Diffuse Leiomyomatosis of the Esophagus: Disorder of Cell-Matrix Interaction?

1998 ◽  
Vol 1 (6) ◽  
pp. 543-549 ◽  
Author(s):  
Paul Thorner ◽  
Laurence Heidet ◽  
Fernando Moreno Merlo ◽  
Vern Edwards ◽  
Corinne Antignac ◽  
...  
Keyword(s):  
Collagen Type ◽  
Rare Condition ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Cell Periphery ◽  
Matrix Interaction ◽  
Type Iv ◽  
Cell Matrix ◽  
Reverse Pattern ◽  
Genes Encoding

Diffuse leiomyomatosis (DL) is rare condition characterized by proliferation of smooth muscle in the upper gastrointestinal tract. Most cases are associated with X-linked Alport syndrome and have partial deletions in the genes encoding both the α5 and α6 chains of collagen type IV. We studied aspects of cell-matrix interaction of myocytes in an esophagogastrectomy specimen from a 12-year-old patient with DL. Myocytes had central areas of cytoplasmic rarefaction, which were actin positive and desmin poor, with the reverse pattern of staining at the cell periphery. Electron microscopy (EM) showed that the areas of rarefaction consisted of disorganized aggregates of filaments. The basement membranes ranged from thickened to thinned or absent. Immunohistochemical staining for the α1–α4 chains of collagen type IV, the α1, α2, β2, and γ1 chains of laminin, nidogen, type VI collagen, and fibronectin was normal. There was loss of the α5 and α6 chains of collagen type IV and the β1 chain of laminin. Normal staining for α1, α2, α3, α4, α6, α8, and β1 integrins was noted. Staining for α5 integrin varied from normal to reduced or negative in different cells. In DL, a primary abnormality of basement membrane may be associated with disorganization of the contractile apparatus and alterations of certain integrins. This may reflect a disturbance of cell-matrix interactions that play a role in cell differentiation and internal organization.

scholarly journals Expression of collagen type IV in human kidney during prenatal development

2020 ◽  
pp. 111-111
Author(s):  
Vladimir Petrovic ◽  
Ivan Nikolic ◽  
Marko Jovic ◽  
Vladimir Zivkovic ◽  
Miodrag Jocic ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Collagen Type ◽  
Kidney Tissue ◽  
Volume Density ◽  
Collagen Iv ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Type Iv ◽  
Metanephric Kidney ◽  
Collecting System

Background / Aim. Type IV collagen belongs to the group of non-fibrillar collagens and is an important component of the basement membranes where it accounts for approximately 50% of its structural elements. The aim of the paper was to describe the expression and distribution of collagen type IV in embryonic and fetal metanephric kidney, and to determine the volume density of collagen type IV in kidney tissue in each trimester of development. Methods. The material consisted of 19 human embryos/fetuses, in the gestational age from 8th to 37th week. Kidney tissue specimens were routinely processed to paraffin molds and stained with hematoxylin and eosin and immunohistochemically using polyclonal anti-collagen IV antibody. Stained slides were examined using light microscope and images of the selected areas, under different lens magnification were captured with digital camera. Volume density of collagen type IV was determined by using ImageJ 1.48v and a plugin of the software which inserted a grid system with 336 points. For the data comparison One-Way Analysis of Variance was used. Results. Strong collagen IV immunopositivity was seen in all specimens, with a distribution in the basement membranes of urinary bud, parietal leaf of Bowman?s capsule, glomerular basement membrane, basement membrane of interstitial blood vessels, and basement membranes of nephron tubules and collecting ducts. No statistically significant difference in the volume density of type IV collagen was found between the different trimesters of development. Conclusion. The synthesis and secretion of collagen type IV simultaneously follows the development of nephron structures, collecting system and blood vessels. The volume density of collagen type IV remains constant throughout all the trimesters of metanephric kidney development, indicating that it plays a crucial role in normal development of nephron and collecting system structures, as well as in maintaining the normal kidney function.

scholarly journals An attempt at quantitation of procollagens I and III and of collagen IV in tooth sections by exposure to the corresponding antibodies followed by 125I-protein A and radioautography.

