scholarly journals The distribution of collagenase in normal rat tissues.

1975 ◽  
Vol 23 (12) ◽  
pp. 910-920 ◽  
Author(s):  
I Montfort ◽  
R Pérez-Tamayo
Keyword(s):  
Connective Tissue ◽  
Immunoglobulin G ◽  
Basement Membranes ◽  
Rat Tissues ◽  
Collagenase Activity ◽  
Rat Uterus ◽  
Triceps Muscle ◽  
Normal Rat ◽  
Immunohistochemical Methods ◽  
Tail Tendon

A rabbit monospecific anti-rat uterus collagenase antibody has been used to study the distribution of collagenase in normal rat tissues by immunohistochemical methods. Indirect staining was performed with fluorescein-conjugated goat anti-rabbit immunoglobulin G antibody. The organs studied were brain, lung, myocardium, liver, spleen, kidney, adrenal, testes, uterus, xiphoid cartilage, tail tendon, skeletal (triceps) muscle and skin. Collagenase is widely present throughout the connective tissue structures in all organs examined. The enzyme is apparently bound to collagen fibers, reticulum fibers and basement membranes. The results suggest that control of collagenase activity depends on factors other than the presence of the enzyme in tissues.

scholarly journals Distribution of fibroblast surface antigen in the developing chick embryo.

1975 ◽  
Vol 142 (1) ◽  
pp. 41-49 ◽  
Author(s):  
E Linder ◽  
A Vaheri ◽  
E Ruoslahti ◽  
J Wartiovaara
Keyword(s):  
Chick Embryo ◽  
Connective Tissue ◽  
Basement Membranes ◽  
Loose Connective Tissue ◽  
Extracellular Medium ◽  
Liver Sinusoids ◽  
Stage Of Development ◽  
Parenchymal Cells ◽  
Fibrillar Network

Fibroblast surface (SE) antigen is present in fibrillar surface structures of cultured normal fibroblasts, shed to the extracellular medium, and is also found in circulation (serum and plasma). Malignant fibroblasts (transformed by viruses) do not express SF antigen on the cell surface. In this study the in vivo differentiation and distribution of SF antigen has been investigated in the developing chick embryo using cryostat sections and immunofluorescence. The major findings were: (a) SF antigen was detectable in the loose connective tissue of very early (2-to 3-day old) embryos. (b) Condensation of SF antigen was seen in various boundary membranes such as the glomerular and tubular basement membranes of the kidney, the boundary membranes of the notochord, yolk sac, and vitelline membranes and liver sinusoids. (c) SF antigen was found to be cell-type specific. It was seen as a fibrillar network in the loose connective tissue of different organs but not in the parenchymal cells. It was not found in muscle cells at any stage of development. (d) The antigen was present in the undifferentiated mesenchymal cells of the kidney; but not found after their development into epithelial cells of the secretory tubules. (e) Both in vivo and in fibroblast cultures SF antigen was distributed as a fibrillar network. These data indicate that SF antigen is a "differentiation antigen" restricted to certain cells of mesenchymal origin and character, and that is accumulates in the connective tissue during embryogenesis.

Expression of vascular permeability factor/vascular endothelial growth factor in normal rat tissues

1993 ◽  
Vol 264 (4) ◽  
pp. C995-C1002 ◽  
Author(s):  
W. T. Monacci ◽  
M. J. Merrill ◽  
E. H. Oldfield
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
In Situ Hybridization ◽  
Rat Tissues ◽  
Vascular Endothelial ◽  
Vascular Permeability Factor ◽  
Organ Specific ◽  
Normal Rat ◽  
Endothelial Growth Factor ◽  
The Brain

Vascular permeability factor (VPF)/vascular endothelial growth factor (VEGF) is a approximately 43-kDa secreted protein that has been shown in bioassays to induce endothelial proliferation, angiogenesis, and capillary hyperpermeability. VPF has been suggested to play an important role in the physiology of normal vasculature. To further elucidate the natural functions of VPF in vivo, the expression of VPF in normal tissues was examined using Northern blot analysis and in situ hybridization histochemistry. VPF mRNA is expressed in the brain, kidney, liver, lung, and spleen of the healthy adult rat. On Northern blots, the relative abundance of VPF mRNA observed in these tissues was highest in the lung and lowest in the spleen. As determined by in situ hybridization, the patterns of VPF expression are organ specific. Hybridization of an antisense VPF probe was concentrated in the cerebellar granule cell layer of the brain and in the glomeruli and tubules of the kidney. In the liver and lung, intense hybridization was observed homogeneously throughout both tissues, demonstrating that VPF mRNA is present in virtually every hepatocyte and pulmonary alveolar cell. Hybridization to the spleen was weaker and more diffuse. The widespread expression and organ-specific distribution of VPF mRNA in normal rat tissues supports the suggestion of an extensive role for this factor in the physiology of normal vasculature.

