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The distribution of fibronectin in normal and regenerating skeletal muscle (the latter caused by autotransplantation) was investigated by means of indirect immunofluorescent technique. Normal myofibers exhibited a thin, continuous pericellular (endomysium) fibronectin distribution; however, their sarcoplasm was devoid of fibronectin. After autotransplantation, the skeletal muscle fibers underwent a process of degeneration that was followed by regeneration from the premyogenic satellite cells. These cells multiplied, fused to form myotubes, and matured into new myofibers. A decrease and an eventual loss of endomysial fibronectin was seen in the degenerating myofibers. At the same time, fibronectin appeared in the sarcoplasm. No significant fibronectin was expressed in the myogenic zone until the formation of myotubes which possessed a complete, circular fibronectin ring. The sarcoplasm of the myotubes lacked fibronectin. Since fibronectin is a component of basement membrane of several tissues, its disappearance and reappearance can be used to follow the fate of basement membrane. We conclude that fibronectin may not be essential for early myogenesis and that regenerated myotubes form an entirely new or at least certain new molecular components of their basement membrane. The present muscle autotransplantation model can be used to further study the role of fibronectin during myogenesis and cell transformation in vivo.
Anat Rec 1982 Nov
PMID:Distribution of fibronectin in normal and regenerating skeletal muscle. 676 Jul 47

The distribution of the glycoprotein, fibronectin, within the cranial region of stage 8--16 chick embryos was examined by indirect immunofluorescence using paraffin sections exposed to affinity-purified rabbit anti-human CIG and FITC-conjugated goat anti-rabbit immunoglobulins. Fluorescence was present within the matrix surrounding the cranial mesenchyme, along the basal surfaces of all epithelia, and surrounding the notochord at all stages. Fluorescence associated with the floor of the foregut was particularly intense. The fluorescent layers beneath the ectoderm and endoderm of the oral (oropharyngeal) membrane at stage 8 merged into a single, continuous, intensely fluorescent line as the extracellular space within the oral membrane narrowed during stages 9--12. This line of uniform fluorescence parallels the previously described histological reorganization of the extracellular compartment of the oral membrane, but the ultrastructural localization of this fluorescent material remains unknown. Fluorescence was also intense beneath the foregut endoderm in the presumptive cardiac region caudal to the oral membrane and was continuous with strands of fluorescent material extending into the matrix of the dorsal mesocardium and cardiac jelly of the developing tubular heart. These observations indicate that the extracellular matrix associated with the floor of the entire foregut contains fibronectin during stages encompassing the formation and rupture of the oral membrane. The presence of fibronectin within the oral membrane and dorsal mesocardium, as well as between Rathke's pouch and infundibulum and within the closing plates between ectodermal clefts and endodermal pouches, is consistent with the possibility that this glycoprotein may play a role in adhesion at these sites.
Anat Rec 1980 Dec
PMID:Indirect immunofluorescent staining of fibronectin associated with the floor of the foregut during formation and rupture of the oral membrane in the chick embryo. 701 Oct 98

The cysteine endopeptidase cathepsin B (CB) can degrade basement membrane (BM) proteins (such as laminin, type IV collagen, and fibronectin) at both acid and neutral pHs suggesting that CB has a role in tumor invasion and distant metastasis. The distribution and intensity of CB protein localization vary in normal prostate, benign prostatic hyperplasia (BPH), and neoplastic prostate. These considerations have led us to examine whether the distribution of CB localization in malignant and normal cells is due to storage or active synthesis of CB. In the present study, we examined the localization patterns of CB at the mRNA level in normal prostate, BPH, and well to moderately differentiated neoplastic prostate, focusing on invasive groups of cells and invasive edges of malignant tumors. We used a 25-base biotinylated oligonucleotide CB cDNA "sense" probe to localize CB message in prostate samples obtained from radical prostatectomies. We have determined that CB is actively synthesized by the epithelia of normal, hyperplastic, and neoplastic prostate including some invasive cells in the invasive edges. In both normal and BPH, CB mRNA was localized predominantly in acinar basal cells with some localization in cuboidal/columnar cells. In contrast, in neoplastic prostate, CB mRNA was localized predominantly in columnar cells and in groups of invasive cells and invasive edges. Thus, in malignant prostate the predominant cell types expressing CB differed from those of the normal prostate and BPH. Analysis of CB mRNA localizations indicated a heterogeneity in staining distribution in prostate cancer with some invasive groups of cells and invasive edges exhibiting CB mRNA and others exhibiting little or no reaction products.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1993 Feb
PMID:Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. 767 71

