Biomedical subjects

L Camps

Publications and source records attributed to L Camps.

9 recordsLinked to original sources

PubMed1997

Effect of prenatal exposure to ethanol on intestinal development of rat fetuses.

BACKGROUND: Chronic alcoholism in pregnant animals and humans lead to general growth impairment in their offspring, which show multiple birth defects and delayed grown (fetal alcohol syndrome). Here we study the maturation of the intestine under the effect of chronic exposure to ethanol in utero together with associated malnutrition. METHODS: Lactase, acid beta-galactosidase, maltase, and alkaline phosphatase activity profiles were monitored in 18-, 19-, 20-, and 21-day-old fetuses from rats kept under three nutritional treatments before and during gestation: alcohol-treated (25% ethanol in drinking water), fiber-treated (50% cellulose-diluted diet) as a control of the malnutrition associated with chronic alcoholism, and control or normal diet. Serum corticosterone determination and lactase immunolocalization were carried out. To detect possible direct effects of ethanol during the period of mucosa development, intestinal explants from 18-, 19-, and 20-day-old control fetuses were cultured either in the basal medium alone or in a medium containing 25 mM ethanol for 72, 48, and 24 h of incubation, respectively. RESULTS: Following chronic ethanol exposure in utero, intestinal weight and brush-border protein content and the specific activities of lactase, acid beta-galactosidase, maltase, and alkaline phosphatase were significantly lower than those of nutritional controls. Organ culture results, under the assay conditions stated, did not show a direct effect of ethanol 25 mM on prenatal mucosal functionality. CONCLUSIONS: All these results suggest that maternal malnutrition is not primarily responsible for the impaired intestinal maturation in rat fetuses from alcohol-treated mothers; indirect effects of ethanol and/or its derivatives throughout embryo-fetal development could be necessary to promote this intestinal delay.

Alcoholism↗

PubMed1995

Liver alcohol dehydrogenase activity and ethanol levels during chronic ethanol intake in pregnant rats and their offspring.

The effects of chronic alcohol intake on the ethanol levels in body fluids (blood, amniotic fluid, and fetal intragastric content), hepatic alcohol dehydrogenase (ADH) activity, isoenzyme distribution, and hepatic zinc levels were studied in pregnant rats at term (19 and 21 days), in their offspring at fetal, perinatal, and weaned stages, and in adult virgin rats. Three experimental groups were studied: 1) the alcohol group received ethanol in drinking water (from 10% to 25% over 2 months), 2) the fibre diet group was undernourished on a hypocaloric diet, to assess the effects of malnutrition associated with chronic alcohol intake, and 3) the control group received no alcohol and normal diet. A gradient of increasing ethanol concentrations was found in fetal blood, amniotic fluid, and fetal intragastric contents with respect to maternal blood. A decrease in ADH activity was found in alcohol-consuming pregnant rats compared to controls. This was related neither to liver ADH isoenzyme distribution nor to changes in hepatic zinc levels. Chronic alcohol consumption in pregnant rats produced high ethanol accumulation in fetal fluids and changes in the liver ADH activity depending on the physiological situation (pregnancy, development, virgin state).

Alcohol Dehydrogenase↗

PubMed1991

Lipoprotein lipase in lungs, spleen, and liver: synthesis and distribution.

Lipoprotein lipase (LPL, E C 3.1.1.34) is the enzyme responsible for hydrolysis of triacylglycerols in plasma lipoproteins, making the fatty acids available for use by subjacent tissues. LPL is functional at the surface of endothelial cells, but it is not clear which cells synthesize the enzyme and what its distribution within tissues and vessels is. In previous studies we reported that in the major LPL-producing tissues (muscles, adipose tissue, and mammary gland) the enzyme is made by the major cell types. In the present work we have studied in adult guinea pigs some tissues that present LPL activity but in lower amounts (lung, spleen, and liver). On cryosections of these tissues we have searched for specific cell expression of the LPL gene (by in situ hybridization using a RNA probe) and for the corresponding protein distribution (by immunocytochemistry). Based on morphological criteria we can suggest that, contrary to the main LPL-producing tissues, in these tissues the enzyme is made by scattered cells, such as macrophages in the lung and spleen and Kupffer cells in the liver; endothelial cells present but do not synthesize the enzyme, indicating that the endothelial LPL originates in other cells. In the liver strong immunoreaction was detected in the sinusoid in contrast to the low level of mRNA expression, suggesting that liver takes up circulating LPL from blood.

Animals↗

PubMed1990

Localization of lipoprotein lipase to discrete areas of the guinea pig brain.

Lipoprotein lipase is a key enzyme in lipoprotein metabolism present primarily in extrahepatic tissues with high turnover of fatty acids. Using immunocytochemistry we have explored where lipoprotein lipase is localized in guinea pig brain. The enzyme was found to be associated with neuronal cells and vascular endothelial surfaces. The distribution was strikingly uneven with intense reaction in some areas, and virtually no reaction in adjacent areas. The highest reactivity was in neocortex, in hippocampus, in Purkinje cells of the cerebellum and in some motor nuclei of the brainstem. The results suggest marked differences between individual brain areas in utilization of plasma lipoproteins.

Animals↗

PubMed1990

Lipoprotein lipase: cellular origin and functional distribution.

