PubMed Health⌕ Search

Biomedical subjects

M De Visscher

Publications and source records attributed to M De Visscher.

At least 19 recordsLinked to original sources
PubMed1979

Hormonal and nutritional status: critical conditions for endemic goiter epidemiology?

Recent advances in protein metabolism and in glycoprotein synthesis bring further insight into endemic goiter epidemiology. Retinol circulates in the blood stream in close parallelism with retinol-binding protein and prealbumin (RBP-PA), a protein complex whose liver secretory rate is dependent upon hormonal and nutritional status. On the other hand, normal glycosylation reaction occurs through the formation of a retinol-linked sugar complex. It is suggested that the relative drop of serum retinol levels, as a result of modified hormonal climate and/or declining protein status, might constitute a critical factor capable of inducing a defective incorporation of mannose into native thyroglobulin, leading to an early depression of the full glycoprotein production. This concept affords a comprehensive explanation of the following unresolved data recorded in goitrous areas: (1) clinical and biochemical discrepancies between subjects living in the same morbid territory, (2) persistence of endemicity in spite of appropriate iodine supplementation, (3) similar prevalence of goiter hypertrophy in male and female prepubertal children, (4) increased frequency of goiter enlargement in the four most vulnerable groups, namely preschool children of both sexes, adolescent girls, pregnant women, and elderly persons, (5) decreased impact of thyroid swelling accompanying improved socio-economic status, even without iodine addition, and (6) resurgence of goitrous hyperplasia as an effect of seasonal or sporadic deterioration of nutritional habits, even when iodine supply remains unchanged.

Adolescent↗
PubMed1978

[Thyroid function in protein-caloric malnutrition in infants (author's transl)].

Iodine kinetics and thyroid function were investigated in 68 cases of protein-caloric malnutrition (senegales children). This nutritional state induces an acute and severe alteration of thyroid function, as indicated by the reduced iodine uptake and clearance, a 50% decrease of hormonal secretion rate, and the low levels of total and free T4. T3 concentration is also very low: this may be partly due to a defective conversion of T4 to T3. Despite this state of primary hypothyroidism, no hypersecretion of TSH is observed.

Age Factors↗
PubMed1976

Secretory activity of isolated thyroid adenomas.

The catabolic phase of thyroid secretion --thyroglubulin (Tg) uptake and hydrolysis, release of hormones--has been investigated in vitro, by incubating thyroid slices with 0.1% labelled Tg, in cases of isolated adenomas. Twenty-two specimens were examined: 11 cold follicular adenomas, 5 hot nodules from euthyroid patients, 2 untreated toxic adenomas, and 4 pretreated toxic adenomas. The results were compared with those obtained in 11 specimens of normal tissue. Tg pinocytosis (the amount of Tg taken up by the slices per mg of tissue) was severely impaired in all the non-toxic nodules, cold or hot, i.e., whatever the in vivo activity of the thyroid iodide pump. In toxic adenomas, every step of the catabolic hormonogenesis was activated: high pinocytotic activity, increased Tg hydrolysis, and the discharge of hormonal products; in pretreated cases, the whole process was slowed down. Enzymic activity of the acid hydrolases, beta-galactosidase and cathepsin, was elevated in all the nodules so far investigated, particularly in the toxic adenomas.

Adenoma↗
PubMed1976

T3 resin uptake in protein-calorie malnutrition.

RT3U3) is significantly elevated (P less than 0.001) in the acute stage of kwashiorkor and returns to normal after 2 weeks of appropriate refeeding. RT3U is characterized by a high negative correlation with TBGcap. This negative correlation is maximal on admission (r equals -0.88) and gradually declines to normal value (r equals -0.63) with clinical recovery. This finding is consistent with the main role attributed to TBG in determining RT3U level. The collected data emphize the importance of the protein plasma levels in the evaluation of the thyroid function with RT3U in protein-calorie malnutrition.

Child, Preschool↗
PubMed1975

Albumin, transferrin and the thyroxine-binding prealbumin/retinol-binding protein (TBPA-RBP) complex in assessment of malnutrition.

A comparative study of the level of 4 plasma proteins in malnutrition shows that albumin has low sensitivity, transferrin has intermediate and the TBPA-RBP complex has the highes sensitivity to an alteration in the nutritional status. According to protein and/or iron deficiency, the synthesis of trnasferrin seems to be submitted to contradictory impulses which partially invalidates this test as a reliable index for estimating protein depletion alone. On the contrary, the components of the TBPA-RBP complex respond together and in a parallel direction to protein deficiency. The high degree of sensitivity of TBPA and RBP to an inadequate protein intake is apparently related to their rapid turnover rate and to their unusual richness in tryptophan, which is known to play a key role in the control of protein synthesis. Measurement of TBPA (or RBP) is proposed as a method for the detection of pre-kwashiorkor and early marasmus.

Child, Preschool↗
PubMed1975

Defective thyroglobulin endocytosis and hydrolysis in thyroid cold nodules.

The catabolic phase of thyroid secretion has been studied by incubating thyroid slices with 0.1 % 125-I thyroglobulin (Tg) in the following cases: 11 follicular adenomas (FA), 8 hyerplastic nodules in multinodular glands (NM), 3 carcinomas (follicular or papillary, FC, PC) and normal (N) or micronodular tissue (M). Tg pinocytosis is severely impaired in all cold nodules (25 to 60 % reduction). In the follicular tumours (FA, FC), Tg hydrolysis is more affected than would be expected based only on reduced Tg endocytosis: the hydrolysis products remain in the phagolysosomes instead of being secreted. As far as the acid hydrolases are concerned these enzymatic activities are increased in nearly all nodules, in particular in follicular adenomas and carcinomas.

Endocytosis↗
PubMed1975

The role of retinol-binding protein in protein-calorie malnutrition.

Plasma RBP is decreased to 1.62 mg plus or minus 0.71/100 ml, or 31.1 percent of normal, in the acute stage of kwashiorkor. RBP doubles its plasma level after 1 wk and triples after 2 wk of appropriate refeeding. The return to normal of RPB runs in close parallel with prealbumin (PA), implying that both components remain bound by 1:1 molar ratio in the PA-RBP complex. Low values recorded on admission for RBP seem to be the result of reduced liver biosynthesis. On the other hand, a high correlation persists between RBP and retinol plasma level along the successive steps of clinical recovery, suggesting that RBP acts as the limiting factor for retinol transport.

Biological Transport↗
PubMed1975

Discrepancy between the measurement of thyroxine-binding prealbumin plasma level and binding capacity in protein-calorie malnutrition.

The measurement of thyroxine-bindung prealbumin (TBPA) in protein-calorie malnutrition by two different techniques leads to the recognition of an unexpected discrepancy. Whereas TBPA plasma levels as measured by immunodiffusion are markedly decreased to 29.3% of the normal, those recorded by maximal binding capacity (TBPAcap) are characterized by a wide dispersion. In the control group, the ratio between TBPAcap and TBPA plasma level is 9.1. In the malnourished group on admission, the same ratio is 30.0. The possibility of a qualitative effect in the tetrameric TBPA structure, with the binding of additional thyroxine (T4) molecules on the secondary binding sites, has been investigated. This hypothesis has been discarded by Scatchard plot studies. The normal 1:1 molar ratio between TBPA and T4 is unaffected in protein-deficient patients. Discrepant results obtained for TBPAcap and TBPA levels appear to be the consequence of low plasma protein levels, leading to an artifact in the electrophoretic method.

Blood Protein Electrophoresis↗