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Biomedical subjects

H H Rasmussen

Publications and source records attributed to H H Rasmussen.

At least 109 records · Page 6Linked to original sources
PubMed1990

[Referral to a department of medical gastroenterology. A study of the content of the referral letter and the reasons for referral].

Knowledge concerning factors that affect referrals of patients by general practitioners to hospitals is important in view of optimal utilization of the resources. Out of 108 referrals from general practitioners to a medical department of gastroenterology, information about the medical history was insufficient in about half the cases, and in 3/4 of the cases information about medicine was absent. Information about allergy and social conditions was found in only a few cases. The reason for referral was in most cases to establish a diagnosis and treatment. It is concluded, that if functions in a medical department of gastroenterology are to be moved to the general practitioners, more education in diagnostic procedures and treatment is needed. Further investigations are needed to solve these problems.

Denmark↗
PubMed1990

A two-dimensional gel protein database of noncultured total normal human epidermal keratinocytes: identification of proteins strongly up-regulated in psoriatic epidermis.

A two-dimensional (2-D) gel database of proteins from noncultured total normal human epidermal keratinocytes has been established. A total of 1449 [35S]methionine labelled proteins (1112 isoelectric focusing, 337 nonequilibrium pH gradient electrophoresis) were resolved and recorded using computer assisted (PDQ-SCAN and PDQUEST software) 2-D gel electrophoresis. By matching the protein patterns of total keratinocytes and transformed human amnion cells (master database; Celis et al., Leukemia 1988, 2, 561-602) as well as by 2-D immunoblotting and microsequencing of keratinocyte proteins, it was possible to identify 72 polypeptides in the keratinocyte database. The database also includes data on polypeptides that are synthesized at a higher level by keratinocytes enriched in basal cells, and on six secreted proteins which are produced, albeit at a reduced rate, by normal keratinocytes and that are strongly up-regulated in psoriatic epidermis (Celis et al., FEBS Letters, in press).

Electrophoresis, Gel, Two-Dimensional↗
PubMed1990

Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes.

We have used two-dimensional gel electrophoresis as a general "preparative" method to purify proteins for microsequencing analysis. In the first experiments, proteins derived from a total extract of Nicotiana tabacum leaf tissue were directly blotted from the gel onto poly(4-vinyl-N-methylpyridinium iodide)-coated glass fiber sheets. The major spots were excised and subjected to NH2-terminal sequence analysis, which made it possible to identify five of the eight selected proteins, while two more were recognized by generated internal sequences. In a second set of experiments, proteins of human origin were separated on multiple two-dimensional gels and the Coomassie Brilliant Blue-stained spots were excised from the gels. The combined spots were re-eluted and concentrated in a new gel and blotted on Immobilon. They were fragmented by in situ proteolysis and the generated peptides were separated by reverse phase-high performance liquid chromatography and sequenced. At the average, the internal sequences that were obtained covered 35 residues per protein and allowed unambiguous identification of 13 of the 23 proteins analyzed so far. The sequence information obtained of the unidentified proteins is sufficient for further cloning. These results demonstrate that systematic sequence analysis of the major proteins seen in two-dimensional gels is within the reach of current technologies. This offers a unique opportunity to link information contained in protein databases with known or forthcoming DNA sequence data.

Amino Acid Sequence↗
PubMed1990

Comprehensive two-dimensional gel protein databases offer a global approach to the analysis of human cells: the transformed amnion cells (AMA) master database and its link to genome DNA sequence data.

