group and 314 in the Silver Sulphadiazine (S. S. D.) group. The Maphenide group and S.S.D. group are compared statistically with the control group. S.S.D. proved superior in relation to clinical infection rate and culture rate in reduction of Pseudomonas and Staphylococcus. Other culture rates were analysed. There were significant reductions in both groups for E. coli and Candida albicans. Pneumonias were significantly increased in both groups and the mortality rate reduced with S.S.D. Overall S.S.D. gave better results than Maphenide.

Adolescent↗