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Fibroblasts cultured within free-floating collagen gels can bind to and reorganize the surrounding collagen fibrils into a more dense and compact arrangement. Collagen gel contraction provides an in vitro model for studying fibroblast-collagen interactions important in wound healing, fibrosis, scar contraction, and connective tissue morphogenesis. We have assessed the role of fibronectin and its interaction with the alpha 5 beta 1 "high affinity" fibronectin-specific integrin receptor in collagen gel contraction. A variety of agents, which specifically inhibit fibronectin-alpha 5 beta 1 interactions, were tested for their abilities to inhibit fibroblast-mediated collagen gel contraction. These included anti-alpha 5 beta 1 monoclonal antibodies, the synthetic peptide GRGDSP, the cell adhesive fragment of fibronectin, and an antibody against the cell adhesive region of fibronectin. None of these agents inhibited collagen gel contraction. Therefore, it is concluded that fibronectin-alpha 5 beta 1 interactions are not necessary for collagen gel contraction. However, collagen gel contraction is dependent on a member or members of the beta 1 subfamily of integrin matrix receptors. A polyclonal antiserum and a monoclonal antibody, both directed against the beta 1 subunit of integrin matrix receptors, inhibited the spreading of fibroblasts in the collagen gel and inhibited collagen gel contraction. This study demonstrates that fibroblast-mediated collagen gel contraction is independent of fibronectin-alpha 5 beta 1 interactions but dependent on an interaction of beta 1 integrin matrix receptors with collagen fibers.
Anat Rec 1992 Oct
PMID:Fibroblast-mediated collagen gel contraction does not require fibronectin-alpha 5 beta 1 integrin interaction. 141 2

Collagen fibrils with a symmetric banding pattern, an as yet overlooked component of the extracellular matrix, were found in the reticular layer of the basement membrane of human sebaceous glands. In longitudinal sections this newly described banding pattern is D-periodic (D = 67 nm) resembling the period length of native type collagen fibrils. In cross sections the symmetrically banded fibrils are irregularly outlined. The period length and the symmetric banding pattern led to the assumption that collagen molecules are staggered by the distance D, similar to native type collagen fibrils, but are arranged antiparallel. This hypothesis was tested by antiparallel superposing transparent photocopies of native type fibrils. In addition, schematic drawings of the cross striation pattern of native type fibrils were superposed in reverse directions by means of computerized image-manipulation. A model of molecular alignment was evolved from these experiments, which is characterized by two features: 1) pairs of antiparallel collagen molecules are D-staggered and 2) the two molecules of a pair are slightly shifted from precise register. The proposed model is the only one correlating with the data obtained from direct measurements on symmetrically cross striated fibrils. The fibrils described in the present study represent a supramolecular aggregate of collagen previously not observed in vivo.
Anat Rec 1992 Jan
PMID:Symmetrically banded collagen fibrils: observations on a new cross striation pattern in vivo. 153 64

This manuscript considers certain aspects of mineral deposition in bone and other vertebrate calcifying tissues in order to examine physical, chemical, and biological factors important in the mineralization process. The paper in a discussion format principally presents a new data and the formulation of concepts based on such data as well as a summary of background material as necessary review. Mineralization is found to occur at spatially independent sites throughout the organic extracellular tissue matrices. Matrix vesicles and collagen fibrils each may serve as independent nucleation centers for mineral with vesicle mineralization being local and collagen mineralization dominating the tissues as a whole. Collagen fibril organization is suggested to be such that hole zones are aligned in three dimensions, creating extensive channels for mineral accommodation. Nucleation occurs initially in hole zones and crystal growth leads to the development of plate-like mineral particles whose orientation, disposition, and sizes within fibrils are detailed. Effects of diffusion, crystallinity, and critical nucleation and growth events are described with respect to their influence on mineral deposition in bulk and local regions of tissue matrices.
Anat Rec 1991 Aug
PMID:A contribution with review to the description of mineralization of bone and other calcified tissues in vivo. 192 50