scholarly journals Monoclonal and polyclonal immunoglobulin G deposits on tubular basement membranes of native and pretransplant kidneys: A retrospective study

2020 ◽  
Author(s):  
Anri Sawada ◽  
Masayoshi Okumi ◽  
Shigeru Horita ◽  
Tomomi Tamura ◽  
Sekiko Taneda ◽  
...  
Keyword(s):  
Retrospective Study ◽  
Immunoglobulin G ◽  
Basement Membranes ◽  
Polyclonal Immunoglobulin

Abstract The authors have withdrawn this preprint due to author disagreement.

scholarly journals INORGANIC CATIONS IN RAT KIDNEY

1971 ◽  
Vol 50 (3) ◽  
pp. 830-839 ◽  
Author(s):  
C. J. Tandler ◽  
A. L. Kierszenbaum
Keyword(s):  
Aqueous Solution ◽  
Connective Tissue ◽  
Rat Kidney ◽  
Basement Membranes ◽  
Cell Nuclei ◽  
Inorganic Cations ◽  
Dense Granules ◽  
Distal Tubules ◽  
The Masses ◽  
Potassium Pyroantimonate

For localization of pyroantimonate-precipitable cations, rat kidney was fixed by perfusion with a saturated aqueous solution of potassium pyroantimonate (pH about 9.2, without addition of any conventional fixative). A remarkably good preservation of the tissue and cell morphology was obtained as well as a consistent and reproducible localization of the insoluble antimonate salts of magnesium, calcium, and sodium. All proximal and distal tubules and glomeruli were delimited by massive electron-opaque precipitates localized in the basement membrane and, to a lesser extent, in adjacent connective tissue. In the intraglomerular capillaries the antimonate precipitate was encountered in the basement membranes and also between the foot processes. In addition to a more or less uniform distribution in the cytoplasm and between the microvilli of the brush border, antimonate precipitates were found in all cell nuclei, mainly between the masses of condensed chromatin. The mitochondria usually contained a few large antimonate deposits which probably correspond to the so-called "dense granules" observed after conventional fixations.

scholarly journals Ultrastructural localization of the major components of the extracellular matrix in normal rat nerve.

1992 ◽  
Vol 40 (6) ◽  
pp. 859-868 ◽  
Author(s):  
P Lorimier ◽  
P Mezin ◽  
F Labat Moleur ◽  
N Pinel ◽  
S Peyrol ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Peripheral Nerve ◽  
Ultrastructural Localization ◽  
Basement Membranes ◽  
Type I ◽  
Immunoperoxidase Method ◽  
Adult Rat ◽  
Normal Rat ◽  
Rat Nerve ◽  
Fibronectin Type

In this study we determined the ultrastructural distribution of the various components of the extracellular matrix (laminin, fibronectin, Type I, III, and IV collagens) of the normal peripheral nerve in adult rat. The localization of these macromolecules was investigated in basement membranes as well as in different areas of epi-, peri-, and endoneurium, by use of a pre-embedding immunoperoxidase method.

scholarly journals Basement membrane chondroitin sulfate proteoglycans: localization in adult rat tissues.

1990 ◽  
Vol 38 (10) ◽  
pp. 1479-1486 ◽  
Author(s):  
K J McCarthy ◽  
J R Couchman
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Rat Kidney ◽  
Basement Membranes ◽  
Rat Tissues ◽  
Adult Rat ◽  
Unique Distribution ◽  
Reichert's Membrane

Heparan sulfate proteoglycans have been described as the major proteoglycan component of basement membranes. However, previous investigators have also provided evidence for the presence of chondroitin sulfate glycosaminoglycan in these structures. Recently we described the production and characterization of core protein-specific monoclonal antibodies (MAb) against a chondroitin sulfate proteoglycan (CSPG) present in Reichert's membrane, a transient extra-embryonic structure of rodents. This CSPG was also demonstrated to be present in adult rat kidney. We report here the tissue distribution of epitopes recognized by these MAb. The ubiquitous presence of these epitopes in the basement membranes of nearly all adult rat tissues demonstrates that at least one CSPG is a constituent of most basement membranes, and by virtue of its unique distribution is distinct from other chondroitin and dermatan sulfate proteoglycans previously described.

scholarly journals Immunocytochemical localization of fibronectin in limb tissues of the adult newt, Notophthalmus viridescens.

