Diabetes education project: community networking in rural Utah.

People in rural areas often lack the financial resources, workforce, and professional network needed to sustain a diabetes education pro gram in their own community. HealthInsight, a nonprofit organization that works to improve the quality of health care in its community, developed a 2-day seminar in an effort to facilitate the networking of rural health professionals who educate patients with diabetes and to help those educators better learn how to use existing resources. Participants included nurses, dietitians, diabetes educators, quality managers, and education directors from hospitals and home health agencies in both rural and metropolitan areas. Speakers presented information on a variety of topics related to program development, and a resource manual containing numerous materials was given to each participant. At the end of the seminar, the group turned in goals for their own programs. Too often, providers of health care compete rather than collaborate with one another. There is a great need for such networking opportunities among health care professionals working on common goals--especially in rural areas.

Characterization of salt-soluble forms of acetylcholinesterase from bovine brain.

The hydrophilic, salt-soluble (SS) form of acetylcholinesterase (AChE) from bovine brain caudate nucleus exists mainly as a tetramer sedimenting at 10.3S (approximately 40%), and a monomer sedimenting at 3.4S (approximately 60%). The enzyme is N-glycosylated and contains similar HNK-1 carbohydrates as detergent-soluble (DS) AChE. No O-linked carbohydrates could be detected. Amino acid sequencing showed that the N terminus of SS-AChE is identical to that of DS-AChE. In tetrameric SS-AChE, two pairs of disulfide-linked dimers are associated by hydrophobic forces located in the C terminus. Antibodies were raised against a peptide identical to the last 10 amino acid residues of bovine brain DS-AChE. The peptide included the sequence of residues 574-583 (H-Tyr-Ser-Lys-Gln-Asp-Arg-Cys-Ser- Asp-Leu-OH) of the enzyme. The antibodies cross-reacted with tetrameric, but not with monomeric, SS-AChE, showing that in the latter form, the C terminus is truncated. Limited proteolysis of tetrameric SS-AChE at the C terminus led to the formation of an enzymatically active monomer, which did not react with anti-C-terminal antibody. Although the DS form of AChE contains a structural subunit that serves as membrane anchor, no anchor was detected in SS-AChE. Enzyme antigen immunoassays showed that SS-AChE reacted with all monoclonal antibodies directed against the catalytic subunit of DS-AChE, but not with monoclonal antibodies targeting the membrane-anchored subunits. From our results, we conclude that SS-AChE utilizes the same alternative splicing pattern as DS-AChE, leading to tetrameric SS-AChE devoid of the membrane anchor.(ABSTRACT TRUNCATED AT 250 WORDS)

Monoclonal antibodies against brain acetylcholinesterases which recognize the subunits bearing the hydrophobic anchor.

Monoclonal antibodies were raised against amphiphilic detergent-soluble (DS) acetylcholinesterase (AChE) from human brain caudate nucleus. Three mAb, 132-4 (IgG1), 132-5 (IgG1) and 132-6 (IgG3), specific for brain DS-AChE were selected and subcloned. These mAb reacted with native as well as heat-denatured and SDS-denatured DS-AChE, indicating that the epitopes to which mAb bound are continuous determinants. The mAb cross-reacted with DS-AChE from bovine and mouse brain and with brain DS-AChE from river trout (Salmo trutta forma fario) and lake trout (Salmo trutta forma lacustris). No cross-reaction was detected with the following antigens: salt-soluble (SS) AChE from bovine brain, glycophospholipid-anchored AChE from human and bovine erythrocytes, DS-butyrylcholinesterase and SS-butyrylcholinesterase (BtChE) from the brains of human and bovine, DS-BtChE from chicken and BtChE from human serum. Deglycosylation of brain DS-AChE with N-glycosidase F did not abolish the binding of mAb to DS-AChE. After reduction of brain DS-AChE by dithiothreitol, the mAb no longer reacted with the antigen, indicating that a disulfide bridge is important for the epitope. Monomerization of brain DS-AChE by trypsin and limited proteinase K treatment also abolished the binding of mAb to DS-AChE. Sucrose-density-gradient centrifugation showed that mAb reacted only with native tetrameric forms, but not with dimeric and monomeric forms. Western blot, after SDS/PAGE under non-reducing conditions, showed that mAb reacted with those subunits carrying the hydrophobic anchor (i.e. tetramers, trimers and heavy dimers) but not with those devoid of it (light dimers or monomers). Since mAb 132-4, 132-5 and 132-6 recognized DS-AChE from fish up to mammalian brain in the evolutionary tree, it is concluded that the epitope to which these mAb bind, is conserved in nature.

