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Biomedical subjects

J Raymond

Publications and source records attributed to J Raymond.

At least 217 records · Page 12Linked to original sources
PubMed1981

Formation of intercellular collagen matrix by cultured liver epithelial cells and loss of its ability in hepatocarcinogenesis in vitro.

Epithelial cells of normal rat liver origin (strain RL34) synthesized the alpha 1 peptide of type I collagen. In nononcogenic cultures (RL34 and RL34EC) and a marginally oncogenic culture (RL34HII), the peptide was continuously secreted from the proliferating cells. Part of the soluble peptide was incorporated into the intercellular matrix of contact-inhibited cells after confluency, while the remainder was degraded. The intercellular matrix contained characteristic collagen fibrils which were argyrophilic and revealed a 64 nm axial periodicity. Epithelial cells of an oncogenic culture (RL34HT) secreted procollagen into the medium continuously throughout their proliferative phases and were unable to accumulate collagen fibrils in the intercellular matrix. The depletion of collagen accumulation in the hepatocarcinoma cell culture was ascribed to lack of the binding of native collagen molecules to the cell membrane and the persistence of high proteolytic activity on the cell surface.

Animals↗
PubMed1980

[Identification of the vestibular projections in the oculomotor nuclei in the cat by autoradiography and electron microscopy].

The projection of vestibular pathways to the oculomotor nuclei ws investigated by electron microscopic radioautography. Unilateral injection of tritiated amino acids into the rostral vestibular complex was used in order to characterize the location and to identify the different types of labeled synaptic terminals involved in these pathways. In the normal oculomotor nuclei, 4 types of synaptic boutons were identified. Following the labeling of the vestibular synapses, in the ipsilateral oculomotor nucleus, types I and II boutons are the most prominent group and make up 75% of the synaptic vesicles, they are distributed on the cellular soma and the large dendrites of the oculomotor neurons. In contrast, in the contralateral oculomotor nucleus, type III boutons which are smaller and have larger diameter synaptic vesicles were predominant; they are prevalent on the distal part of the dendritic tree. From the results obtained, a relationship between the present anatomical findings and previously published physiological studies is established. The following conclusion is suggested: the inhibitory vestibular inputs probably terminate on the oculomotor neurons by these large types I and II boutons and the excitatory vestibular inputs by the smaller type III boutons. Also discussed is the complexity of the pattern of afferentation and the functional arrangement of the oculomotor nuclei.

Animals↗
PubMed1980

[Neutral calcium dependent proteinase from rabbit skeletal muscle: activity on myofibrillar proteins].

Experiments have been carried out to explore the proteolytic cleavage of rabbit skeletal myofibrils by a calcium dependent neutral proteinase (CaANP). Polyacrylamide gel elctrophoresis on great slabs showed the ability of CaANP to degrade myofibrils more readily than supposed. Besides the hydrolysis of troponin T and the apparition of degradation product of 30,000 molecular weight, the activity of this enzyme is obvious too on some components of the M-line and on heavy subunits of tropomyosin as well as on three unidentified proteic fractions. The variety of the degradation products which appear suggest that the specificity of CaANP is not as selective as presumed. The participation of this proteinase in the postmorten evolution of muscle and its intervention in the turnover of myofibrillar proteins is discussed.

Animals↗
PubMed1980

Cell surface adenosine 5'-triphosphatase as an in vitro marker of the lineage and cytodifferentiation of oncogenic epithelial cells from rat liver parenchyma.

The relationship between the oncogenicity and the surface properties of cultured liver epithelial cells has been studied with the newborn Wistar rat-derived euploid line, RL34, and its heteroploid variants. An oncogenic variant, RL34HT, appeared to be more functionally active than its nononcogenic counterparts with respect to cell surface adenosine 5'-triphosphatase (ecto-ATPase) as well as to cytoplasmic enzymes such as tyrosine aminotransferase, gamma-glutamyl transpeptidase, and alkaline phosphatase. The cell surface of RL34HT was distinguished from those of nononcogenic and marginally oncogenic cell populations by the presence of abundant microvilli and by the absence of large external transformation-sensitive protein (fibronectin). High-Km and high-Vmax Ca2+-Mg2+ -ecto-ATPase was found in RL34HT. All nononcogenic cell lines had a flat granular surface membrane with high levels of fibronectin and also exhibited ecto-ATPase activity with low Km and low Vmax. When RL34HT was grown in dibutyryl cyclic adenosine 3',5'-monophosphate and theophylline, the external cell surface was partially restored to the polypeptide compositions of RL34, and there was an increase in Vmax of ecto-ATPase without a change in Km. The high-Km ecto-ATPase may be a useful indicator reflecting the lineage and cytodifferentiation of oncogenic liver epithelial cells, since it is also known to be localized at the bile canalicular microvilli of normal adult hepatocytes.

