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Biomedical subjects

I Axelsson

Publications and source records attributed to I Axelsson.

At least 37 records · Page 2Linked to original sources
PubMed1994

Oral findings in a group of newborn Swedish children.

Oral examinations were performed of 1021 newborn Swedish children, of whom 101 were re-examined after 2-3 or 4-5 months. The most common findings, registered in 74.9% of the children, were of oral mucosal cysts situated either palatally or on the alveolar ridges. The majority of the palatal cysts disappeared shortly after birth, and some alveolar cysts appeared after birth. Ankyloglossia was found in 2.5% of the children, and Fordyce spots in 1.0%. No natal teeth were found. The upper labial frenum was attached to the crest of the alveolar ridge in 76.7% of the children, palatally in 16.7% and buccally in 6.7%. The relationship of the alveolar ridges was recorded: the anterior segment of the mandibular ridge was distal to the maxillary in 99% of cases, and, posteriorly, the mandibular ridges were lingual to the maxillary in 97.6%. An open bite was found in 39.8% of the children.

Female↗
PubMed1993

Visual functions in a Swedish population of dyslexic and normally reading children.

Eighty-six 9-year old dyslexic children were carefully matched to controls with regard to age, sex, class in school, and intelligence and thorough visual functions tests and eye examinations were performed. As a group the dyslexic pupils exhibited a lower distance as well as near visual acuity both with monocular and binocular viewing. Furthermore, the dyslexic pupils had a lower contrast sensitivity at the lower and higher spatial frequencies. These differences were all statistically significant. However, no statistically significant differences between the two groups could be observed regarding refractive errors or contrast sensitivity in the middle spatial frequency range. Although some eyes were amblyopic, any severe eye anomalies or diseases were not found in any of the investigated children.

Child↗
PubMed1991

Structure and composition of proteoglycans from human annulus fibrosus.

Proteoglycans were extracted from ground human lumbar annuli fibrosi with 4M guanidinium chloride and purified by means of associative equilibrium density gradient centrifugation. The proteoglycan preparations contained chondroitin sulphate, keratan sulphate and hyaluronic acid, but no dermatan sulphate. Degradation experiments suggested that the proteoglycans contain three regions: a chondroitin sulphate-rich region, a keratan sulphate-rich region and a region that binds to hyaluronic acid, thus allowing proteoglycan aggregates to be formed. The keratan sulphate-rich region seemed to be more prominent than in bovine hyaline cartilage proteoglycans. The model for the structure of bovine hyaline cartilage proteoglycans, Hascall and Heinegård, seems to be applicable to the proteoglycans from human annulus fibrosus. The amino acid composition of annulus fibrosus proteoglycans is very similar to that of bovine hyaline cartilage proteoglycans.

Animals↗
PubMed1990

Kinetics of proteoglycans and cells in growth plate of normal, diabetic, and malnourished rats.

The metabolism of proteoglycans in normal growth plate and the changes in growth plate morphology induced by diabetes and malnutrition were studied in rats. The proteoglycans had a significantly faster turnover (half-life measured with [35S]sulfate labeling: 25-30 h) than the cells in the growth plate. Morphometric studies showed significant reductions of cell number, zone height, and [3H]thymidine incorporation in growth plates from rats with untreated streptozotocin-induced diabetes compared to normal rats. Similar, although less pronounced alterations were observed in malnourished, nondiabetic rats. Disaggregation and degradation of proteoglycans are probably necessary prerequisites for calcification. Our data indicate that the proteoglycans are in a dynamic state of rapid biosynthesis and degradation throughout the growth plate with a shift in the balance at the calcification front toward less synthesis and more degradation.

Animals↗
PubMed1989

Macromolecular absorption in preterm and term infants.

Human alpha-lactalbumin (alpha-LA) has been used as a marker for measuring macromolecular absorption. The serum concentration of human alpha-LA after a human milk feed has been studied in 32 healthy very low birthweight infants (VLBW), fed human milk (gestational age 26-32 weeks) and in 56 term, breast-fed infants, age 3-140 days. At 31 weeks of gestation the serum concentration of human alpha-LA was more than 10 times higher (mean value 3,000 and median value 2,101 micrograms/l serum/l human milk/kg body weight, n = 11) than in the term infants aged 3-30 days (mean value 257 and median value 152, n = 29). The serum concentration of alpha-LA decreased with increasing maturity in the VLBW-infants. At a postconceptional age of 37 weeks the values were similar (mean value 200 and median value 99, n = 8) to those found for term infants during the first month. In the term infants a decreasing absorption of alpha-LA was found with increasing postnatal age.

Female↗
PubMed1988

Protein and energy intake during weaning. III. Effects on plasma amino acids.

Preprandial plasma amino acid concentrations were measured at 5 and 6 months of age in 30 healthy term infants who were either breast-fed ad libitum or fed one of two different formulas (1.9 g of protein per 100 ml with a whey:casein ratio of 50:50; 2.9 g of protein per 100 ml with a whey:casein ratio of 20:80) ad libitum, plus the same supplementary food regimen. The mean plasma concentrations of total amino acids and especially total essential amino acids were higher in the formula-fed infants. Those fed formula also had plasma concentrations of methionine, isoleucine, phenylalanine, leucine, valine, threonine, aspartate, proline, lysine, tyrosine, histidine that exceeded plasma concentrations of breast-fed infants by 2 or more standard deviations. Concentrations of arginine, glutamic acid, glutamine, ornithine, serine, cystine did not differ and taurine was higher in the breast-fed infants. The data indicate that formulas in common use today during weaning (4-6 months) provide excessive protein intakes when compared to the breast-fed control infants. A lowering of protein concentration and a further manipulation of the whey:casein ratio is necessary if plasma amino acid patterns similar to those found in breast-fed infants is to be achieved with artificial feeding.