1981 ◽  
Vol 29 (8) ◽  
pp. 937-945 ◽  
Author(s):  
L A Repesh ◽  
L T Furcht ◽  
D Smith
Keyword(s):  
Connective Tissue ◽  
Striated Muscle ◽  
Basement Membranes ◽  
Similar Distribution ◽  
Immunocytochemical Localization ◽  
Tissue Scaffold ◽  
Cell Matrix ◽  
Tissue Organization ◽  
Adult Newt ◽  
Cell Matrix Interactions

This study describes the immunocytochemical localization of fibronectin, a defined connective tissue and plasma glycoprotein, and its relationship to collagen and reticulin in adult newt limb tissues. We have also isolated the plasma form of fibronectin in a related species, the adult mudpuppy. The insoluble form of fibronectin was detected with immunoperoxidase stain in basement membranes and loose connective tissue. The endoneurium and perineurium of nerve bundles and the connective tissue elements of striated muscle stained heavily for fibronectin. The dermis and blood vessel walls also reached positively with the immunoperoxidase stain. A similar distribution was observed for reticulin with conventional histologic techniques with the exception of the dermis where only trace amounts of the protein were observed. Fibronectin and collagen were codistributed in the tissues studies. Fibronectin appeared to be intercalated among larger collagenous fibers. Collagen and fibronectin form an extracellular connective tissue scaffold that abuts against many types of adherent cells in different tissues. This supports the possible role of fibronectin in cell-matrix interactions and normal cell and tissue organization.

Der Einfluß von D-Penicillamin auf den Gehalt einiger Organe an Spurenelementen sowie auf die mechanischen Eigenschaften von Kollagen / Trace Elements in Several Organs and Mechanical Properties of Collagen under the Influence of D-Penicillamin

1978 ◽  
Vol 33 (5-6) ◽  
pp. 346-358 ◽  
Author(s):  
H. Wesch ◽  
R. Jonak ◽  
H. Nemetschek-Gansler ◽  
H. Riedl ◽  
Th. Nemetschek
Keyword(s):  
Mechanical Properties ◽  
Trace Elements ◽  
Schiff Base ◽  
Connective Tissue ◽  
Functional Groups ◽  
Schiff Bases ◽  
Collagen Fibrils ◽  
Principal Effect ◽  
Tail Tendon ◽  
Cu Ions

Abstract The content of trace elements in several organs of rats under the influence of D-penicillamine (D-PA) was investigated by the neutronactivation-analysis. It could be shown an diminution of Cu, and Co under D-PA-treatment, the content of Fe, Mn, Rb and Zn was not influenced. The investigat­ ed organs didn’t show any submicroscopic alterations under D-PA. On isolated collagen fibrils of tail tendon was seen a significantly diminuition of E-moduls. In accordance with Siegel the principal effect of D-PA is thought to block the synthesis of functional groups from Schiff-base crosslink precursors but not to inhibit lysyloxidase by loss of Cu-ions of connective tissue. The thermostability of D-PA influenced fibrils is changed in stretched state only and will be due to the lack of crosslink Schiff-bases; where as the shrinking point of not stretched fibrils shows only aging dependent changes.

On the Basement Membrane of the Nephron

1965 ◽  
Vol 32 (1) ◽  
pp. 44-50
Author(s):  
Antti Paalanen
Keyword(s):  
Connective Tissue ◽  
Basement Membrane ◽  
Outer Membrane ◽  
Renal Tubule ◽  
Basement Membranes ◽  
Functional Adaptation ◽  
Renal Tubules ◽  
Elastic Tissue ◽  
Renal Corpuscle ◽  
Bowman's Capsule

This study comprises some observations about the structure of the connective tissue of the basement membrane and interstitium in some normal, post-natal human kidneys. The basis of the basement membrane is mainly a reticular, homogeneous membrane that belongs uniformly to both Bowman's capsule and the wall of the renal tubule. Outside it in the capsule is a durable collagenic membrane whose development must be considered and evincement of functional adaptation under the pressure conditions of the cavity. In renal tubules there is no such well-defined outer membrane, but in them the basement membrane has in addition collagenic traits to some extent and is thus reticular-collagenic when examined as a whole. The renal tubules are surrounded by a dense, spiraling reticular network of fibres which attaches to the connective tissue of the interstitium where fibrocytes are scarce. The network extends all the way around the renal corpuscle. There is no elastic tissue at all in the basement membranes.

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