Adenosine Triphosphatases↗
PubMed1979

Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle.

Ca(2+)-activated neutral proteinase was purified from rabbit skeletal muscle by a method involving DEAE-Sephacel chromatography, affinity chromatography on organomercurial-Sepharose and gel filtration on Sephacryl S-200 and Sephadex G-150. The SDS (sodium dodecyl sulphate)/polyacrylamide-gel-electrophoresis data show that the purified enzyme contains only one polypeptide chain of mol.wt. 73000. The purification procedure used allowed us to eliminate a contaminant containing two components of mol.wt. about 30000 each. Whole casein or alpha(1)-casein were hydrolysed with a maximum rate at 30 degrees C, pH7.5, and with 5mm-CaCl(2), but myofibrils were found to be a very susceptible substrate for this proteinase. This activity is associated with the destruction of the Z-discs, which is caused by the solubilization of the Z-line proteins. The activity of the proteinase in vitro is not limited to the removal of Z-line. SDS/polyacrylamide-gel electrophoresis on larger plates showed the ability of the proteinase to degrade myofibrils more extensively than previously supposed. This proteolysis resulted in the production of a 30000-dalton component as well as in various other higher- and lower-molecular-weight peptide fragments. Troponin T, troponin I, alpha-tropomyosin, some high-molecular-weight proteins (M protein, heavy chain of myosin) and three unidentified proteins are degraded. Thus the number of proteinase-sensitive regions in the myofibrils is greater than as previously reported by Dayton, Goll, Zeece, Robson & Reville [(1976) Biochemistry15, 2150-2158]. The Ca(2+)-activated neutral proteinase is not a chymotrypsin- or trypsin-like enzyme, but it reacted with all the classic thiol-proteinase inhibitors for cathepsin B, papain, bromelain and ficin. Thus the proteinase was proved to have an essential thiol group. Antipain and leupeptin are also inhibitors of the Ca(2+)-activated neutral proteinase.

Animals↗
PubMed1976

[Pathways and ascending vestibular projections emanating from primary nuclei: radioautographic study (author's transl)].

A study of the pathways and ascending vestibular projections was carried out in the cat after unilateral injection of tritiated leucine into the rostral vestibular complex. Radioautographic analysis revealed a gradual decline in the density of labeling as ascending fibers were found to progress towards more rostral relays. The pathways and projections were very compact in the oculomotor nuclei, became less intense in the Cajal and Darkschewitsch nuclei, and thinned out considerably until they reached a transitional zone in the thalamus between the ventrobasal and ventrolateral complexes. These results confirm established and previous findings in this laboratory obtained by neurophysiological and neurohistological examination procedures. They provide the first anatomical evidence concerning the existence of vestibulothalamic projections and pathways.

Afferent Pathways↗
PubMed1976

A vestibulothalamic pathway: electrophysiological demonstration in the cat by localized cooling.

Localized cooling was used in the search for vestibulothalamic pathways and a study was made of its effect on the activity of the thalamic neurons brought into action by stimulation of the vestibular nerve. Two cell populations were identified by their distinctive latencies in the ventral part of the posterior thalamus. Short latency responses were transmitted monosynaptically by means of a direct controlateral pathway whose course was identified. For long latency responses, the hypothesis of a polysynaptic path seems probable.

Animals↗
PubMed1976

[Cathepsin D from horse spleen. I. Purification and study of certain physicochemical properties].