A total of 3430 polypeptides (2592 cellular; 838 secreted) from transformed human amnion cells (AMA) labeled with [35S]methionine were separated and recorded using computer-aided two-dimensional (2-D) gel electrophoresis. A master 2-D gel database of cellular protein information that includes both qualitative and quantitative annotations has been established. The protein numbers in this database differ from those reported in an earlier version (Celis et al. Leukemia 1988, 2,561-602) as a result of changes in the scanning hardware. The reported information includes: percentage of total radioactivity recovered from the gels (based on quantitations of polypeptides labeled with a mixture of 16 14C-amino acids), protein name (including credit to investigators that aided identification), antibody against protein, cellular localization, (nuclear, 40S hnRNP, 20S snRNP U5, proteasomes, endoplasmic reticulum, mitochondria, Golgi, ribosomes, intermediate filaments, microfilaments and microtubules), levels in fetal human tissues, partial protein sequences (containing information on 48 human proteins microsequenced so far), cell cycle-regulated proteins, proteins sensitive to interferons alpha, beta, and gamma, heat shock proteins, annexins and phosphorylated proteins. The results presented should be considered as the initial phase of a joint effort between our laboratories to undertake a general and systematic analysis of human proteins. Using this integrated approach it will be possible to identify phenotype-specific proteins, to microsequence them and store the information in the database, to identify the corresponding genes, to search for homology with previously characterized proteins and to study the function of groups of proteins (pathways, organelles, etc.) that exhibit interesting regulatory properties. In particular, the 2-D gel protein database may become increasingly important in view of the concerted effort to map and sequence the entire human genome.

Amnion↗
PubMed1990

The MRC-5 human embryonal lung fibroblast two-dimensional gel cellular protein database: quantitative identification of polypeptides whose relative abundance differs between quiescent, proliferating and SV40 transformed cells.

A new version of the MRC-5 two-dimensional gel cellular protein database (Celis et al., Electrophoresis 1989, 10, 76-115) is presented. Gels were scanned with a Molecular Dynamics laser scanner and processed by the PDQUEST II software. A total of 1895 [35S]methionine-labeled cellular polypeptides (1323 with isoelectric focusing and 572 with nonequilibrium pH gradient electrophoresis) are recorded in this database, containing quantitative and qualitative data on the relative abundance of cellular proteins synthesized by quiescent, proliferating and SV40 transformed MRC-5 fibroblasts. Of the 592 proteins quantitated so far, the levels of 138 were up- or down-regulated (51 and 87, respectively) by two times or more in the transformed cells as compared to their normal proliferating counterparts, while only 14 behaved similarly in quiescent cells. Seven MRC-5 SV40 proteins, including plastin and two interferon-induced proteins, were not detected in the master MRC-5 images. The identity of 36 of the transformation-sensitive proteins whose levels are up or down regulated by two times or more was determined and additional information can be transferred from the master transformed human epithelial amnion cells (AMA) database (Celis et al., Electrophoresis 1990, 11, 989-1071) for those polypeptides of known and unknown identity that have been matched to AMA polypeptides. As more information is gathered in this and other laboratories, including data on oncogene proteins and transcription factors, this comprehensive database will outline an integrated picture of the expression levels and properties of the thousands of protein components of organelles, pathways and cytoskeletal systems that may be directly or indirectly involved in properties associated with the transformed state.

Cell Transformation, Viral↗
PubMed1990

Measurement of gastrointestinal pH and regional transit times in normal children.

Gastrointestinal pH and regional intestinal transit times of a capsule were measured in twelve healthy children aged 8-14 years using a radiotransmitting pH-sensitive capsule. The location of the capsule was determined by fluoroscopy. pH in the stomach was 1.5, but rose to 6.4 in the duodenum (mean values). pH gradually rose in the small intestine and reached an alkaline peak value of 7.4 in the distal part. pH dropped to 5.9 in the cecum but rose to 6.5 in the rectum. Median gastric residence time of the capsule was 1.1 h. Small intestinal transit time was 7.5 h, and colonic transit time was 17.2 h. pH profile and intestinal transit times found in the present study are almost identical to values found in studies on healthy adults. It is therefore concluded that the release pattern of pH-dependent sustained-release tablets in children is likely to be equal to that of adults.

Adolescent↗
PubMed1990

Gastrointestinal pH and transit times in healthy subjects with ileostomy.

