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A crucial part of secondary palate morphogenesis is the movement of the palatal shelves from an initial vertical position on either side of the tongue to a final horizontal one above it to achieve palate closure. The immunocytochemical localization of extracellular matrix (ECM) molecules in the palatal shelf during this remodelling and reorientation revealed the existence of an ECM infrastructure within the mesenchyme. The major components of this infrastructure were collagen III, fibronectin, and hyaluronate (HA). With remodelling, HA's domain within the mesenchyme was expanded, whereas those of fibronectin and collagen III became more circumscribed. The expansion of an HA-rich matrix within the mesenchyme is thought to be crucial for palatal reorientation. The results of this study suggest that, as this expansion occurs, it is modulated by collagen and fibronectin components of the ECM infrastructure. Prior to shelf remodelling, this infrastructure may be anchored by a specialized region of the midoral epithelial-mesenchymal interface and the subjacent mesenchyme which is characterized by the unique distribution of collagen III, fibronectin, and tenascin. The midoral palatal epithelium also may play a role in directing shelf expansion. This epithelial region undergoes changes in cell packing and epithelial cell layering that correlate with shelf remodelling. These changes occur concomitantly with changes in the expression of collagen III, collagen IV, and laminin within the underlying basement membrane. The localization and patterning of tenascin within the developing palate suggests that it not only contributes to the postulated anchoring structure of the midoral epithelial-mesenchymal region, but also plays a role in the determining the fate of the medial edge epithelial cells during the final stage of palate closure.
Anat Rec 1992 Dec
PMID:An extracellular matrix infrastructure provides support for murine secondary palatal shelf remodelling. 128 Sep 22

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

The importance of the extracellular matrix (ECM) in epithelial-mesenchymal interactions in developing organisms is well established. Proteoglycans and interstitial collagens are required for the growth, morphogenesis, and differentiation of epithelial organs and the distribution of these molecules has been described. However, much less is known about other ECM macromolecules in developing epithelial organs. We used confocal microscopy to examine the distribution of laminin, heparan sulfate (BM-1) proteoglycan, fibronectin, and collagen types I, IV, and V, in mouse embryonic salivary glands. Organ rudiments were isolated from gestational day 13 mouse embryos and cultured for 24, 48, or 72 hours. Whole mounts were stained by indirect immunofluorescence and then examined using a Zeiss Laser Scan Microscope. We found that each ECM component examined had a distinct distribution and that the distribution of some molecules varied with culture time. Laminin was mainly restricted to the basement membrane. BM-1 proteoglycan was concentrated in the basement membrane and also formed a fine network throughout the mesenchyme. Type IV collagen was mainly located in the basement membrane of the epithelium, but it was also present throughout the mesenchyme. Type V collagen was distributed throughout the mesenchyme at 24 hours, but at 48 hours was principally located in the basement membrane. Type I collagen was distributed throughout the mesenchyme at all culture times, and accumulated in the clefts and particularly at the epithelial-mesenchymal interface as time in culture increased. Fibronectin was observed throughout the mesenchyme at all times.
Anat Rec 1992 Nov
PMID:Localization of extracellular matrix components in developing mouse salivary glands by confocal microscopy. 144 71

Immunocytochemical techniques were used to study the distribution of fibronectin, type IV collagen (collagen-IV), and laminin in four different stages of mouse blastocyst development. Immunoreactivity for collagen-IV and laminin is present in a granular pattern inside the inner cell mass (ICM) cells in stage 1 blastocysts, while these blastocysts are negative for fibronectin. Fibronectin immunoreactivity appears extracellularly under the trophectoderm (TE) in stage 2 blastocysts, in the form of homogeneously distributed dots, and/or fibrils located preferentially close to cell boundaries. It is followed by the appearance of both collagen-IV and laminin immunoreactivity in patches on the basal side of the TE in stage 3 blastocysts. These patches are initially localized under the central region of TE cells, thus in a location clearly different from that of fibronectin-positive fibrils. As development proceeds the collagen-IV- and laminin-positive patches become larger, covering, by stage 4, an extensive portion of the inner lining of the blastocoel. Fibronectin-positive material is still present in a fibrillar form in stage 3 blastocysts, but is generally reduced to thin strands by stage 4. These results indicate that fibronectin is independent of the mouse blastocyst basement membrane, but may play a transient role in cell adhesion during its deposition. In addition, the results suggest that the ICM plays a major role in the production of collagen-IV and laminin, while the basal surface of TE cells is the primary site of basement membrane assembly.
Anat Rec 1992 Jan
PMID:Basement membrane and fibronectin matrix are distinct entities in the developing mouse blastocyst. 153 59