The neovascularization of the rabbit phallus at ages between prenatal days 15 and 21 was investigated by light- and electron microscopy, computer-aided light microscopic reconstruction, and immunocytochemistry. The phalli are embedded by an abundance of mesenchymal cells, which are in contact with the neighboring ones or with the endothelial lining of growing capillaries. They often form solid cell cords that eventually make contact with the growing capillaries. The computer-aided reconstruction of the serial light micrographs reveals that these cell cords are involved in connecting the adjacent capillaries. The incorporation of such mesenchymal cell projections into the endothelial lining, occasionally conjugated with simple attachment devices, is frequently observed by transmission and scanning electron microscopy. The contact areas between the mesenchymal and endothelial cells show immunoreactions of fibronectin. These results indicate the successive transformation of mesenchymal cells to endothelial cells of the growing capillaries. As endothelial cells of the growing capillaries show mitotic proliferation, such vasoformative mesenchymal cells seem to be involved in the acceleration of the neocapillarization of the rabbit phallus. Fibronectin actively produced in the mesenchymal cells may participate in their migration and the mechanical linkage with the endothelial cells.
Anat Rec 1994 Jan
PMID:Role of mesenchymal cells in the neovascularization of the rabbit phallus. 811 87

Using an agarose gel culture system, the response of adult human chondrocytes to prolonged exposure of ascorbic acid was evaluated using histochemical, immunocytochemical and morphological techniques. The response of these cells to ascorbic acid was different from those previously reported in the literature. Many chondrocytes branched within the agarose gel with continued exposure to ascorbic acid while other chondrocytes maintained a round configuration typical of chondrocytes in vivo. Fibronectin and type I collagen were closely associated with the cell processes of the branching cells. Type II collagen and an alcian blue-staining matrix were associated with the rounded cells but not with the branched cells. These data suggest that the chondrocytes are able to express both dedifferentiated and redifferentiated phenotypes with ascorbic acid under these culture conditions. In addition, human chondrocytes were cultured in a collagen gel and began branching within 1 hour of culture. It is possible that an accumulation of type I collagen in the pericellular matrix of ascorbic acid treated cultures may enhance and explain the branching seen in these cultures. Studies by others have indicated that ascorbic acid may enhance, reduce, and/or modify the cartilage matrices produced by chondrocytes. These controversial reports in the literature are presumably due to variations between species and the culture methods employed.
Anat Rec 1994 Jan
PMID:Prolonged exposure of human chondrocytes to ascorbic acid modifies cellular behavior in an agarose gel. 811 89

The involvement of fibronectin in adhesion and migration of individual mesoblast cells during chicken gastrulation was examined after microinjection of functional and nonfunctional antifibronectin antibodies in the blastoderm during the period of rapid migration of mesoblast cells. The injection of affinity-purified polyclonal antihuman fibronectin antibody (total IgG or Fab fragment) or of monoclonal antichicken cellular fibronectin caused a thickening of the primitive streak, which was composed of loosely connected cells. This effect was most evident at the level of Hensen's node, and very few mesoblast cells were observed migrating in the space between upper layer and deep layer. The obvious explanation of this effect was that the de-epithelialization of upper layer cells persisted in the presence of antibodies, but ingressed cells failed to emigrate from the primitive streak. Immunostaining of microinjected antibodies showed binding to the basement membrane, to the cell surface of mesoblast cells that had migrated before microinjection occurred, and to the cell surface of deep layer cells. Cells that ingressed and detached in the course of reincubation of the embryo possessed little immunolabelling along their cell surface. The results suggest that the failure of ingressed cells to emigrate from the primitive streak and to form mesoblast was due (1) to alterations in adhesion between newly ingressed primitive streak cells, which had the ability to detach but possessed relatively little fibronectin along their cell surfaces and a small number of cell protrusions, and (2) probably to a lack of adhesion of detached cells to the basement membrane, which was blocked by the presence of antifibronectin antibodies. We conclude that the presence of fibronectin in the basement membrane is required for emigration of ingressed cells and migration of mesoblast cells to occur. Once migration has commenced, fibronectin is also deposited along the cell surface of migrating cells, a factor that may increase their mutual adhesion.
Anat Rec 1993 Aug
PMID:Microinjection of antifibronectin antibodies in the chicken blastoderm: inhibition of mesoblast cell migration but not of cell ingression at the primitive streak. 837 92

Immunolocalization of laminin, fibronectin, and type IV collagen was examined during early morphogenetic shape changes of the avian inner ear and eye. The ear was studied from formation of the otic placode to invagination of the otic pit and the eye from the optic vesicle stage to formation of an optic cup. Distribution and intensity of immunoreactivity were compared in the two organ primordia and in adjacent epithelial layers. Laminin formed a continuous layer at the basal surface of the otic ectoderm and adjacent neural tube at all stages. The basal surfaces of the optic and lens epithelia also were continuously covered with laminin throughout development. The otic placode became attached to the neural ectoderm through a single layer of fibronectin and collagen IV between the layers of laminin. The ring-like attachment between the edges of the optic cup and lens primordium had the same structure. In addition, the central regions of the optic and lens primordia were attached by fibrils containing type IV collagen, whereas finer strands containing fibronectin and laminin also connected the otic epithelium and neural tube. The results are discussed in terms of models of invagination for the two primordia.
Anat Rec 1993 Mar
PMID:Immunolocalization of basal lamina components during development of chick otic and optic primordia. 843 Sep 14