Gastrointestinal pH in 11 healthy subjects with ileostomy was determined with a pH-sensitive, radiotransmitting capsule. Median pH was 7.0 in duodenum, dropped to pH 6.3 in the proximal part, but rose to 7.3 in the distal part of the small intestine. In five subjects the pH of the ileostomy effluents was determined with the pH capsule as well as with a pH meter. Median pH was 7.2 measured with the capsule and 7.4 with the pH meter. The difference between the results obtained with the two methods ranged from 0.1 to 0.3 pH units. The median gastrointestinal transit time of the capsule was 10.5 h (range 6.2-12.8 h). Gastric residence time was 0.6 h (range 0.2-3.8 h), and small intestinal transit time was 10.3 h (range 5.6-11.9 h). Thus the small intestinal transit time in ileostomates is slightly increased compared with values reported from studies on subjects with intact gut. However, no statistically significant correlation was found between the small intestinal transit time and the time elapsed after the creation of the ileostomy. We conclude that colectomy does not alter small intestinal pH but seems to increase the small intestinal transit time of single units.

Adult↗
PubMed1990

Two stable levels of diastolic potential at physiological K+ concentrations in human ventricular myocardial cells.

Cells in many specimens of human ventricle can exhibit either of two stable levels of diastolic potential (DP) when exposed to 4 mM K+ in vitro (i.e., -78 +/- 4 mV or -45 +/- 5 mV, mean +/- SEM). In this report we show that the DP of some partially depolarized human ventricular cells developed a sustained 25-35 mV hyperpolarization (n = 28) when bath K+ concentration (K+b) was raised from 4 to 7 mM. On return of K+b to 4 mM, the DP of most, but not all, of these cells returned to the original depolarized levels. In other cells, the transition between the two levels of DP occurred at variable K+b ranging from 1 to 20 mM. We investigated the ionic mechanism(s) underlying the shifts between the two levels of potential by studying the K+ dependence of the DP in partially depolarized cells in 22 specimens of human ventricle. DP hyperpolarized an average of 25.6 mV (from -44.4 +/- 1.3 to -70.0 +/- 1.3 mV; n = 25) when K+b was increased from 4 to 7 mM. Intracellular K+ activity, determined by K+-selective microelectrodes, was within the range of normal reported for other mammalian species (106.7 +/- 4.4 mM in 4 mM K+; n = 22) and was unaffected by increasing K+b to 7 mM (111.7 +/- 6.6 mM; n = 6). Ba2+ (0.05 mM), a blocker of the inward rectifying K+ current, reversibly prevented the hyperpolarization, whereas acetylstrophanthidin (9 microM) failed to inhibit it. These results suggest that the hyperpolarization was due to a K+-dependent increase in K+ permeability and that electrogenic sodium pumping did not contribute significantly to the process. The ionic basis of the depolarization from a hyperpolarized level of DP also was investigated. Decreasing bath Na+ concentration and exposure to 30 microM tetrodotoxin did not prevent the depolarization. However, the depolarization could be inhibited by 2 mM Mn2+. These findings suggest that the depolarization may have been due to a Mn2+-sensitive inward current.

Diastole↗
PubMed1990

Inhibition of electrogenic Na(+)-pumping in isolated atrial tissue from patients treated with digoxin.

The effect on the cardiac sarcolemmal Na+,K(+)-pump of therapeutic concentrations of cardiac glycosides administered long-term to humans in a clinical setting is uncertain. We therefore examined Na+,K(+)-pump activity in atrial tissue from two groups of patients undergoing cardiac surgery. Fourteen patients received digoxin long-term until the time of surgery and 12 "controls" never received digoxin. The hyperpolarization produced by the electrogenic Na+,K(+)-pump in response to an increase in intracellular Na+ activity was utilized to evaluate Na+,K+)-pump activity. After excision from the patients, specimens of atrial tissue were Na(+)-loaded by cooling to 2-3 degrees C for 1 hr. They were then warmed to 30 degrees C in Tyrode's solution containing 20 mM K+. After warming the resting membrane potential of the tissues from both groups transiently hyperpolarized to levels more negative than the equilibrium potential for K+ (= approximately -50 mV in 20 mM K+) indicating that the hyperpolarization was the consequence of electrogenic Na(+(-pumping. The maximal hyperpolarization of the resting potential in tissue from patients receiving digoxin long-term (-58.4 +/- 1.9 mV, mean +/- S.D.) was significantly (P less than .01) less negative than that in tissue from patients in the control group (-69.9 +/- 2.2 mV). These data support the hypothesis that digoxin, administered therapeutically in the clinical setting, can inhibit the Na(+)-pump in human heart, and that during long-term administration of digoxin the inhibition can be sustained.

