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Biomedical subjects

G Jori

Publications and source records attributed to G Jori.

At least 127 records · Page 7Linked to original sources
PubMed1986

Role of high-, low- and very low-density lipoproteins in the transport and tumor-delivery of hematoporphyrin in vivo.

Free hematoporphyrin administered intravenously to healthy rabbits (1-28 mg/kg body weight) is bound by the 3 major lipoprotein components of plasma (VLDL, LDL and HDL) with different efficiency. In vitro-prepared complexes of hematoporphyrin (Hp) with lipoprotein fractions isolated from mouse serum have been injected intracardiacally into mice affected by MS-2 fibrosarcoma (1 mg of Hp per kg body weight). LDL appear to allow a more specific delivery of the complexed Hp to the tumor tissue as compared with HDL, VLDL or free Hp. The different behavior of VLDL, LDL and HDL as carriers of Hp in vivo is also discussed.

Animals↗
PubMed1986

Controlled targeting of different subcellular sites by porphyrins in tumour-bearing mice.

Unilamellar liposomes of dipalmitoyl-phosphatidylcholine can incorporate various porphyrins in either the phospholipid bilayer or the internal aqueous compartment depending on the water-/lipo-solubility of the drug. Intraperitoneal injection of the liposome-bound porphyrins to mice bearing a MS-2 fibrosarcoma results in remarkably more efficient tumour targeting than that obtained by administration of the same porphyrins dissolved in homogeneous aqueous solution. Moreover, also water-insoluble porphyrins can be transported to the tumour via liposomes. Fractionation of liver and neoplastic cells indicates that the subcellular distribution of liposome-delivered porphyrins is also dependent on their solubility properties: thus, relatively polar porphyrins, such as tetra(4-sulfonatophenyl)porphine and uroporphyrin, are mainly recovered from the soluble fraction, whereas hydrophobic porphyrins, such as haematoporphyrin or porphyrin esters, preferentially partition in the cytoplasmic membrane. As a consequence, different subcellular sites can be targeted by porphyrins and possibly photodamaged through a suitable choice of the drug-carrier system.

Animals↗
PubMed1985

The photosensitizing activity of haematoporphyrin on mollicutes.

The photosensitizing activity of haematoporphyrin (HP) on Mycoplasma hominis and Acholeplasma laidlawii was studied as a function of the phase of growth and the amount of sterols in the cell membrane. Less HP was bound to cells when the membrane had a high sterol content. Both strains in the exponential but not in the stationary phase of growth were sensitive to HP treatment (above 1 microgram ml-1) in the dark. Visible light irradiation of HP-loaded cells caused in all cases a decrease of cell survival, with concomitant changes in the pattern of membrane proteins that suggested protein-protein cross-linking, and the appearance of ultrastructural alterations (rounded and lysed cells); the photosensitivity was indirectly related to the sterol content of the cell membrane. On the whole, our findings suggest that the cell membrane is a major target for HP photosensitization of mycoplasma cells.

Acholeplasma laidlawii↗
PubMed1984

The role of copper and quaternary structure on the conformational properties of Octopus vulgaris hemocyanin.

Some structural properties of Octopus vulgaris hemocyanin have been investigated by fluorescence spectroscopy. The three-dimensional structure of Octopus hemocyanin is remarkably tight, resulting in a deep burial of almost all the tryptophyl residues of the protein. The hemocyanin conformation has been studied in the two main aggregation states (11 S, 50 S) of the protein, and with respect to the presence or absence of copper in the active site. Upon changing the pH of the solution, Octopus hemocyanin in the 50 S aggregation state can assume at least three different conformations. During the transition between each conformation the fluorescence quantum yield changes, but the environment of tryptophans does not change. Dissociation of the protein from 50 S to 11 S strongly enhances its susceptibility toward denaturating agents such as pH or temperature, and modifies the effects of fluorescence quenchers such as acrylamide. Moreover, these effects are more pronounced when copper is removed from the active site. A comparative analysis of the results shows that the subunit-subunit interactions exerted within the 50 S species are more important in the maintenance of the conformational stability than the copper ions present in the active sites. This behavior can be accounted for by the large amount of Ca(II) ions linked to 50 S hemocyanin.

Animals↗
PubMed1984

Evidence for a major role of plasma lipoproteins as hematoporphyrin carriers in vivo.

Hematoporphyrin (5 mg/ml), administered intravenously to tumor-bearing patients, becomes associated with different serum proteins, including lipoproteins (mainly HDL), globulin and albumin. No residual porphyrin is bound to the two latter classes of proteins after 48 h, whereas the complexation with the lipoproteins appears to be particularly stable probably owing to the hydrophobic nature of hematoporphyrin. The late persistence of hematoporphyrin in serum is due to the binding to the VLDL fraction with special regard to its cholesterol moiety. The importance of hematoporphyrin transport by lipoproteins for the photodynamic therapy of tumors is briefly discussed.

Blood Proteins↗
PubMed1983

Intramolecular distances between tryptophan residues and the active-site serine residue in alkaline bacterial proteinases as measured by fluorescence energy-transfer studies.

Singlet-singlet energy transfer from the tryptophan residues to an active-site-serine-bound 5-dimethylaminonaphthalene-1-sulphonyl group was investigated in four subtilisins. The transfer distances for subtilisin Novo and mesentericopeptidase are 1.93 +/- 0.20 nm (19.3 +/- 2.0 A) and 1.81 +/- 0.20 nm (18.1 +/- 2.0 A) respectively. The positions of the indole groups in the three-dimensional structures of the two pairs of proteinases, namely subtilisin Novo and mesentericopeptidase on the one hand and subtilisins Carlsberg and DY on the other, are essentially identical.

Binding Sites↗