We have developed a co-culture system suited for the study of epithelial-mesenchymal interactions in the human fetal small intestine. As the epithelial component of this model, we used the human intestinal cell line Caco-2 that is unique in its property to differentiate in vitro into a mature fetal enterocyte-like cell type. A sheet of human intestinal mesenchymal cells, which we derived from an 18-week-old fetus, was used as mesenchymal element. Expression and distribution of cell-specific markers (cytokeratin 18 and dipeptidyl peptidase IV), major basement membrane components, and beta 1 integrins were analyzed. In 14-day co-cultures, Caco-2 cells formed a cytokeratin 18-positive epithelial-like sheet covering the vimentin-positive HIM cell layers. As assessed by brush border dipeptidyl peptidase IV expression, co-cultured Caco-2 cells achieved cytodifferentiation as when cultured on plastic. A complete deposition of all known major human fetal intestinal basement membrane components occurred at the Caco-2/HIM interface. Type IV collagen and tenascin were produced from the mesenchymal compartment, whereas laminin and fibronectin were contributed by both cell types. Interestingly, synthesis and deposition of basement membrane heparan sulfate proteoglycan were exclusively observed in co-cultures, suggesting modulation of epithelial expression of this molecule by HIM cells. Finally, we observed that epithelial integrin-beta 1 chains redistributed at the basal domain of co-cultured Caco-2 cells. Taken together, these observations indicate that the Caco-2/HIM co-culture model is a valuable system to study in vitro human basement membrane formation in the context of intestinal epithelial-mesenchymal interactions.
Anat Rec 1993 Apr
PMID:Basement membrane formation and re-distribution of the beta 1 integrins in a human intestinal co-culture system. 846 88

Osteopontin (OPN), a noncollagenous, extracellular matrix sialoprotein found at relatively high levels in both normal and pathological mineralized tissues, is expressed by tissue-specific cells in bone, calcified cartilage, and teeth. On the other hand, a hallmark of OPN expression in pathologically mineralizing tissue, and in other soft tissues experiencing a more generalized type of necrotic injury, is the production of OPN by macrophages at the lesion site. In the present study, we have localized OPN and other noncollagenous proteins by ultrastructural colloidal-gold immunocytochemistry using a rat model in which mineralized tissue defects are surgically created in mandibular bone and teeth. The healing response was examined by immunocytochemistry and transmission electron microscopy at 10 min, 3 days and 7 days post-surgery using antibodies against OPN, bone sialoprotein, osteocalcin, bone acidic glycoprotein-75, fibronectin, and amelogenin. Whereas most of these proteins were characteristically distributed within their respective extracellular matrices as described previously, OPN was additionally observed to accumulate as a lamina limitans at surgically exposed bone and tooth surfaces, as well as at the surface of particulate, mineralized tissue debris. Intracellular labeling of the Golgi apparatus and secretory granules of macrophages at the lesion site demonstrated that OPN production by macrophages was a prominent secretory event of the inflammatory response during wound healing in mineralized tissues. Pseudopodal and lamellipodal cytoplasmic extensions of macrophages were observed in direct contact with the OPN-containing lamina limitans at these surfaces. Particulate, calcified debris internalized by macrophages also displayed a prominent surface "coating" of OPN. In conclusion, our interpretation of the present data is that OPN secreted by macrophages may serve as a macrophage adhesion protein, and where concentrated at the surface of small particulate, mineralized tissue debris, may act as an opsonin, thereby facilitating cell adhesion and phagocytosis by macrophages, a process likely mediated by integrin-binding, signal transduction, and cytoskeletal restructuring.
Anat Rec 1996 Jun
PMID:Secretion of Osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: a potential requirement for macrophage adhesion and phagocytosis. 876 75

The aim of this work was to study the effect of a dose of 150 microCi 131I on the barrier properties of the thyroid epithelium in pregnant female rats. Thirty-five female Wistar rats were divided into a control and four experimental groups (each distinguished by the time of 131I injection: group I--no less then 12 days before mating; groups II, III, and IV--on 5th, 10th, and 16th days of gestation, respectively). The thyroid glands were fixed in Bouin's fluid, embedded in paraffin, and stained immunohistochemically for thyroglobulin and fibronectin. In group IV the appearance of follicles with fibronectin-positive colloid demonstrates the penetration of blood plasma into the follicular lumen. There are more fibronectin positive follicles in group III. Regardless of the nature of the follicles' contents, numerous thyrocytes with an intensive fibronectin positive reaction begin to appear in the follicles. In group II the number of fibronectin positive follicles and thyrocytes is clearly reduced, and in group I only a few remain. In group IV there is a noticeable reduction in the quantity of colloid inside the follicles and often an absence of any thyroglobulin positive reaction. There are thyrocytes in which thyroglobulin positive granules localized in the basal zone. There is thyroglobulin positive staining in the stroma and blood vessels. In group II thyroglobulin is no longer found in the stroma. Small doses of 131I provoke a serious breakdown in the thyroid epithelium's barrier properties, although these changes are of a transient nature. The central zone of the thyroid gland reacts more actively and dynamically to exposure to radioactive iodine than the peripheral zone.
Anat Rec 1998 12
PMID:Immunohistochemical study of fibronectin and thyroglobulin in the thyroid gland of female rats after exposure to radioactive iodine. 984 10


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