Surgical ablation of the cardiac neural crest from the chicken embryo results in persistent truncus arteriosus (PTA) and a change in the elastic laminae of the great vessels, wherein elastin and the elastin microfibril show significant spatial disorder. The purpose of this study was to test the hypothesis that the interstitial collagens would also be disordered in the elastic laminae of chicken embryos with PTA. The birefringence characteristics of interstitial collagen were examined to evaluate spatial ordering. The results showed that collagen in the elastic laminae assumed an orderly configuration of well-defined fiber bundles in the great vessel walls of control embryos, whereas vessels from embryos with PTA lacked any distinct spatial order. Collagens type I and III were localized in the vessel walls. Type III collagen was the principal collagen of the elastic laminae, but was absent from the intima of all vessels. In the elastic laminae of vessels from control embryos, collagen type III showed well-defined fiber bundles whereas embryos with PTA had diffuse collagen type III in poorly defined laminae that were not separated by discrete layers of smooth muscle cells. Collagen type I was a minor component of the elastic laminae but formed robust pericellular fiber bundles throughout the media and intima. Collagen type I fibers appeared to be coarsened and less uniform in the vessels from embryos with PTA.
Anat Rec 1991 Jan
PMID:Spatial disorder of collagens in the great vessels, associated with congenital heart defects. 199 77

The organization of the network of collagen fibers of rabbit Peyer's patches was examined by scanning electron microscopy (SEM) in alkali-water macerated tissues. The relationship between this network and the reticular cells within it was further studied by SEM of ultrasonicated tissues. Collagen fibrils (about 60 nm in diameter) formed collagen fibers or sheets. There were sheets of collagen fibrils with numerous pores beneath the patch dome epithelium. Within the patches, collagen fibers repeatedly divided and fused, forming the reticular network. The reticular network within the follicle was looser than within the dome, the corona, or the interfollicular area. The latter three compartments showed similar structures and consisted of numerous intercommunicating small subcompartments. Reticular cells were in contact with groups of free cells lodged in these subcompartments within the reticular network. Reticular cell processes with numerous fenestrations embraced not only collage fibers forming the reticular network, but also sheaths of collagen fibers of blood and lymphatic vessels. Sheaths of collagen fibers of high endothelial venules and lymphatic vessels were also fenestrated, indicating the sites through which lymphocytes and other free cells migrate. These results indicate that the reticular network of Peyer's patches is organized so as to facilitate migration and lodging of free cells and thus facilitate antigen-to-cell and cell-to-cell interactions during an immune response. The naked areas on the collagen fibers seem to provide a scaffolding for free cells during their migration.
Anat Rec 1991 Feb
PMID:Organization of the reticular network of rabbit Peyer's patches. 201 12

Although the artery wall consists of three distinct layers, only the structures of the intima and media have been well characterized. The adventitia has generally been overlooked. Our examination focused on the organization of elastin and collagen which are the major components of this tunic. Canine infrarenal aortas were excised, stretched to their in vivo length, then pressure fixed in formalin. Transverse, longitudinal, and frontal sections were prepared with specific elastin and collagen stains. Areas of adventitia in these sections were examined with LM, and interconnections between collagen and elastin were photographed at various magnifications. Subsequently, the slides were fractured for attachment to SEM stubs, and the coverslips were demounted. The identical areas were then examined with SEM using the LM micrographs as a guide to identify elastin and collagen. Whole mount aortic ring preparations were digested in formic acid for 72 and 96 h at 45 degrees C to confirm adventitial elastin architecture. The adventitia was organized in alternating lamellae of collagen and elastin. The elastin lamellae consisted of continuous sheets of elastin with a longitudinal fibrillar substructure. Finer circumferential elastin fibers were also identified. These attached to both longitudinal elastin and adjacent collagen lamellae. Collagen lamellae were arranged in broad corrugated bands of fibrils. The unique architecture of the adventitia may explain some of the visco-elastic properties of the aorta in both normal and pathologic states.
Anat Rec 1991 May
PMID:The architecture of adventitial elastin in the canine infrarenal aorta. 206 31