Digoxin↗
PubMed1989

[Tuberculosis in the aged population. Disease pattern, etiologic factors and preventive measures].

The incidence of tuberculosis is greatest among elderly individuals. The clinical features may be atypical, non-specific and may be confused with coexistent or age-related diseases. The risk factors predisposing to tuberculosis are related to underlying chronic or acute disease and malnutrition which disrupt integumental barriers, impair clearance mechanisms or compromise cellular responses to infecting agents. It is essential to provide optimal treatment of chronic disease, to avoid invasive procedures, to limit unnecessary medication and to ensure adequate nutrition.

Aged↗
PubMed1989

[A diet survey at a long-term care department].

Elderly patients are at risk of undernourishment during hospitalization. The quality of the diet can be further compromised by physical and mental disabilities. Investigation of the individual patient is necessary to find the patients at risk of under/malnutrition. For clinical use, a three-day dietary record with analyses of the food-composition provides a useful method. Individually suitable nutrition with dietary supplements and vitamins could be planned, and the food intake could be recorded regularly.

Aged↗
PubMed1989

Comprehensive, human cellular protein databases and their implication for the study of genome organization and function.

Comprehensive, computerized databases of cellular protein information derived from the analysis of two-dimensional gels, together with recently developed techniques to microsequence proteins offer a new dimension to the study of genome organization and function. In particular, human protein databases provide an ideal framework in which to focus the human genome sequencing effort.

Amino Acid Sequence↗
PubMed1989

Computerized, comprehensive databases of cellular and secreted proteins from normal human embryonic lung MRC-5 fibroblasts: identification of transformation and/or proliferation sensitive proteins.

Databases of protein information from human embryonal lung fibroblasts (MRC-5) have been established using computer analyzed two-dimensional gel electrophoresis. One thousand four hundred and eighty-two cellular proteins (1060 with isoelectric focusing and 422 with nonequilibrium pH gradient electrophoresis, in the first dimension) ranging in molecular mass between 8 and 234 kDa were separated and numbered. Information entered in the database (in most cases for major proteins) includes: protein name, HeLa protein catalog number, mouse protein catalog number, proteins matched in transformed human epithelial amnion cells (AMA) and peripheral blood mononuclear cells (PBMC), transformation and/or proliferation sensitive proteins, synthesis in quiescent cells, cell cycle regulated proteins, mitochondrial and heat shock proteins, cytoskeletal proteins and proteins whose synthesis is affected by interferons. Additional information entered for a few transformation-sensitive proteins that have been selected for future studies includes levels of synthesis and amounts in fetal human tissues. A total of four hundred and seventy-six [35S]methionine labeled polypeptides (258 isoelectric focusing; 218, nonequilibrium pH gradient electrophoresis) secreted by MRC-5 fibroblasts were separated and recorded (J. E. Celis et al., Leukemia 1987, 1, 707-717). Information entered in this database includes molecular weight and transformation sensitive proteins. These databases, as well as those of epithelial and lymphoid cell proteins (J. E. Celis et al., Leukemia 1988, 9, 561-601), represent the initial stages of a systematic effort to establish comprehensive databases of human protein information. In the long run, these databases are expected to offer a useful framework in which to focus the human genome sequencing effort.

Cell Line, Transformed↗
PubMed1989

pH-profile and regional transit times of the normal gut measured by a radiotelemetry device.

The pH of the gut lumen was measured in 39 healthy persons using a pH-sensitive, radiotransmitting capsule. Thirteen persons were studied twice. The location of the capsule was determined by X-ray. The pH rose from 6.4 in the duodenum to 7.3 in the distal part of the small intestine. In 17 persons the pH dropped by 0.1-0.8 pH units during the last hours of the small intestinal transit. The pH was 5.7 in the caecum, but rose to 6.6 in the rectum. Gastric residence time was 1.1 h, small intestinal transit was 8 h, and colonic transit time was 17.5 h (median values). The results provide a firmer basis for prediction of the level, and the rate of release of active substance from pH-dependent sustained-release oral preparations.