Ratio of immunochemically determined amniotic fluid acetylcholinesterase to butyrylcholinesterase in the differential diagnosis of fetal abnormalities.

A total of 111 amniotic fluid samples, clear or blood stained, with elevated levels of alpha-fetoprotein and acetylcholinesterase was analysed by immunoassays specific for acetylcholinesterase and butyrylcholinesterase and the acetylcholinesterase/butyrylcholinesterase-ratios determined. Samples from 40 pregnancies associated with anencephaly, 47 pregnancies associated with open spina bifida or encephalocele and six pregnancies with fetal intrauterine death or miscarriage all had ratios of greater than 0.14. All 11 pregnancies with fetal ventral wall defects had ratios less than 0.14 as had four pregnancies with normal outcome and elevated levels of alpha-fetoprotein and acetylcholinesterase. Three fetuses with both open spina bifida and ventral wall defects were associated with ratios above 0.14. These results suggest that immunochemical determination of acetylcholinesterase and butyrylcholinesterase can be used to distinguish pregnancies complicated by anencephaly, open spina bifida, encephalocele and miscarriage from those with ventral wall defects and samples with false positive elevated levels of alpha-fetoprotein and acetylcholinesterase. The procedure is accurate and simple to carry out and well suited to routine use in a clinical chemistry laboratory.

Enzyme immunoassay of human cholinesterase (EC 3.1.1.8). Comparison of immunoreactive substance concentration with catalytic activity concentration in randomly selected serum samples from healthy individuals.

We developed an enzyme immunoassay (ELISA) for quantitation of plasma cholinesterase substance concentrations in native plasma or serum samples. The ELISA assay is based on polyclonal (rabbit) antihuman cholinesterase and a highly specific monoclonal (mouse) antibody, with a commercially available peroxidase-conjugated (rabbit) antibody directed against mouse immunoglobulins as the signal carrier. The detected serum cholinesterase substance concentrations (mean: 4.51 mg/l, SD: 0.90 mg/l) in randomly selected serum samples from 33 healthy individuals were closely and linearly related to the corresponding catalytic activity concentrations.

Amateur boxing in Denmark. The effect of some preventive measures.

A survey of all amateur boxing matches in Denmark was made during a 3 year period. Data was gathered on means by which bouts were ended by the referee or attending physician, such as knock outs or blows to the head. A total of 5272 matches were fought: 3240 were senior matches (over age 19) and 2032 were junior matches (ages 17 to 19). Prophylactic intervention--unlimited length of hand bandage, voluntary use of boxing helmets, and heavier gloves for boxers greater than 149 pounds--did not affect the frequency of matches being stopped because of knock outs or blows to the head.

[Idiopathic autoimmune haemolytic anaemia in dogs (author's transl)]. / Idiopatisk autoimmun haemolytisk anaemi hos hunde

Three cases of autoimmune hemolytic anemia in dogs are described. The description includes results of laboratory tests. All three cases were characterized by a short course of disease before the first "crisis". One of the dogs is still alive 2 years after the first crisis, having had one remission after 3 months. A second dog died five days after hospitalization (four days after initiation of medical treatment) whereas the third dog was killed one day after initiation of medical treatment because of rapidly developing weakness.