Amino Acids↗
PubMed1987

Protein and energy intake during weaning: I. Effects on growth.

The growth and food consumption of 30 healthy infants from 4 to 6 months of age have been measured. Two groups were assigned randomly to either a formula with 1.9 g of protein and 72 kcal per 100 ml (F1) or 2.7 g of protein and 69 kcal per 100 ml (F2). A third group of infants were fed breast milk (0.96 g of protein and 65 kcal per 100 ml (HM)). All infants received supplementary food according to the same regimen and were fed ad libitum. The mean protein intake was 1.3, 2.6 and 3.6 g/kg/day in the HM-, F1- and F2-groups respectively. The corresponding mean energy intake was 80, 101 and 94 kcal/kg/day. The formula-fed infants had significantly higher protein and energy intakes when compared to the breast-fed group. No significant differences were found in the rate of growth of crown-heel length, head circumference or in weight gain. The differences in protein intake between the breast- and formula-fed infants without differences in growth indicate that the formulas may provide a protein intake in excess to the needs.

Body Height↗
PubMed1987

Protein intake during weaning. II. Metabolic responses.

Metabolic responses to different feeding regimens during the weaning period have not previously been studied. In this study 30 healthy infants aged 4-6 months were divided into three feeding regimens with 10 infants in each. The regimens were: Human milk (HM-group), formula F1 with 1.9 g protein/100 ml (F1-group) or formula F2 with 2.7 g protein/100 ml (F2-group). All infants received the same supplementary food and were fed ad libitum. Concentrations of serum urea were significantly higher (p less than 0.001) in the formula groups as compared to the breast-fed infants throughout the entire study period. Serum albumin concentrations were within normal limits in the breast-fed infants indicating adequate protein nutritional status. There were no differences in the concentrations of creatinine and total nitrogen in urine between the artificially fed and the breast-fed infants at the beginning of the study (4 months), but at 6 months these concentrations were significantly higher in the formula-fed (infants (p less than 0.001). The results suggest that formulas now in common use during weaning provide amounts of protein which produce metabolic manifestations implying excessive protein intakes.

Blood Urea Nitrogen↗
PubMed1986

Bovine beta-lactoglobulin in the human milk. A longitudinal study during the whole lactation period.

Human milk samples (n = 232) collected during the whole lactation period from 25 healthy, Swedish mothers were analyzed by radioimmunologic method for content of bovine beta-lactoglobulin. Detectable amounts (5-800 micrograms/l) were found in 93 of 232 milk samples (40%). Six mothers had no detectable beta-lactoglobulin in their breast milk on any occasion. Two mothers had measurable beta-lactoglobulin in all their milk samples. No correlation was found between daily cow's milk intake and concentration of beta-lactoglobulin in the milk samples. Six mothers with allergic symptoms such as asthma, hay-fever, eczema all had detectable amounts of beta-lactoglobulin in their milk. Of 19 mothers without allergy, 13 had detectable amounts. This difference did not show statistical significance. The presence of symptoms in the infant such as diarrhoea, vomiting, colic, exanthema was significantly correlated to high levels of beta-lactoglobulin in the milk. Bovine beta-lactoglobulin was also detected in 7 of 13 serum samples. The two mothers with detectable beta-lactoglobulin in all milk samples had the highest serum values, and their infants suffered from gastro-intestinal symptoms, weight decline and exanthema.

Animals↗
PubMed1986

Human alpha-lactalbumin as a marker of macromolecular absorption.

alpha-Lactalbumin was purified from human milk and a competitive radioimmunoassay for measuring serum concentrations of human alpha-lactalbumin was developed. Human alpha-lactalbumin was not detected (less than 5 micrograms/l) in serum from adult men (n = 4), non-pregnant women (n = 6) or in serum from seven of eight formula fed infants. alpha-Lactalbumin was found in serum from pregnant women (19-130 micrograms/l, n = 4), cord blood (22-72 micrograms/l, median value 35 micrograms/l, n = 9), and from newborn non-fed infants (less than 1 day old) (less than 5-50 micrograms/l, median value 15 micrograms/l, n = 11). In breast fed infants the serum concentration of alpha-lactalbumin was highest in preterm infants (140-952 micrograms/l serum/l human milk/kg body weight, n = 4) and decreased in term infants successively with maturity (age 5-30 days: median value 85 micrograms/l serum/l human milk/kg body weight, n = 7; age 31-60 days: median value 43, n = 6; age 61-135 days: median value 12, n = 6). A human milk feeding to three infants one month of age gave serum peak values of alpha-lactalbumin after 30 to 60 minutes. We suggest that human alpha-lactalbumin is a suitable marker for investigating macromolecular absorption in physiological and pathological conditions.

Female↗