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W Matthew

Publications and source records attributed to W Matthew.

4 recordsLinked to original sources

Cross validation of USARIEM heat strain prediction models. U.S. ARMY Research Institute of Environmental Medicine.

HYPOTHESIS: This study was a cross validation of three heat strain prediction models developed at the U.S. Army Research Institute of Environmental Medicine: the ARIEM, HSDA, and ARIEM-EXP models ability to predict core temperature. METHODS: Seven heat-acclimated subjects completed twelve experimental tests, six in each of two hot climates, at three exercise intensities and two uniform configurations in each climate. RESULTS: Experimental results showed physiological responses as expected with heat strain increasing with work load and level of protective clothing, but with similar heat strain between the two environments matched for wet bulb, globe index. Neither the ARIEM or HSDA model closely predicted core temperatures over the course of the experiment, due mostly to an abrupt initial rise in core temperature in both models. A proportionality constant in the ARIEM-EXP buffered some of this abrupt rise. CONCLUSIONS: Comparisons of the core temperature and tolerance times data with the three models led to the conclusions that for healthy males: 1) the ARIEM and HSDA models provide conservative safety limits as a result of predicting rapid initial increases in core temperature; 2) the ARIEM-EXP most closely represents core temperature responses; 3) the ARIEM-EXP requires modifications with an alternate proportionality coefficient to increase accuracy for low metabolic cost exercise; 4) all of the models require additional input from existing research on tolerance to heat strain to better predict tolerance times; and 5) additional models should be examined to investigate the transient state of the body as it is affected by environment, clothing and exercise.

Acclimatization↗

Carbohydrate-electrolyte solutions during field training: an overview.

The rationale and methods of evaluating two carbohydrate-electrolyte solutions at a field training exercise in hot weather are presented in this overview. The carbohydrate-electrolyte solutions were formulated to produce a multipurpose replacement beverage which could satisfy diverse requirements of troops working in hot climates. Several uses of these beverages include replacement of electrolytes and fluid while in Mission Oriented Protective Posture IV, fluid replacement for mild heat casualties, and oral rehydration therapy for treatment of diarrheal losses.

Adult↗

Distribution and biochemical characterization of the INO antigen during chick neural crest cell migration.

The INO (inhibitor of neurite outgrowth) antibody recognizes a laminin-heparan sulfate proteoglycan complex and was isolated for its ability to functionally inhibit axonal outgrowth of peripheral neurons. Here, we examine the distribution and biochemical characteristics of INO in the early chick embryo. Because the INO antigen is sensitive to most classical fixation procedures and fixation leads to abundant nuclear staining, the antibody was directly injected into 1.5-2.5-day-old embryos prior to fixation. The distribution of the injected antibody was then observed in cryostat sections by indirect immunofluorescence. Particular attention was focussed upon regions of ongoing neural crest cell migration. The INO antigen was observed along both cranial and trunk neural crest cell migratory pathways. The antigen was seen around the basement membrane surrounding the neural tube and notochord, and underneath the ectoderm and endoderm. In addition, fibrillar staining was observed in the cranial mesenchyme and in both rostral and caudal halves of the somitic sclerotome in the trunk. The distribution pattern was identical to that previously observed for laminin or heparan sulfate proteoglycan. To confirm the nature of the INO antigen, we performed immunoprecipitations of chick embryos ranging from 1.5 to 9 days of incubation. Half of each sample was digested with heparinase prior to SDS-PAGE and silver staining. In material from young embryos, bands of 200 and 180 kD (probably corresponding to the B-chains of laminin) plus two broad smears of bands at 180-150 kD and 130-85 kD were observed without heparinase digestion. Following enzymatic digestion, the 200-kD and 180-kD bands remained, while the smears disappeared and were replaced by numerous low-molecular-weight bands. In contrast to preparations from young embryos, samples taken from embryos at day 3 or beyond did not enter the 8% gel without heparinase digestion, though the banding pattern appeared identical to younger samples after heparinase digestion in the presence or absence of Ca2+. This change in the INO antigen with age could result from an increase in the heparin-side-chains attached to similar core proteins, or from an increase in the stability of the laminin-heparan sulfate proteoglycan containing complex with time.

Animals↗