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Biomedical subjects

C Maison

Publications and source records attributed to C Maison.

14 recordsLinked to original sources
PubMed2006

[Cornea transplant].

The keratoplasty, or cornea transplant, is one of the oldest surgical techniques in opthalmology, whose indication are: 1) tectonic, in order to preserve corneal anatomy and integrity; 2) clinical, in order to eliminate the inflamed corneal tissue in cases refractory to medical treatment; 3) optical, in order to improve visual acuity; and 4) cosmetic, in order to improve the appearance of the eye. Improvements in technique and instruments, as well as in post-operative treatment and the means of preserving donated tissue, have improved survival of the grafts. The Pamplona Model of transplant coordination of the Virgen del Camino Hospital is considered to be original and unique in Spain. The logistics of this program include the protocol for detection and extraction of corneas as well as for keratoplasties.

Adolescent↗
PubMed2001

Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases.

Histone modifications might act to mark and maintain functional chromatin domains during both interphase and mitosis. Here we show that pericentric heterochromatin in mammalian cells is specifically responsive to prolonged treatment with deacetylase inhibitors. These defined regions relocate at the nuclear periphery and lose their properties of retaining HP1 (heterochromatin protein 1) proteins. Subsequent defects in chromosome segregation arise in mitosis. All these changes can reverse rapidly after drug removal. Our data point to a crucial role of histone underacetylation within pericentric heterochromatin regions for their association with HP1 proteins, their nuclear compartmentalization and their contribution to centromere function.

Animals↗
PubMed2000

RanGTP-binding protein NXT1 facilitates nuclear export of different classes of RNA in vitro.

To better characterize the mechanisms responsible for RNA export from the nucleus, we developed an in vitro assay based on the use of permeabilized HeLa cells. This new assay supports nuclear export of U1 snRNA, tRNA, and mRNA in an energy- and Xenopus extract-dependent manner. U1 snRNA export requires a 5' monomethylated cap structure, the nuclear export signal receptor CRM1, and the small GTPase Ran. In contrast, mRNA export does not require the participation of CRM1. We show here that NXT1, an NTF2-related protein that binds directly to RanGTP, strongly stimulates export of U1 snRNA, tRNA, and mRNA. The ability of NXT1 to promote export is dependent on its capacity to bind RanGTP. These results support the emerging view that NXT1 is a general export factor, functioning on both CRM1-dependent and CRM1-independent pathways of RNA export.

Animals↗
PubMed1997

The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles.

We have examined the in situ organization and nearest neighbours of the 'lamina-associated polypeptide-1' (LAP1), a type II membrane protein and a major constituent of the mammalian nuclear envelope. We show here that, during interphase, LAP1 forms multimeric assemblies which are suspended in the inner nuclear membrane and are specifically associated with B-type lamins. The LAP1-lamin B complex is distinct from analogous complexes formed by the 'lamina-associated polypeptide-2' (LAP2), another inner nuclear membrane protein, and includes a protein kinase. Upon nuclear envelope breakdown, LAP1 partitions with mitotic vesicles which carry nuclear lamin B. The LAP1 vesicles can be distinguished from fragments of the nuclear envelope containing LAP2 and exhibit a striking co-alignment with spindle microtubules. These observations suggest that the inner nuclear membrane comprises discrete territories which accommodate specific integral membrane proteins and are differentially disassembled during mitosis.

Amino Acid Sequence↗
PubMed1996

The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope.

Morphological studies have established that peripheral heterochromatin is closely associated with the nuclear envelope. The tight coupling of the two structures has been attributed to nuclear lamins and lamin-associated proteins; however, it remains to be determined which of these elements are essential and which play an auxiliary role in nuclear envelope-chromatin interactions. To address this question, we have used as a model system in vitro reconstituted vesicles assembled from octyl glucoside-solubilized nuclear envelopes. Comparing the chromosome binding properties of normal, immunodepleted and chemically extracted vesicles, we have arrived at the conclusion that the principal chromatin anchorage site at the nuclear envelope is the lamin B receptor (LBR), a ubiquitous integral protein of the inner nuclear membrane. Consistent with this interpretation, purified LBR binds directly to chromatin fragments and decorates the surface of chromosomes in a distinctive banding pattern.

