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At least 127 records · Page 7Linked to original sources
PubMed1995

Osteogenesis by human osteoblastic cells in diffusion chamber in vivo.

Osteogenic potential of osteoblastic cells isolated from human bone was evaluated by a diffusion chamber method. Cells placed in diffusion chambers were implanted intraperitoneally into the athymic mice. The diffusion chambers cultured in vivo were harvested and examined after implantation for 6-8 weeks. The content of the chamber was proved by a soft roentogenogram to contain the radioopaque area. Light microscopic study revealed that this area was made up of bone-like nodule. Within the diffusion chambers, the cell layers were observed alongside the interior surface of the membrane filters, and mineralized nodules were formed among the cell layers. The mineralized nodules were confirmed by staining with the von Kossa technique for calcium mineral deposits. In electron microscopic study, the osteoblastic cells had a relatively large nuclei, and an abundant rough endoplasmic reticulum produced numerous extracellular matrix. In the bone-like nodules, the osteoblastic cells were surrounded by a heavily mineralized matrix with nonmineralized matrix separating the osteoblastic cells from the mineralized matrix. The mineralized matrix contained well-banded collagen fibrils. Matrix vesicles and collagen fibrils which were closely associated with mineral deposition were observed at the mineralizing front. These results together with our previous report [13] indicate that isolated human osteoblastic cells possessed osteogenic potential in vivo as well as mineralization activity in vitro.

Animals↗
PubMed1989

Proteins of Newcastle disease virus envelope: interaction between the outer hemagglutinin-neuraminidase glycoprotein and the inner non-glycosylated matrix protein.

Using linear sucrose-density ultracentrifugation analysis of Triton-solubilized Newcastle Disease Virus envelopes, we have evidenced, for the first time, the existence of interactions between the outer hemagglutinin-neuraminidase transmembrane glycoprotein and the inner non-glycosylated peripheral matrix protein. Such interactions seem to be electrostatic. These conclusions are based on the behavior of both proteins at different ionic strengths. When in low ionic strength buffer, hemagglutinin-neuraminidase and matrix proteins band together in the sucrose gradient, whereas at high ionic strength both proteins band at different rates in the gradient. The behavior of the inner matrix protein in our conditions was the expected one for a peripheral protein. The results of these 'in vitro' studies are also discussed in terms of the possible 'in vivo' role of such interactions.

Animals↗
PubMed1993

Immunological characterization of lamins in the nuclear matrix of onion cells.

We have used polyclonal and monoclonal antibodies against different lamins from vertebrates, and the IFA antibody recognizing all kinds of intermediate filament proteins, to investigate the lamins of the nuclear matrix of Allium cepa meristematic root cells. All the antibodies react in the onion nuclear matrix with bands in the range of 60-65 kDa, which are enriched in the nuclear matrix after urea extraction, and do not crossreact with other antibodies recognizing intermediate filaments in plants (AFB, anti-vimentin and MAC 322), ruling out crossreaction with contaminating intermediate filaments of cytoplasmic bundles. In 2-D blots the chicken anti-lamin serum reacts with one spot at 65 kDa and pI 6.8 and the anti B-type lamin antibodies with another one at 64 kDa and pI 5.75. Both crossreact with IFA. The lamin is localized at the nuclear periphery and the lamina by indirect immunofluorescence. Immunogold labelling of nuclear matrix sections reveals that the protein is not only associated with the lamina, but also with the internal matrix. Taken together these results reveal that higher plants, which do not possess an organized network of cytoplasmic intermediate filaments, nevertheless present a well-organized lamina containing lamins in which at least one of them is immunologically related to vertebrate lamin B. Our data confirm that lamins are very old members of the intermediate filament proteins that have been better conserved in plants during evolution than their cytoplasmic counterparts.

Allium↗
PubMed1986

Purification of erythrocyte band 4.1 and other cytoskeletal components using hydroxyapatite-Ultrogel.

An improved method for purifying erythrocyte band 4.1, the protein which mediates the interaction between spectrin and actin, has been developed. The new procedure, using adsorption chromatography on hydroxylapatite crystals immobilized within a crosslinked agarose gel (HA-Ultrogel), is simple and reproducibly provides a high yield of band 4.1 which is essentially free of protein kinase. Other components eluted from the hydroxylapatite matrix include band 4.9, ankyrin, and a 35,000-Da polypeptide that appears to be glyceraldehyde-3-phosphate dehydrogenase that remains bound to the erythrocyte membrane in 150 mM NaCl.

Actins↗
PubMed2001

Enzymes active in the areas undergoing cartilage resorption during the development of the secondary ossification center in the tibiae of rats aged 0-21 days: II. Two proteinases, gelatinase B and collagenase-3, are implicated in the lysis of collagen fibrils.

In the transformation of the cartilaginous epiphysis into bone, the first indication of change in the surfaces destined for resorption is the cleavage of aggrecan core protein by unidentified matrix metalloproteinases (MMPs) (Lee et al., this issue). In cartilage areas undergoing resorption, the cleavage leaves as superficial, 6-microm-thick band of matrix, referred to as "pre-resorptive layer." This layer harbors G1-fragments of the aggrecan core protein within a framework of collagen-rich fibrils exhibiting various stages of degeneration. Investigation of this layer in every resorption area by gelatin histozymography and TIMP-2 histochemistry demonstrates the presence of an MMP whose histozymographic activity is inhibited by such a low dose of the inhibitor CT1746 as to identify it as gelatinase A or B. Attempts at blocking the histozymographic reactions with neutralizing antibodies capable of inhibiting either gelatinase A or B reveals that only those against gelatinase B do so. Immunostaining of sections with anti-gelatinase B IgG confirms the presence of gelatinase B in every pre-resorptive layer, that is, at the blind end of excavated canals (stage I; 6-day-old rats), at sites along the walls of the forming marrow space (stage II; 7days), at sites within the walls of this space as it becomes the ossification center (stage III; 9 days) and along the wall of the maturing center (stage IV; 10-21 days). We also report the presence of collagenase-3 in precisely the same sites, possibly as active enzyme, but this remains to be proven. Because the results reveal that collagenase-3 is present beside gelatinase B in every pre-resorptive layer and, because these sites exhibit various signs of degradation including fibrillar debris, reduction in fibril number, or overt loss, we propose that gelatinase B and collagenase-3 mediate the lysis of this pre-resorptive layer-most likely through a cooperative attack leading to the disintegration of the collagen fibril framework.

Animals↗