1980 ◽  
Vol 28 (12) ◽  
pp. 1355-1358 ◽  
Author(s):  
G M Wright ◽  
C P Leblond
Keyword(s):  
Collagen Type ◽  
Protein A ◽  
Collagen Iv ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Periodontal Tissue ◽  
Rat Incisor ◽  
Type Iv ◽  
Silver Grains ◽  
Procollagen Iii

The immunoreactivity of procollagen types I and III and of collagen type IV was detected in frozen sections of the growing apical end of rat incisor teeth by an indirect method making use of protein A. The sections were exposed to affinity-purified antibodies against these substances. The bound antibodies were then detected by incubation with radioiodinated protein A, followed by radioautography. This immunoradioautographic approach yielded preparations with low background, in which the reactions could be quantitated by counts of silver grains. The distribution of the radioautographic reactions was essentially the same as that previously observed with direct and indirect peroxidase methods, that is, procollagen I antigenicity predominated in odontoblasts and predentin, with minor amounts in periodontal tissue and pulp; procollagen III antigenicity was present in periodontal tissue and, to a lesser extent, in the pulp; and collagen IV antigenicity was restricted to basement membranes. Moreover, grain counts provided quantitative support for the conclusions on the distribution of procollagen I and III antigenicity.

scholarly journals A role for collagen type IV in cardiovascular disease?

2018 ◽  
Vol 315 (3) ◽  
pp. H610-H625 ◽  
Author(s):  
L. B. Steffensen ◽  
L. M. Rasmussen
Keyword(s):  
Cardiovascular Disease ◽  
Coronary Artery Disease ◽  
Coronary Artery ◽  
Collagen Type ◽  
Experimental Studies ◽  
Significant Risk ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Type Iv ◽  
Artery Disease

Over the past decade, studies have repeatedly found single-nucleotide polymorphisms located in the collagen ( COL) 4A1 and COL4A2 genes to be associated with cardiovascular disease (CVD), and the 13q34 locus harboring these genes is one of ~160 genome-wide significant risk loci for coronary artery disease. COL4A1 and COL4A2 encode the α1- and α2-chains of collagen type IV, a major component of basement membranes in various tissues including arteries. Despite the growing body of evidence indicating a role for collagen type IV in CVD, remarkably few studies have aimed to directly investigate such a role. The purpose of this review is to summarize the clinical reports linking 13q34 to coronary artery disease, atherosclerosis, and artery stiffening and to assemble the scattered pieces of evidence from experimental studies based on vascular cells and tissue collectively supporting a role for collagen type IV in atherosclerosis and other macrovascular disease conditions.

scholarly journals Human Basement Membrane Collagens do not Elicit Platelet Aggregation

1977 ◽  
Author(s):  
R. L. Trelstad ◽  
A. C. Carvalho
Keyword(s):  
Platelet Aggregation ◽  
Basement Membrane ◽  
Collagen Type ◽  
Serotonin Release ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Type Iv ◽  
Skin Collagen ◽  
Human Collagen

The immediate subendothelial connective tissue matrix consists of the basement membrane, a collagenous felt-like cell surface coat. The collagen from basement membranes has been isolated from human lung, skin, and kidney using a new fractionation method which separates native forms of collagen Types I, II, III, and IV. The Type IV collagens from the basement membranes have been characterized in respect to amino acid and carbohydrate composition, molecular size, charge and native structure. Antibodies prepared against the Type IV collagen reacted with both epithelial and vascular basement membranes as judged by immunofluorescence. Platelet-rich plasma (250,000/μl) from 5 normal subjects were tested for aggregation and 14C-serotonin release with human collagen Types I, II, III, and IV. Complete aggregation (100%) and 14C-serotonin release (80–100%) was obtained when Types I, II, and III were used. Human kidney, lung, and skin collagen Type IV (10–100μg/ml) did not aggregate platelets nor cause release of their contents. Pre-incubation of platelets and human collagen Type IV for periods of 30 minutes did not result in inhibition of platelet aggregation by Types I, II, or III.These data indicate that the collagenous component of the basement membrane, the first extra-vascular collagen to which a platelet is exposed, does not elicit aggregation as do the fibrillar collagens in the perivascular matrix.

scholarly journals Protease treatment combined with immunohistochemistry reveals heterogeneity of normal and neoplastic basement membranes.