Animals↗
PubMed1996

Characterization of p18, a component of the lamin B receptor complex and a new integral membrane protein of the avian erythrocyte nuclear envelope.

Employing avian erythrocytes, we have previously isolated a multimeric complex consisting of the lamin B receptor (LBR, or p58), the nuclear lamins, an LBR-specific kinase, a 34-kDa protein, and an 18-kDa polypeptide termed p18. As the LBR kinase and the 34-kDa component have been recently characterized, we now proceed in the characterization of p18. We show here that p18 is an integral membrane protein specific to the erythrocyte nuclear envelope which binds to LBR and B-type lamins. NH2-terminal sequencing indicates that p18 is distinct from other nuclear envelope components, but has similarity to the mitochondrial isoquinoline-binding protein. In situ analysis by immunoelectron microscopy and examination of digitonin-permeabilized cells by indirect immunofluorescence show that p18, unlike LBR and other lamin-binding proteins, is equally distributed between the inner and outer nuclear membrane. Furthermore, cycloheximide inhibition experiments reveal that the fraction of p18 that resides in the outer nuclear membrane does not represent nascent chains en route to the inner nuclear membrane, but rather material in equilibrium with the p18 that partitions with the inner nuclear membrane. The paradigm of p18 suggests that transmembrane complexes formed by the nuclear lamins and LBR provide potential docking sites for integral membrane proteins of the nuclear envelope that equilibrate between the rough endoplasmic reticulum and the inner nuclear membrane.

Amino Acid Sequence↗
PubMed1996

Integration of intermediate filaments into cellular organelles.

The intermediate filaments represent core components of the cytoskeleton and are known to interact with several membranous organelles. Classic examples of this are the attachment of keratin filaments to the desmosomes and the association of the lamin filament meshwork with the inner nuclear membrane. At this point, the molecular mechanisms by which the filaments link to membranes are not clearly understood. However, since a substantial body of information has been amassed, the time is now ripe for comparing notes and formulating working hypotheses. With this objective in mind, we review here pioneering studies on this subject, together with work that has appeared more recently in the literature.

Animals↗
PubMed1996

[Smoking and pregnancy: search for a correlation between cotininemia and Doppler findings].

OBJECTIVE: To search for a possible correlation between an effective marker of smoking and uterine and placental resistance during pregnancy. STUDY DESIGN: A prospective study was conducted at the Intercommunal Hospital Center of Montreuil, France: 81 healthy pregnant women underwent uterine and placental Doppler and cotidin blood assay, the best current test for smoking. RESULTS: This study shows a significative increase of utero-placental vascular resistances according with increased cotidine levels. CONCLUSIONS: The previously observed association between smoking and perinatal events most likely involves vascular resistance of uterus and placenta.

Adult↗
PubMed1995

Vimentin-associated mitotic vesicles interact with chromosomes in a lamin B- and phosphorylation-dependent manner.

We have assessed the involvement of the nuclear lamins in nuclear envelope reassembly. Analysis of perforated mitotic cells shows that A-type lamins are partly cytosolic and partly chromosome-bound, whereas B-type lamins are associated with vesicular structures throughout cell division. Lamin B-containing vesicles appear to dock on vimentin intermediate filaments during prometaphase, but dissociate from the cytoskeleton and assemble around chromatin at later phases of mitosis. Mitotic vesicles isolated from prometaphase cells en bloc with vimentin filaments can specifically capture chromosomes. Efficient chromosome capturing requires cytosolic factors and a dephosphorylating environment. Urea-stripping of the vesicles abolishes binding to chromosomes. However, reconstitution of the stripped membranes with purified B-type lamins restores their ability to bind to chromosomes in a cytosol- and dephosphorylation-dependent fashion. Vesicles reconstituted with B-type lamins form membraneous 'crescents' on the surfaces of chromosomes, but, unlike native vesicles, do not fuse into large sheets. From these observations we conclude that the initial targeting of mitotic vesicles to chromosomes is dependent on B-type lamins and on factors present in the mitotic cytoplasm. Apparently, further recruitment of membranes and fusion of chromosome-bound vesicles onto chromatin involves non-lamin peripheral membrane proteins.