The generation of tension in granulation tissue undergoing contraction is believed to be a cell-mediated event. In this study we used attached collagen lattices as a model system for studying the cellular mechanisms of tension generation by fibroblasts in an extracellular matrix. Fibroblasts in attached collagen lattices developed stress fibers, surface associated fibronectin fibrils, and a fibronexus-like transmembrane association interconnecting the two structural components. Release of the attached collagen lattice from its points of attachment resulted in a rapid, symmetrical contraction of the collagen lattice. Rapid contraction occurred within the first 10 minutes after release of the lattice from the substratum, with greater than 70% of the contraction occurring within the first 2 minutes. Rapid contraction resulted in a shortening of the elongate fibroblasts and compaction of the stress fibers with their subsequent disappearance from the cell. Cytochalasin D treatment prior to release disrupted the actin cytoskeleton and completely inhibited rapid contraction. The removal of serum prior to release inhibited rapid contraction, while the re-addition of serum restored rapid contraction. These results demonstrate that fibroblasts can develop tension in an attached collagen lattice and that upon release of tension the fibroblasts undergo contraction resulting in a rapid contraction of the collagen lattice. Fibroblast contraction is dependent upon an organized actin cytoskeleton and is promoted by the presence of serum.
Anat Rec 1992 Mar
PMID:Fibroblast contraction occurs on release of tension in attached collagen lattices: dependency on an organized actin cytoskeleton and serum. 154 60

Fibrotic development is a common response of the lung to toxic or deleterious insult. For example, the lung is the dose-limiting organ for irradiation of the thorax for primary or metastatic lesions, due in large part to latent fibrosis. The development of the fibrotic response reflects a cascade of cell-cell and cell-extracellular matrix interactions, the ultimate target of which is the fibroblast. There is increasing evidence of subpopulations of pulmonary fibroblasts, which may have differing roles in either the initiation or progression of fibrosis. Recently we described two fibroblast subpopulations from the murine lung, which differ in the presence or absence of the membrane antigen Thy-1 (Phipps et al., 1989). These Thy-1+ and Thy-1- subpopulations are stable and differ in certain functions, such as the production of cytokines and the display of Class II MHC antigens. To determine the morphologic development of the two subpopulations and their growth characteristics in vitro, cultures of the two cell subtypes were prepared for transmission and scanning electron microscopy at varying stages of growth. Thy-1+ fibroblasts are more spindle-shaped, contain intracellular lipid, exhibit abundant cell-cell contacts, and are capable of secreting large amounts of collagen and modest amounts of fibronectin. Thy-1- fibroblasts are more rounded and spread, contain no intracellular lipid droplets, possess more intracellular microfilaments and microtubules, and synthesize less collagen and more fibronectin than do Thy-1+ cells. There are no significant differences between the two subpopulations insofar as growth rates are concerned, but Thy-1+ fibroblasts possess an additional DNA peak during periods of early growth.
Anat Rec 1992 Mar
PMID:Morphologic and functional characteristics of subpopulations of murine lung fibroblasts grown in vitro. 154 67

Cells derived from an epithelial-mesenchymal transformation within the atrioventricular canal and outflow tract are involved in the partitioning of the early embryonic heart into a four-chambered organ. This transformation process has been shown to proceed from an inductive interaction between the myocardium and competent, target endothelial cells within these regions of the heart. Interestingly, immunohistochemistry revealed the presence of fibronectin-positive particulates within the matrix of mesenchyme-forming regions (Mjaatvedt et al., 1987). This particulate matrix is extractable by EDTA and can elicit the epithelial-mesenchymal transformation in culture (Mjaatvedt and Markwald, 1989). Analysis of EDTA extracts of embryonic heart tissue revealed the presence of fibronectin and about 40 unidentified proteins, 6 of which appeared to be enriched in the biologically active 100,000g pellet fraction (Mjaatvedt and Markwald, 1989). Based on these and other data we have proposed that the particulate matrix is composed of a multicomponent complex of fibronectin and one or more of the low-molecular-weight proteins in this pellet. The purpose of the present study was to begin a biochemical characterization of the nonfibronectin proteins thought to be present in the matrix particulates. Given that many matrix constituents are glycoproteins, lectins were used to initially characterize the particulate constituents. Of the lectins tested, soybean agglutinin (SBA) was found to be specific only for matrix particulates. Histochemical analyses showed that SBA and antibodies against fibronectin colocalized regionally and temporally to the same matrix particulates in embryonic heart tissue.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1992 Feb
PMID:Multiple glycoproteins localize to a particulate form of extracellular matrix in regions of the embryonic heart where endothelial cells transform into mesenchyme. 154 6

