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1.
Proc Natl Acad Sci U S A ; 111(35): 12689-92, 2014 Sep 02.
Article in English | MEDLINE | ID: mdl-25136108

ABSTRACT

Volcanism is a substantial process during crustal growth on planetary bodies and well documented to have occurred in the early Solar System from the recognition of numerous basaltic meteorites. Considering the ureilite parent body (UPB), the compositions of magmas that formed a potential UPB crust and were complementary to the ultramafic ureilite mantle rocks are poorly constrained. Among the Almahata Sitta meteorites, a unique trachyandesite lava (with an oxygen isotope composition identical to that of common ureilites) documents the presence of volatile- and SiO2-rich magmas on the UPB. The magma was extracted at low degrees of disequilibrium partial melting of the UPB mantle. This trachyandesite extends the range of known ancient volcanic, crust-forming rocks and documents that volcanic rocks, similar in composition to trachyandesites on Earth, also formed on small planetary bodies ∼ 4.56 billion years ago. It also extends the volcanic activity on the UPB by ∼ 1 million years (Ma) and thus constrains the time of disruption of the body to later than 6.5 Ma after the formation of Ca-Al-rich inclusions.

2.
Cell Tissue Res ; 310(1): 19-29, 2002 Oct.
Article in English | MEDLINE | ID: mdl-12242480

ABSTRACT

Previous studies have indicated the importance of basement membrane components both for cellular differentiation in general and for the barrier properties of cerebral microvascular endothelial cells in particular. Therefore, we have examined the expression of basement membrane proteins in primary capillary endothelial cell cultures from adult porcine brain. By indirect immunofluorescence, we could detect type IV collagen, fibronectin, and laminin both in vivo (basal lamina of cerebral capillaries) and in vitro (primary culture of cerebral capillary endothelial cells). In culture, these proteins were secreted at the subcellular matrix. Moreover, the interaction between basement membrane constituents and cerebral capillary endothelial cells was studied in adhesion assays. Type IV collagen, fibronectin, and laminin proved to be good adhesive substrata for these cells. Although the number of adherent cells did not differ significantly between the individual proteins, spreading on fibronectin was more pronounced than on type IV collagen or laminin. Our results suggest that type IV collagen, fibronectin, and laminin are not only major components of the cerebral microvascular basal lamina, but also assemble into a protein network, which resembles basement membrane, in cerebral capillary endothelial cell cultures.


Subject(s)
Basement Membrane/metabolism , Blood-Brain Barrier/physiology , Cell Adhesion Molecules/metabolism , Cell Adhesion/physiology , Cerebral Cortex/blood supply , Endothelium, Vascular/metabolism , Animals , Basement Membrane/cytology , Biological Assay , Cells, Cultured , Collagen Type IV/metabolism , Endothelium, Vascular/cytology , Extracellular Matrix/metabolism , Extracellular Matrix/ultrastructure , Fibronectins/metabolism , Fluorescent Antibody Technique , Laminin/metabolism , Sus scrofa
3.
Biochem Biophys Res Commun ; 293(1): 86-92, 2002 Apr 26.
Article in English | MEDLINE | ID: mdl-12054567

ABSTRACT

Thrombospondin-1 (TSP-1) is an extracellular glycoprotein that is involved in a variety of physiological processes such as tumor cell adhesion, invasion, and metastasis. It has been hypothesized that TSP-1 provides an adhesive matrix for osteosarcoma cells. Here we present data showing that TSP-1 can promote cell substrate adhesion to U2OS and SAOS cells through the alpha 4 beta 1 integrin. The dose-dependent adhesion to TSP-1 was inhibited by anti-integrin antibodies directed against the alpha 4 or beta 1 subunit, but not by control antibodies against other integrins. To localize the potential alpha 4 beta 1-binding site within the TSP-1 molecule, the protein was subjected to limited proteolysis with chymotrypsin in the absence of calcium. The stable 70-kDa core fragment produced under these conditions promoted alpha 4 beta 1-dependent osteosarcoma cell adhesion in a manner similar to that of the intact protein. Moreover adhesion experiments with neutralizing antibodies revealed that the adhesion was totally dependent on the alpha 4 beta 1 interaction. Further blocking experiments with potential inhibitory peptides revealed that the alpha 4 beta 1-mediated adhesion was not influenced by peptides containing the RGD sequence. Attachment to the 70-kDa fragment was strongly inhibited by the CS-1 peptide, which represents the most active recognition domain for alpha 4 beta 1 integrin in fibronectin. The present data provide evidence that TSP-1 contains an alpha 4 beta 1 integrin-binding site within the 70-kDa core region.


Subject(s)
Cell Adhesion/physiology , Integrins/physiology , Receptors, Lymphocyte Homing/physiology , Thrombospondin 1/physiology , Bone Neoplasms , Cell Adhesion/drug effects , Humans , Integrin alpha4beta1 , Osteosarcoma , Peptide Fragments/pharmacology , Thrombospondin 1/pharmacology , Tumor Cells, Cultured
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