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Biomedical subjects

E Fosslien

Publications and source records attributed to E Fosslien.

16 recordsLinked to original sources
PubMed1992

Quantitative alteration of some aortic intima proteins in fatty streaks and fibro-fatty lesions.

Proteins from grossly and histologically normal human aortic intimas and human aortic intima with fatty streaks or fibro-fatty lesions were extracted with 9 M urea mixture. Protein extracts were mixed with an internal absorbance calibrator (carbonic anhydrase) and subsequently separated by two-dimensional gel electrophoresis, silver stained, and quantitated by a laser beam densitometer. The vascular-origin proteins actin, tropomyosin-like proteins, tubulin, glycoprotein G35, and two myosin light chains were present in the highest amounts in normal aortic intima (27-year-old male). Quantitation of vascular-origin proteins in aortic intima with a fibro-fatty lesion from the same subject showed a slight decrease in relative amount of these proteins as compared to the normal intima. Several polypeptides (P15, P18, P60, P110b) and plasma-derived proteins not observed in the normal intima were found in fibro-fatty lesion (albumin, haptoglobin beta-chain, fibrinogen beta-chain, alpha 1-HS-glycoprotein). Other proteins which were present in very low amounts in the normal intima (transferrin, alpha 1-antitrypsin, apolipoprotein A-1, P56, P190) were found to be major proteins of intima with fibro-fatty lesion. Differences in relative amount of plasma-derived and vascular-origin proteins between normal intima and intima with fatty streaks, studied in a large number of specimens from 38 thoracic intimas and 18 paired abdominal intimas (16-34 years old) were less prominent. Statistically significant increases of the albumin/actin ratio were found in fatty streaks as compared to paired normal intimas as well as in the mean value of albumin/actin ratio in the group of fibro-fatty lesions (mean = 6.1) as compared to the group of fatty streaks (mean = 1.7) or normal intima (mean = 0.7). Several lesion unique proteins were observed; however, the frequency of the occurrence of these proteins in 41 specimens with lesion was low. No significant differences were observed in intima protein pattern and quantities of selected intima proteins between paired thoracic and abdominal aortas.

Actins↗
PubMed1988

Long-term oral ciprofloxacin: experience in the treatment of incurable infective endocarditis.

Acute septic infective endocarditis caused by Pseudomonas aeruginosa, in two patients with conditions that made it incurable, was treated with long-term orally administered ciprofloxacin. Bacteremia and symptoms cleared, resulting in subjective well-being without cure for three and one half and 22 months, respectively. Large amounts of ciprofloxacin, 150 and 1,440 g, respectively, were given continuously without apparent adverse reactions. Blood isolates of P. aeruginosa after treatment had limited progression of resistance to ciprofloxacin. Use of orally administered ciprofloxacin provides new opportunities for the long-term treatment of serious infections with restricted risk of bacterial drug resistance and no appreciable side effects.

Administration, Oral↗
PubMed1987

Effect of menstrual cycle on protein expression in human uterine leiomyomas.

Tissue proteins in paired samples of uterine leiomyomas and normal myometria from 26 patients were compared after extraction with 9 M urea, separation by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE), and visualization by silver staining. A creatine kinase carbamylation train and a rat heart extract were used as internal standards for the relative charge and the relative molecular weight (Mr) scales, respectively. Two groups of four proteins each, a first group of Mr = 34,500 (34K) and relative charge of creatine kinase of -14 to -21(P34a-d) and a second group of Mr = 56,000 (56K) and relative charge of creatine kinase less than -23(P56a-d), were more frequently expressed in uterine leiomyoma tissue than in normal myometrial tissue: P34, 14 of 26 (53.8%) in tumors and zero of 26 (0%) in normal myometria; P56a&d, 17 of 26 (65.3%); P56b&c, 20 of 26 (76.9%) in tumors and P56a&d, zero of 26 (0%); and P56b&c, 12 of 26 (46.1%) in normal myometria. Both P34 and P56 were expressed more frequently in the uterine leiomyoma during the proliferative phase than during the nonproliferative phase (P34 in proliferative phase: 12 of 13, 92.3%; and in nonproliferative phase: two of 13, 15.3%; P56a-d in proliferative phase: 13 of 13, 100%; and in nonproliferative phase: P56a&d, four of 13, 30.7%, and P56b&c, seven of 13, 53.8%). The cyclic expression of P34 and P56 suggests that their synthesis is related to the intrinsic hormonal environment of the tumors.