The distribution of type I collagen, fibronectin, laminin, and heparan sulfate was studied in marrow of rats by indirect immunofluorescence. Most of the type I collagen of marrow is associated with large blood vessels and connective tissue trabeculae, but type I collagen was also localized in a delicate meshwork throughout the marrow and in the basement membrane of the sinusoidal endothelium. Fibronectin is partially co-distributed with type I collagen, but is much more widely distributed. Sheets or septa of fibronectin-rich material divide the marrow into small compartments that contain and appear to separate clusters of developing blood cells. These septa may serve as a substrate for anchorage and migration of blood cells. Labeling of laminin was observed in the basement membranes of blood vessels, of fat cells, and of the sinusoidal wall, but only scattered labeling was seen in other extracellular materials. Heparan sulfate proteoglycan was poorly labeled in the extracellular matrix of marrow.
Anat Rec 1991 Oct
PMID:Immunochemical localization of extracellular materials in bone marrow of rats. 174 22

The fibronexus is a close transmembrane association between fibronectin filaments and actin microfilaments. It has been found at the surfaces of fibroblasts in tissue culture, as well as within contracting granulation tissue. This specialized connection has been proposed to play an important role in the adhesive properties of fibroblasts. The purpose of this study is to determine whether the fibronexus is present in other contracting tissues besides granulation tissue, specifically in Dupuytren's diseased tissue. Dupuytren's disease is a pathologic condition in which the palmar aponeurosis becomes shortened leading to irreversible flexion of the digits. Shortening of the aponeurosis is believed to be an active cellular process. Extracellular filaments and actin microfilaments form close transmembrane associations at the surfaces of actin-rich fibroblasts in Dupuytren's disease. Extracellular filaments extend from the cell surface into the surrounding tissue connecting fibroblasts with collagen fibrils and adjacent cells. In this study we have used immunoelectron microscopy to demonstrate that the extracellular filaments that participate in these close transmembrane associations contain fibronectin. High voltage electron microscopy has been used to examine the three-dimensional relationships between the cytoskeleton and fibronectin filaments in Dupuytren's diseased tissue. We propose that the fibronexus is a dominant adhesive structure at the surface of fibroblasts in Dupuytren's diseased tissue. The fibronexus, by mediating cell-to-cell and cell-to-matrix attachments, may serve to transmit contractile forces generated by actin microfilaments in these cells throughout the diseased tissue.
Anat Rec 1991 Jun
PMID:Fibronectin filaments and actin microfilaments are organized into a fibronexus in Dupuytren's diseased tissue. 186 94

As part of an ongoing study of heart development in normal and cardiac lethal mutant axolotls (Mexican salamanders) we examined the extracellular matrix (ECM) by microscopical methods. With scanning electron microscopy we are unable to detect ECM on the apical surface of cells of the early cardiogenic mesoderm. During the period of lateral plate migration, which coincides with the period of cardiogenic induction of mesoderm by anterior endoderm, there is little ECM, aside from some microfibrils, on the basal surface of the endoderm or mesoderm of the pharyngeal region. Later, a basal lamina (BL) is found on the endoderm and along portions of the developing endocardial and myocardial tubes. By the time of heartbeat initiation the BLs are complete and invested with striated collagen-like fibrils that are sparsely distributed in the "cardiac jelly" of normal and mutant hearts. Striated fibril deposition, which increases with time, is generally random in orientation, with the exception of some regions where there is a preferred directionality. During the post-hatching period striated fibrils appear in the subepicardial space. In addition, branching fibers that are probably elastin appear in the bulbus arteriosus. In these later stages the density of fibrils in the cardiac lethal mutant heart is much less than normal. Indirect immunofluorescent microscopy reveals laminin and fibronectin in the basal laminae of the endocardial and myocardial tubes of both normal and cardiac lethal mutant hearts. In addition, punctate and fibrillar staining for fibronectin, and punctate staining for laminin are found in the cardiac jelly. These matrix proteins are not abundant at the apical (exterior) surface of the myocardium until the epicardium appears.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1991 Jul
PMID:Extracellular matrix of the developing heart in normal and cardiac lethal mutant axolotls, Ambystoma mexicanum. 186 13


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