Adolescent↗
PubMed1989

Na+-dependent activation of Na+-K+ pump in human myocardium during recovery from acidosis.

In cardiac cells of some species, an intracellular Na+ load and enhanced electrogenic Na+ pumping can develop during recovery from acidosis. We examined whether this can also occur in human heart. Specimens of human right atrial appendage were incubated in cold (2 degrees C) NH4Cl-substituted (for NaCl) Tyrode solution and then transferred to warm (30 degrees C) Na+-Tyrode solution containing 20 mM K+ to induce an intracellular acid load. After transfer, resting membrane potential (Em) transiently hyperpolarized to a maximal level (Emax) of -58.6 +/- 1.3 mV (n = 8), a level significantly (P less than 0.001) more negative than the equilibrium potential for K+. Decreasing K+ conductance with 0.5 mM Ba2+ increased Emax to -74.0 +/- 2.7 mV (n = 6, P less than 0.001), indicating that the hyperpolarization was not due to efflux of NH+4 through K channels. Acetylstrophanthidin (0.5 microM) reduced Emax to -37.5 +/- 3.1 mV (n = 5, P less than 0.001), indicating that an increased level of Na+-K+ pump activity was involved in the hyperpolarization. The Na+-K+ pump-induced hyperpolarization was abolished (Emax = -22.6 +/- 1.6 mV, n = 8, P less than 0.001) by 10 microM 5-(N,N-dimethyl)amiloride and, when the extracellular Na+ concentration was reduced to 50 mM, by 50 mM Li+. These findings suggest that Na+-H+ exchange can produce a Na+ load which then can stimulate electrogenic Na+ pumping in human cardiac cells during recovery from acidosis.

Acidosis↗
PubMed1989

Inhibition of Na-K pump current in guinea pig ventricular myocytes by dihydroouabain occurs at high- and low-affinity sites.

Binding of cardiac glycosides to the Na+,K+-dependent ATPase has been shown to occur at both high- and low-affinity sites. However, recent reports suggest that glycoside-induced inhibition of electrogenic Na-K pump current occurs with simple first-order binding kinetics at relatively low-affinity sites. This implies that high-affinity binding sites have little to do with Na-K pump inhibition during exposure to cardiac glycosides. To better understand the role of the high-affinity site, we investigated the concentration dependence of Ipump inhibition by dihydroouabain (DHO) in guinea pig ventricular myocytes through use of wide-pore patch pipettes to "fix" internal Na+ activity at approximately 30 mM and to voltage clamp at -40 mV (T = 34 degrees C). DHO was found to have no effect on membrane conductance at a holding potential of -40 mV. Holding current was monitored and the difference between steady-state holding current before and during external exposure to nine concentrations (range, 0.01-1,000 microM) of DHO was measured and normalized to cellular membrane capacitance. The concentration dependence of the inhibition of Na-K pump current was biphasic and well fitted to a two-binding site model with inhibitory KD values of 0.05 microM and 64.5 microM. This is consistent with previously reported 3H-ouabain binding studies in guinea pig myocardium. These findings indicate that the electrogenic properties of the Na-K pump can be inhibited by glycoside binding to both high- and low-affinity sites.

Animals↗
PubMed1989

Depression and magnesium deficiency.

The psychiatric symptoms of magnesium deficiency are unspecific, ranging from apathy to psychosis, and may be attributed to other disease processes associated with poor intake, defect absorption, or excretion of magnesium. Serum magnesium should be determined when there are symptoms consistent with magnesium deficiency and/or in conditions which can lead to a deficiency, e.g., malabsorption, malnutrition, alcoholism and diuretic treatment. A low serum value suggests magnesium deficiency, but the diagnosis is reinforced with analyses of magnesium in the urine and a loading test with magnesium. Magnesium can be given orally or intramuscular/intravenously.

Aged↗