Adult↗
PubMed1986

Basic proteins in the human aortic intima: nonequilibrium two-dimensional electrophoretic analysis of tissue extracts.

The protein composition of atheroma-free human thoracic intima was compared with that containing fatty streaks or fibro-fatty lesions utilizing two-dimensional gel electrophoresis (2-DE) and silver staining. Intimal proteins extracted with 9 M urea were separated by nonequilibrium pH gradient electrophoresis (NEPHGE) followed by polyacrylamide gel electrophoresis (PAGE) in the second dimension. NEPHGE-PAGE of proteins extracted from atheroma-free intima revealed several major proteins: actin, tropomyosin-like proteins, proteins with relative molecular weight (Mr) of 250,000 (P250), two proteins with Mr about 15,000 (P15a, P15b), and many medium proteins such as a myosin heavy chain, two myosin light chains, and proteins P47, P44, P32, P27, P20a, P20b, P19a, P19b. Several additional proteins were observed in intimas with fatty streaks and fibro-fatty lesions. Most of them, such as albumin, transferrin, Apo A-I, alpha 1-antitrypsin, fibrinogen beta-chain, IgG, appear to originate from plasma. Differences in protein composition of intima with fibro-fatty streaks compared with adjacent lesion-free intima varied from case to case and need further study. NEPHGE-PAGE in combination with isoelectric focusing (ISO)-PAGE revealed more intimal proteins in atheroma-free and diseased aortas than either method alone, proteins which might be quantitated, isolated for binding studies, and further evaluated for their potential role in atherogenesis.

Actins↗
PubMed1986

Human aortic intima protein composition during initial stages of atherogenesis.

Protein extracted from 24 human aortic intimas (6-33 years old) with 9 M urea mixture, were studied after separation by two-dimensional gel electrophoresis (2-DE) and silver staining. The protein composition of normal intima in 4 cases, each without any gross changes in the thoracic aorta, displayed similarity. In each 2-DE protein pattern of these intimas about 150 polypeptide spots were detectable/mg of wet tissue. Major and medium polypeptides were described by relative molecular weight Mr in kilodaltons (kDa) and relative charge Cr. Major proteins found were actin (P44-18; Mr = 44 kDa; Cr = -18), tropomyosin-like proteins (P34-29, P35-28.5, P36-31) and two glycoproteins (G35-21, G35-23.5). Several new major and medium extracellular proteins were demonstrated in fibro-fatty lesions as well as in the lesion-free intimas adjacent to lesion in 3 cases. Many of these proteins appeared to originate from plasma: albumin, IgG, alpha 1-antitrypsin, transferrin, haptoglobin beta-chain, apo A-I, apo A-II, fibrinogen beta-chain, alpha 2-HS glycoprotein and alpha 1-antichymotrypsin. Visual comparison of intimal protein patterns from 17 different cases with varying degree of fatty streaks in the thoracic aorta, showed variability in 2 polypeptides P32-17.8 and P32-19.8 as well as 4 plasma proteins albumin, alpha 1-antitrypsin, transferrin and apo A-I. This study suggests that changes in protein composition may occur in the human aortic intima during the initial histological stages of atherogenesis providing potentially useful markers for their identification and pathophysiological evaluation.

Adolescent↗
PubMed1985

Effect of aging on human aortic protein composition. I. One-dimensional polyacrylamide gel electrophoretic analysis of tissue extracts.

Proteins extracted from matching areas of homogenized intimas of 17 human aortas, from two age groups (15-34 and 35-82), were studied after separation by polyacrylamide gel electrophoresis, silver staining, and densitometric scanning. Several definite protein bands including 6 major and 16 minor bands were identified in 17 aortic intima samples grossly and microscopically lesion free. However, such electrophoretic patterns were found to differ in the two age groups studied. For instance, (1) the integrated densities (amounts) of protein bands 1, 6, 13, 16, and 19 which we interpreted as of mural vascular origin were significantly higher in the younger age group, whereas the amounts of bands 2, 7, 9, 11, and 21 suspected to be of plasma origin were found to be significantly higher in the older age group; (2) protein band No. 8 was found to be double in the younger age group vs a single line in the older age group, whereas band No. 12 was the opposite. These changes in protein composition appear to correlate closely with diffuse intimal thickening found histologically in older age group, and will be further studied to relate to those in atherosclerotic lesions.

Adolescent↗
PubMed1985

Effect of aging on human aortic protein composition. II. Two-dimensional polyacrylamide gel electrophoretic analysis.