Animals↗
PubMed1993

Inactivation of interleukin-6 in vitro by monoblastic U937 cell plasma membranes involves both protease and peptidyl-transferase activities.

Human promonocytic U937 cells have previously been shown to possess at their cell surface specific transmembrane serine proteases and N-terminal amino acid proteases as well as associated enzymes including elastase and cathepsin G. In this study, purified plasma membranes from U937 cells are reported to degrade the recombinant 21-kDa 125I-interleukin-6 (125I-IL-6) into 8-kDa products with loss of biological activity, as monitored by polyacrylamide gel electrophoresis and a cell-proliferation bioassay. Degradation of 125I-IL-6 by plasma membranes was completely prevented by the serine-protease inhibitor diisopropyl fluorophosphate, but was only partially impaired by alpha 1-protease inhibitor and antibody against cathepsin G. A similar incubation of 125I-IL-6 with cathepsin G purified from U937 cells caused hydrolysis of the cytokine into similar inactive 8-kDa fragments, whereas incubation with purified U937 cell elastase failed to degrade the peptide. These findings indicate that U937 cells hydrolyze IL-6 using cell-associated serine-protease activity and that cathepsin G partially participates in this degradation. Prolonged incubation of 8-kDa 125I-IL-6 fragments with purified U937 plasma membranes, led to a complete loss of IL-6 activity related to the transformation of the 8-kDa forms into a higher-molecular-mass complex (16 kDa). This complex was stable in SDS and 2-mercaptoethanol at 100 degrees C and was not dissociated by hydroxylamine treatment, indicating the formation of a covalent non-ester bond between the 8-kDa 125I-IL-6-derived peptide and an undetermined acceptor. An initial oxidative treatment of 125I-IL-6 partially prevented complex formation, suggesting the presence of one or more oxidizable methionine residues at the binding site of 8-kDa 125I-IL-6 peptide. The kinetics of complex formation (time dependence and plasma-membrane-concentration dependence), as well as its inhibition by a specific inhibitor of N-amino-peptidase activity, bestatin, suggest the participation of peptidyl-transferase activity in complex formation. Finally, a plasma-membrane fraction, corresponding to a molecular mass > or = 30 kDa, was able to convert the 8-kDa 125I-IL-6 forms into the 125I-labeled 16-kDa complex, suggesting that a > or = 30-kDa peptidyl-transferase enzyme catalyzes the reaction and provides the 125I-labeled 16-kDa peptide by dimerization of 8-kDa 125I-IL-6-derived intermediates. Further identification of the plasma-membrane-associated peptidyl transferase as a regulator of IL-6 proteolysis may be of physiological relevance for the control of IL-6 biological activity.

Aminopeptidases↗
PubMed1993

Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis.

During mitosis, several types of intermediate-sized filaments (IFs) undergo an extensive remodelling in response to phosphorylation by cdc 2 and other protein kinases. However, unlike the nuclear lamins, the cytoplasmic IFs do not seem to follow a fixed disassembly stereotype and often retain their physical continuity without depolymerizing into soluble subunits. To investigate potential interactions between mitotically modified IFs and other cellular structures, we have examined prometaphase-arrested cells expressing the IF protein vimentin. We demonstrate here that vimentin filaments associate in situ and co-fractionate with a distinct population of mitotic vesicles. These vesicles carry on their surfaces nuclear lamin B, the inner nuclear membrane protein p58, and wheat germ agglutinin (WGA)-binding proteins. Consistent with a tight interaction between the IFs and the mitotic membranes, vimentin, nuclear lamin B, and a 180-kD WGA-binding protein are co-isolated when whole mitotic homogenates are incubated with anti-vimentin or anti-lamin B antibodies immobilized on magnetic beads. The vimentin-associated vesicles are essentially depleted of ER, Golgi and endosomal membrane proteins. The interaction of vimentin with lamin B-carrying membranes depends on phosphorylation and is weakened by dephosphorylation during nuclear reassembly in vitro. These observations reveal a novel interaction between IFs and cellular membranes and further suggest that the vimentin filaments may serve as a transient docking site for inner nuclear membrane vesicles during mitosis.

Animals↗