The extracellular matrix (ECM) of first-trimester human decidua was examined with indirect immunofluorescence using affinity-purified antibodies to human collagen types I, III, IV, V, laminin, and fibronectin. In addition, the validity of the classification "mesenchymal-epithelioid" for differentiated decidual cells was addressed using antibodies to the intermediate filament proteins, vimentin, a mesenchymal marker, and keratin, an epithelial marker. Biosynthesis of extracellular matrix components was examined by radiolabeling of decidual explants in culture with 3H-proline, followed by immunoprecipitations of synthesized proteins with collagen type-specific antibodies. Immunofluorescence showed decidual cells are embedded in an extensive network of collagen types I and III, and intracytoplasmic staining suggested synthesis of these collagens by the decidual cells. Collagen type IV and laminin localized in the external lamina which surrounds the differentiated decidual cell, and some fluorescence was evident in the peripheral cytoplasm. Immunoreactive collagen type V was observed in close association with the external lamina and in the peridecidual matrix. Fibronectin localized throughout the decidual ECM and in fibrillar and punctuate patterns in the decidual cell cytoplasm. Differentiated decidual cells retained a "mesenchymal" intermediate filament cytoskeleton containing an abundance of vimentin filaments, but very few, if any, keratin filaments. Collagen types I, III, V, and to a lesser extent, IV, were immunoprecipitated from the medium of decidual explants after 24 hours of culture, demonstrating in vitro synthesis and secretion of these collagens by first trimester human decidua.
Anat Rec 1987 Aug
PMID:Immunolocalization of extracellular matrix proteins and collagen synthesis in first-trimester human decidua. 244 38

Collagen fibrils were present within membrane-bound vacuoles in the cytoplasm of mouse decidual cells on the 7th day of pregnancy. The space between the vacuole membranes and the fibrils was narrow and frequently filled with a granular electron-dense material. The loss of banding of the collagen fibrils, their association with lysosomelike bodies, and the demonstration of acid phosphatase activity in the vacuoles indicate that the fibrils were internalized by the decidual cells and were being digested. It is suggested that phagocytosis of collagen is a mechanism of remodeling of the mouse decidua.
Anat Rec 1989 Oct
PMID:Phagocytosis of collagen by mouse decidual cells. 281 34

The localization of collagenolytic activity within the tissue compartments of the mouse uterus was investigated during postpartum involution. The rate of collagenase activity was measured by analysis of tissue levels of hydroxyproline from the day of parturition to the 10th postpartum day. Collagen bonding was analyzed by viewing birefringence induced by the picrosirius red-binding technique. An attempt was made to interrelate quantitative analysis with the histologic distribution of collagen during postpartum days 1-10. Histologic and quantitative evidence indicated the following: 1) The collagenous compartments of the endometrium and myometrium differ in their response to the postpartum rise in collagenase activity; collagen degradation occurs primarily in the endometrium, that is, the myometrial collagen remains, but much of the endometrial collagen is removed. 2) Endometrial collagen is degraded particularly in the immediate subluminal compartment.
Anat Rec 1988 Feb
PMID:Removal of collagen bundles in murine uterus during postpartum involution. 335 57

MDCK (Madin-Darby canine kidney) cells were cultured either dispersed within hydrated collagen gel (HCG) or seeded atop a collagen substrate and then immediately overlaid with HCG. Individual cells exhibited clonal growth in three dimensions to form spherical cysts made up of a simple epithelium enclosing a fluid-filled lumen. The cells of MDCK cysts were polarized with the basolateral surface in contact with the collagen gel and the apical surface bordering the lumen. The ultrastructure of MDCK cysts showed similarities to distal nephron. The cells bore apical microvilli and solitary cilia and had occluding junctions and a simple basolateral surface. MDCK cysts increased in size (greater than 800 microns diameter) with continued culture. MDCK cysts grown between layers of HCG were stripped free of the overlying collagen to give direct access to basolateral surface membrane. Unlike monolayer culture, morphogenetic clonal growth of cell line MDCK produces a polarized cell population with a true lumenal and basolateral surface. Collagen-gel-cultured MDCK cysts provide an easily manipulable in vitro cell system that may offer unique advantages for the study of renal cell structure and function.
Anat Rec 1987 Mar
PMID:Morphogenetic clonal growth of kidney epithelial cell line MDCK. 357 40


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