Arterial intima proteins were extracted by 9 M urea from matching histologically atheroma-free areas of 27 human thoracic aortas of both sexes from younger (15-34) and older (35-82) age groups and studied after separation by high-resolution two-dimensional polyacrylamide gel electrophoresis. Seventeen specific protein groups on each gel were identified according to their relative charges and molecular weights and their distribution in the two age groups compared. Some plasma-derived proteins occurred rarely in young aortas while they were consistently found in those from older cases, i.e., protein group 4 (alpha 1-antichymotrypsin) 1/13 (8%) vs 12/14 (86%), group 7 (haptoglobin beta-chain) 1/13 (8%) vs 13/14 (93%) and groups 6 and 9 (IgG chains) 3/13 (23%) vs 9/14 (64%), respectively. Other plasma-derived proteins such as group 3 (albumin) and 5 (alpha 1-antitrypsin) were identified in all samples of both age groups but their expression in the aortic intima increased with age. Proteins which are typically found intracellularly such as those from groups 11 (actin), 12 (cytoskeleton proteins), and 13 (tropomyosin-like proteins) appeared in samples of intima of both age groups but were less apparent in older specimens. These studies suggest that the changes in aortic intima protein distribution in the absence of atherosclerosis closely correlate with histological changes such as intimal thickening often found with aging, providing new sensitive markers of vascular senescence.

Adolescent↗
PubMed1984

Tissue proteins in breast cancer, as studied by use of two-dimensional electrophoresis.

Proteins from 25 specimens of malignant breast tissue were separated by "high-resolution" two-dimensional gel electrophoresis. The number of polypeptide spots detectable in individual gels varied from 259 to 471 (mean 347; SD 68) per milligram of wet tissue. Many polypeptide spots were not consistently present in all malignant tissues. Ten different in vivo polypeptides, observed neither in five non-malignant breast tissues nor in human milk, were present in more than 22 of the 25 cases of breast tumor tissues examined. Five of these polypeptides appeared to be identical to five in vitro polypeptides found in separations from cultured human ductal carcinoma cells. Further studies are required to verify the specificity of these tumor-associated proteins before they can be considered for breast tumor-specific in vitro diagnostic testing or targeting in selective in vivo anti-cancer therapy.

Adult↗
PubMed1977

Automated zone electrophoresis--experiments and new concepts.

I have investigated various modalities of automation of zone electrophoresis. One system has already been previously described (U.S. Pat. No. 3,896,021). Other systems investigated can be divided into batch systems and one random-access system; the former involve separation on cellulose acetate that is supported on 0.127 mm thick polyester (Mylar) film in the form of tape, cards, or discs. Systems in which the separation is in a direction transverse to the long axis of the tape use a typical tape width of 7.5 cm; systems in which separation is longitudinal make use of supports of various widths, depending upon the assay rate desired. Concepts were also developed for a random-access systems for automated electrophoresis, which requires no start-up time. Small Lucite cassettes are used, one for each sample. Each cassette has one surface of either cellulose acetate or any of several gels used for electrophoretic separation. There are further small wells for sample and calibrator. The loaded cassette is inserted into an input queue that allows serial processing. The cassettes move sequentially through prewetting (if needed), sample application, electrophoretic separation, staining, and scanning. This system should also be suitable for automated isoelectric focusing.

Automation↗
PubMed1970

Automatic lipid extraction and thin-layer chromatography application with a prgrammed flow system.

An eight-channel programmed flow system for automatic lipid extraction and TLC application is described. Each channel has a container for lipid extraction connected by Acidflex tubing through an AutoAnalyzer pump to a TLC applicator needle. Extraction containers are prepared from disposable Oxford sampler pipet tips by inserting a small cotton filter into their lower, narrower end, which is connected to the pump tubing. The applicator needles are supported vertically in a manifold, and their tips rest on a TLC plate placed on a hot plate. Serum is added to isopropanol in each extraction container, and proteins are completely precipitated in 2 min and retained in the extraction chambers by the cotton filters; lipid extracts are then transferred on to the heated TLC plate by intermittent pumping at a rate allowing for continuous evaporation of isopropanol under streams of warmed air or nitrogen. The lipids accumulate on the plate in eight small spots, one for each channel. Solvent is proportionally added into the extraction chambers from a common reservoir through Acidflex tubing in a second AutoAnalyzer pump. During the extraction procedure, both pump motors are automatically operated by a programmed timer with a solid-state switch. Of several different solvents tested, isopropanol is the fastest for protein precipitation and lipid extraction and does not extract substances from the Acidflex tubing which interfere with chromatographic separation.

1-Propanol↗