Lipoprotein lipase (LPL, E.C. 3.3.1.34) is the enzyme responsible for hydrolysis of triacylglycerols in plasma lipoproteins, making the fatty acids available for use by subjacent tissues. LPL is functional at the surface of endothelial cells, but it is not clear which cells synthesize the enzyme and what its distribution is within tissues and vessels. We have searched for specific cell expression of the LPL gene by in situ hybridization using a RNA probe and for the corresponding protein distribution by immunocytochemistry on cryosections of some LPL-producing tissues of guinea pigs. In white and brown adipose tissues, heart and skeletal muscle, and lactating mammary gland, there was positive hybridization for LPL mRNA over all members of the major cell types, indicating that mature and immature adipocytes, muscle cells, and mammary epithelial cells are main sources of LPL. In large vessels, LPL expression was detected in some smooth muscle cells in the media layer. There was no positive hybridization for LPL mRNA over endothelial cells in any of the tissues studied, but there was immunoreaction for LPL protein at endothelial surfaces of all blood vessels. In the kidney, there was strong immunofluorescence at the vascular endothelium, particularly in the glomeruli, but little or no LPL mRNA was detected in the surrounding cells. These observations suggest that in some tissues LPL is synthesized by parenchymal cells and spreads along the vascular mesh. Transfer to the vascular endothelium is, however, not the only route taken by LPL. In the mammary gland most of the enzyme protein appeared to be secreted, partly in association with milk fat droplets.(ABSTRACT TRUNCATED AT 250 WORDS)

Adipose Tissue↗

PubMed1989

Histopathological features of unilateral stapling in animal experiments.

Blount stapling of the proximal medial tibial growth was performed in 10-week-old domestic pigs. A total of 37 animals for up to 17 weeks were followed up. The histological evaluation showed a different reaction of the growth plate in the medial (stapled), central and lateral area. Up to 6 days after stapling the morphological features were characterized by deviations of the cell column from the axial alignment. Herniations of mature chondrocytes as well as isles of epiphyseal cartilage splintered into the adjacent metaphyseal cancellous bone were seen. From the 10th to the 11th postoperative day on there was a decline in the number of distal hypertrophic and degenerating cartilage cells due to impaired proliferation. Cell atrophy due to disturbed maturation or cell degeneration was evident. Local clusters of chondrocytes with loss of columnar arrangement indicated impaired chondrogenesis. Twenty-eight days after the operation coarser structures and changed alignment of cancellous bone characterized the morphological picture. The postoperative follow-up showed epiphyseal plates bounded by mature bone blocks or even a distinct sheet of horizontally oriented bone plates on the metaphyseal side. Many metaphyseal findings, such as augmented hypertrophic cells in the early postoperative period, or platelike limitations of the epiphyseal plate complete the morphological picture.

Animals↗

PubMed1989

Metaphyseal aspects of stapling. An experimental study in pigs.

Blount stapling of the growth plate induced changes in the metaphyseal architecture, which progressed in correlation to the postoperative follow-up. The stereological investigations revealed a subtile reaction of the medial stapled tibial plate in a total of 37 domestic pigs (10 weeks old) during the postoperative follow-up (up to 17 weeks). Zone 1, 380-1120 microns distal to the plate representing "bone modelling", and zone 2, 1180-2360 microns distally representing "bone remodelling", were investigated separately. The findings in zone 2 were very similar to zone 1 but were less extensive. The parameter most sensitive to stapling was the surface density; the trabecular distance showed parallel but less impressive findings. The specific surface and trabecular diameter changed with some delay. The last parameter to change was the volume density.

Animals↗

PubMedDate not supplied

[Morphological, morphometric and stereological aspects of Blount's unilateral stapling of the growth plate in animal experiments].

Medial stapling of the proximal tibial growth plate in ten-week-old pigs effects in the first instance a local reaction of the growth plate being first limited to the region between the staple branches. From the 4th-5th postoperative day on, there is a significant decrease of the growth rate, the surface area of cells in the zone of opening cells, and of the surface density of the adjacent metaphyseal spongiosa. From the 10th-11th day after stapling a significant decrease in the height of the metaphyseal columns and the growth plate occurs in the medial compartment as well as a trabecular broadening of the metaphyseal spongiosa in the stapled area. Subsequently, the surface density of the metaphyseal spongiosa is significantly lower, the volume density significantly higher than the control values. With advancing postoperative interval the stapling effects involve the whole growth plate. However, the central and the lateral compartments show always less distinct findings. Unilateral stapling of the growth plate brings about a significant diminution of the radiologically determined length of the epiphysis, metaphysis and the total tibia as well as an evident broadening of the growth plate.

Animals↗

PubMedDate not supplied

Expression of lipoprotein lipase in ovaries of the guinea pig.

Guinea pig ovaries were found to have significant lipoprotein lipase (LPL) activity, corresponding to almost one-tenth the activity in paraovarian adipose tissue and in heart per gram of tissue. Northern blot analysis demonstrated the same three species of LPL mRNA in ovaries (1.8, 3.1, and 3.5 kb) as in adipose tissue. In situ hybridization showed LPL mRNA in cells of the follicular wall, and in granulosa and theca lutein cells of the mature corpus luteum. By immunolocalization, LPL was visualized in the vascular endothelium throughout the ovary, but with highest concentration in the endothelium of capillaries and large vessels of the cortical region and capillaries in the stroma of the corpus luteum. These results suggest that in the guinea pig LPL may have a function for the delivery of lipids from lipoproteins to ovarian cells.

Adipose Tissue↗