Biomedical subjects

A M Lajous-Petter

Publications and source records attributed to A M Lajous-Petter.

4 recordsLinked to original sources

PubMed1995

A human autoantibody recognizing nuclear matrix-associated nuclear protein localized in dot structures.

A human autoimmune serum is used to characterize a protein which is located within a dot-like structure of the interphase nucleus. The dots are located in the nucleoplasma outside the nucleoli. The dot-like structure could be observed on a variety of human substrates (HEp-2, HepG2, HeLa, Molt-4, WI-38 cell lines, peripheral blood lymphocytes), mouse cell lines and tissues (3T3, L929, spleen sections), rat sections, marsupial PtK2 cells and hamster cell lines. The range of the number of dots and their size differed between cells and cell lines and varied between 1 and 24. The antigen could be identified as a 53 kDa protein with a pI of 8.7 and was named NDP53. Digestion experiments suggested that the protein is not associated with DNA or RNA, but is associated with the nuclear matrix. Immunelectron microscopy using ultra-thin sections revealed filamentous structures with a diameter of 0.1 to 0.6 microns. The antigen colocalizes with Sp100, PML and NDP55, which are part of a multiprotein complex known as PML oncogenic domain (POD), nuclear bodies, Kr bodies or ND10.

Animals↗

PubMed1994

Liver-intestine cadherin: molecular cloning and characterization of a novel Ca(2+)-dependent cell adhesion molecule expressed in liver and intestine.

A novel member of the cadherin family of cell adhesion molecules has been characterized by cloning from rat liver, sequencing of the corresponding cDNA, and functional analysis after heterologous expression in nonadhesive S2 cells. cDNA clones were isolated using a polyclonal antibody inhibiting Ca(2+)-dependent intercellular adhesion of hepatoma cells. As inferred from the deduced amino acid sequence, the novel molecule has homologies with E-, P-, and N-cadherins, but differs from these classical cadherins in four characteristics. Its extracellular domain is composed of five homologous repeated domains instead of four characteristic for the classical cadherins. Four of the five domains are characterized by the sequence motifs DXNDN and DXD or modifications thereof representing putative Ca(2+)-binding sites of classical cadherins. In its NH2-terminal region, this cadherin lacks both the precursor segment and the endogenous protease cleavage site RXKR found in classical cadherins. In the extracellular EC1 domain, the novel cadherin contains an AAL sequence in place of the HAV sequence motif representing the common cell adhesion recognition sequence of E-, P-, and N-cadherin. In contrast to the conserved cytoplasmic domain of classical cadherins with a length of 150-160 amino acid residues, that of the novel cadherin has only 18 amino acids. Examination of transfected S2 cells showed that despite these structural differences, this cadherin mediates intercellular adhesion in a Ca(2+)-dependent manner. The novel cadherin is solely expressed in liver and intestine and was, hence, assigned the name LI-cadherin. In these tissues, LI-cadherin is localized to the basolateral domain of hepatocytes and enterocytes. These results suggest that LI-cadherin represents a new cadherin subtype and may have a role in the morphological organization of liver and intestine.

Amino Acid Sequence↗

PubMed1990

Totally implantable catheter system in the dog.

Four totally implantable catheter systems for arterial and venous access were implanted for a maximum of 17 months. Hematological and bacteriological tests were performed. The platelets remained normal. Occasionally observed bacteremias were successfully treated. The morphological and SEM results show that in comparison to the standard externalized catheter the totally implantable catheter system has a longer functional lifetime and less problems with sepsis while the well-being of the experimental animal is improved.

Animals↗

PubMedDate not supplied

Intracellular bactericidal activity of fosfomycin against staphylococci: a comparison with other antibiotics.

The intracellular bactericidal activity of fosfomycin was compared to that of other anti-staphylococcal agents. Two staphylococcal strains (one isolate of Staphylococcus aureus and one isolate of Staphylococcus epidermidis) were incubated in vitro with human granulocytes isolated from volunteers. After phagocytosis and removal of residual extracellular bacteria, the cells were resuspended in the presence of clinically relevant concentrations of fosfomycin, teicoplanin, vancomycin and rifampin. The number of bacteria surviving intracellularly was determined by colony counts after osmotic lysis of the granulocytes at different time intervals. Incubation with fosfomycin resulted in a mean reduction of intracellular bacteria by approximately two logs of ten within 18 h for both staphylococcal strains. Although less effective than rifampin, fosfomycin showed a significantly higher intracellular activity than the glycopeptide antibiotics in this model.

Anti-Bacterial Agents↗