Horse spleen cathepsin D (3.4.23.5.) was purified from crude extract by sodium chloride and ethanol precipitation, column chromatography fractionation on DEAE cellulose and CM Sephadex, re-chromatography on DEAE cellulose and gel filtration. The enzyme has been purified about 3.000 folds with a yield of 30 per cent. The purified enzyme seems to be homogeneous on Sephadex G100, one protein band is apparent on disc electrophoresis. Determined by dansylation the N-terminal amino acid is glycine. A molecular weight of 42,500 +/- 3,000 was obtained with Sephadex G100 gel filtration and light scattering measurements. Amino acid analysis and chemical determinations were performed: cathepsin D is a glycoprotein (2 or 3 osamine residues) including 344 amino acids and 4 disulfide bonds. Spectrophotometric data show that E1cm/1 mg/ml = 1.01 at lambda = 280 nm. ORD measurements indicate about 20 per cent of helicoidal content in the molecule.

Amino Acids↗
PubMed1976

[Cathepsin D from horse spleen. II. Study of certain enzymatic properties].

This work reports some enzymatic properties of highly purified horse spleen cathepsin D. Hydrolysis rate of several proteins are compared. The Kinetic constants (Km = 4.95 10(-5) M and Vm = 1,76 delta DO/mn/mug) have been determined in the presence of a denatured haemoglobin substrate. Stability of the enzymatic preparation is discussed according to the pH, concentration and time of storage. Some investigations concerning the active site are described. Enzymatic and chemical results show that dicarboxylic and tryptophanyl residues seem to be involved in the hydrolytic process. Catalysis does not depend on sulfhydryl or seryl residues. Different salts, particularly nitrate, nitrite and polyphosphate are potent inhibitors of enzymatic activity.

Animals↗
PubMed1976

Effects of source and concentration of thrombin, and divalent cations, on thrombin time of heparinized plasma.

The effects of the source and concentration of thrombin, and those of divalent cations, on the thrombin time (TT) of heparinized plasma were investigated. A correlation between TT and the heparin concentration was obtained only when the thrombin was of human origin and when it was reconstituted in divalent cation solutions. Relatively small variations in thrombin concentration resulted in marked differences in TT of heparinized plasma. Bovine thrombin gave a very prolonged TT of heparinized plasma compared with human thrombin, though the two thrombins gave identical TT's for non-heparinized control plasma. Divalent cation solution, in which thrombin was reconstituted, had a profound influence on TT of heparin plasma. When thrombin was reconstituted in 0.1 M MnCl2 solution, the TT of a plasma containing 0.5 unit heparin per ml. was the same as that of a plasma containing no heparin. The reliability of the thrombin time test as a means of monitoring heparin anticoagulation must be established by individual laboratories via extensive testing of clinical samples.

Animals↗
PubMed1976

Critical importance of citrate--blood ratio in platelet aggregation studies.

The effects of citrate concentration on adenosinediphosphate-, epinephrine-, collagen-, and ristocetin-induced human platelet aggregation were investigated. Relatively small increments in citrate concentration markedly inhibited platelet aggregation by all three physiologic agents. The inhibitory effect was greatest on epinephrine-induced aggregation, and least on collagen-induced aggregation. Ristocetin-induced aggregation was not affected by excess citrate anticoagulation. These findings indicate the importance of controlling the citrate:blood ratio in clinical platelet aggregation studies and in the assessment of antiplatelet drugs.

Adenosine Diphosphate↗
PubMed1976

Metal ion content of Escherichia coli versus cell age.

The potassium, calcium, magnesium, and zinc ion content of cells in exponential and synchronously growing cultures of Escherichia coli B/r was determined with an X-ray fluorescence spectrometer and an atomic absorption spectrophotometer. Cellular potassium, calcium, and magnesium content increased smoothly during the cell cycle, but cellular zinc showed a steplike increase about 10 to 15 min after cell division in a culture having a doubling time of 47 min. The possible role of cellular zinc in the control of cell division is discussed.

Calcium↗
PubMed1975

An absolute requirement for serum macromolecules in phytohaemagglutinin-induced human lymphocyte DNA synthesis.

We have examined the effect of different variables such as tissue culture media, with or without various supplements, lymphocyte isolation techniques, lymphocyte contamination by autologous red blood cells and platelets, and lymphocyte numbers, on the requirement for serum during phytohaemagglutinin (PHA) induced DNA synthesis in human lymphocytes. At all mitogen doses tested, we have found that dialysable constituents of serum enrich the ability of all tissue culture media to support lymphocyte DNA synthesis; however, human lymphocytes display an absolute requirement for nondialysable macromolecular constituents of serum in order to synthesize DNA.

Cell Separation↗