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Biomedical subjects

P Bardos

Publications and source records attributed to P Bardos.

At least 127 records · Page 7Linked to original sources
PubMed1980

Specificity and nephrotoxicity of heterologous antibodies directed against renal basement membranes.

Two immune sera have been raised in sheep against rabbit glomerular and tubular basement membranes, respectively (GBM and TBM). Their specificity was investigated by immunoabsorption and radioimmunoassay, and their nephrotoxicity was studied by injecting them into New Zealand rabbits. Both antisera reacted in vitro collagen and noncollagen-related glycopeptides. However, while the anti-GBM antiserum reacted preponderantly with GBM and TBM collagen which probably represent the antigen(s) shared by the two basement membranes, the anti-TBM antiserum was directed preferentially against the noncollagenous component of rabbit TBM. The anti-GBM antiserum induced in rabbits a diffuse extracapillary glomerulonephritis with linear fixation of autologous IgG and C3 along the GBM. The anti-TBM antiserum also induced an extracapillary glomerulonephritis but in addition a focal tubular atrophy was seen and autologous IgG and C3 were fixed along both GBM and TBM and glucosuria frequently occurred. These results suggested that the glomerular lesions induced by the two antisera were due to anticollagen antibodies while the tubulointerstitial lesions were due to antibodies directed against the noncollagenous portion of TBM.

Animals↗
PubMed1979

[Presence of lectin-like substances in the basement membrane of the human kidney glomerulus].

Crude extracts from the human glomerular basement membranes solubilized by pepsin or bacterial collagenase agglutinate normal or transformed human cells. Cytoagglutination is inhibited by N-acetyl-osamines. These properties are reminiscent of lectins. When agglutinated cells are incubated for an additional 20 hrs. period in minimal serum free medium but in presence of these basement membrane extracts, they attach to the glass and spread out.

Agglutination↗
PubMed1979

Lectin-like activity of components extracted from human glomerular basement membrane.

Different fractions of human glomerular basement membranes have been isolated by enzymatic and chemical methods. These fractions were analyzed for their chemical structure and biological activity. The hypothesis that human glomerular basement membrane glycopeptide fractions related to collagenous sequences could act as a lectin-like substance was explored; in fact, extracellular glycoprotein factors play a role in cell-cell interactions and cell adhesion. These collagenous glycopeptides agglutinate human transformed or embryonic cells within 2 hr. The cell agglutination is inhibited by the following sugars: N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. In addition, the rapid cytoagglutination is followed by a cell spreading effect after a further 20-hr incubation. These data led to the postulate that the maintenance of tissue differentiation is governed by the interaction of cells with peculiar sites of the basement membrane consisting of a proteolysis-resistant association between collagen and matrix glycoprotein.

Agglutination Tests↗
PubMed1978

Nephrotoxic potency of antisera to three rat glomerular basement membrane glycoproteins.

In a previous article, we cited studies which have allowed us to isolate diverse glycoproteins of the rat glomerular basement membrane (GMB) and to study their biochemical structures and antigenicity. This present study attempts to examine, using the heterologous nephrotoxic nephritis model (Masugi's nephritis) the nephrotoxicity of immune sera prepared from three of these glycoproteins: one fairly rich in collagen-like structures (A3), another lacking collagen-like structures (A1), and a third of intermediate composition (A2). The results obtained are discussed in relation to those already published concerning the nature of the GBM antigen(s) responsible for the nephrotoxicity of the sera.

Animals↗
PubMed1977

[Isolation of structural glycoproteins from human placenta].

Microfibrils about 100 A wide are isolated by mechanical procedures (sieving and ultrasonic disintegration from villosities of human placenta. Amino acid and carbohydrate compositions seem to be related to structural glycoproteins described before in connective tissues.

Amino Acids↗
PubMed1977

[Simultaneous isolation of rabbit glomerular and tubular basement membrane].

A method allowing simultaneous isolation of Rabbit alomerular and tubular basement membranes has been perfected. Rabbit tubular basement membrane has also been obtained by tryptic digestion of the renal cortex. Electron microscopic observation and biochemical analysis show that the contamination of the membrane preparations by cellular components is negligible.

Animals↗
PubMed1976

[Variations of the concentrations of certain glycoproteins in maternal serum, fetal serum and amniotic fluid during pregnancy (author's transl)].

The authors investigated systematically the variations during normal pregnancies of the concentrations of alpha-1-antitrypsin, orosomucoid, transferrin and alpha-fetoprotein simultaneously in maternal serum, fetal serum and amniotic fluid. The role of certain factors such as the gestational age birth weight, placental weight and pairty were studied with regard to variations in the concentrations of each of these proteins. This research permitted the definition during pregnancy of the normal concentrations for these four proteins and allowed us to learn more about protein exchanges between fetal blood, maternal blood and amniotic fluid. There exists a difference between the concentrations of alpha-1-antitrypsin and of orosomucoid found for primigravidae and for multigravidae. The role of these glycoproteins in preventing the mother from rejecting the fetus (insofar as the fetus may be considered as an allograft) is discussed.

Amniotic Fluid↗