1988 ◽  
Vol 36 (2) ◽  
pp. 213-220 ◽  
Author(s):  
F J Leu ◽  
I Damjanov
Keyword(s):  
Smooth Muscle ◽  
Collagen Type ◽  
Malignant Tumors ◽  
Differential Susceptibility ◽  
Basement Membranes ◽  
Benign Tumors ◽  
Collagen Type Iv ◽  
Human Tissues ◽  
Proteolytic Digestion ◽  
Type Iv

Heterogeneity of normal tissue and neoplastic basement membranes was investigated immunohistochemically with monoclonal antibodies and polyclonal antisera to laminin and collagen type IV. Cryostat sections of normal and neoplastic human tissues were digested with bacterial protease or trypsin. The duration of digestion and the concentration of enzyme were varied to determine whether laminin and collagen type IV could be removed differentially from basement membranes from distinct anatomic sites. After digestion, the residual antigenicity of glycoprotein was assessed immunohistochemically. Laminin could be removed more easily from all tissues than could collagen IV, and also much more easily from malignant tumors than from benign tumors or normal tissues. On the basis of susceptibility to proteolytic digestion, basement membranes from normal human tissues were classified as susceptible (e.g., heart and smooth muscle of gastrointestinal tract and uterus), moderately resistant (e.g., nerve, skeletal muscle, epithelial basement membrane of skin, smooth muscle of arteries), and very resistant (e.g., glomerulus). Differential susceptibility to proteolytic digestion most likely reflects quantitative and possibly also qualitative differences in the composition of basement membranes.

Substratum modification by endothelial cells (EC) in culture

1992 ◽  
Vol 50 (1) ◽  
pp. 656-657
Author(s):  
J.C. Lewis ◽  
I. Hermanns ◽  
K.W. Grant ◽  
S. Evans ◽  
C. Gossen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Collagen Type ◽  
Umbilical Vein ◽  
Surface Characteristics ◽  
Collagen Iv ◽  
Collagen Type Iv ◽  
Cell Periphery ◽  
Natural Polymers ◽  
Type Iv ◽  
Grafting Materials

Thrombosis resulting from blood interaction with prostheses is a concern following vascular grafting, and efforts have been made to endothelialize grafting materials and thereby reduce thrombogenicity. These efforts have focused upon altering polymer surfaces to enhance endothelial compatibility following surgery; however, using homologous EC attempts are being made to pre-seed grafting materials having defined surface characteristics. Such surfaces might be pre-absorbed with natural polymers as collagens, fibrin(ogen) or fibronectin. Irrespective of the starting character, these surfaces are rapidly altered following contact with tissues and body fluids, and as an extension by the EC themselves. To address this latter question, human umbilical vein endothelial cells (HUVEC) were seeded for whole-mouat microscopy onto carbon-stabilized, formvar-coated surfaces to which either collagen Type IV or its CB3 fragment had been adsorbed. Following culture for 3 or 24 hrs the cells were fixed in situ with glutaraldehyde, washed and processed for two-stage multiantigen immunogold microscopy. The first stage was comprised of rabbit anti-human fibronectin and mouse antihuman collagen Type IV. These were followed by second stage probes including goat anti-rabbit IgG (5nM gold), goat anti-mouse IgG (15 nM gold) and goat anti-human IgG (10 nM gold) as a control. HUVEC readily attached to and spread upon collagen IV and the CB3 fragment; the degree of spreading was much more pronounced with CB3 at both 3 and 24 hrs. The primary difference between the culture times was in cell density, with more cells at 24 than 3 hrs (Fig. 1). This difference could be explained by the additional generation time. The interaction of cells with the substratum was complex. This included deposition of proteins on the surface and extension of delicate macromolecular bridges from the cell periphery. Through the use of immunogold microscopy, fibronectin, collagen and immunoglobulin could be detected in all samples, including those plated in the absence of serum. Initially, collagen (IV and CB3) was more dense on the substrate than on the cells, and this was consistent with surface coating prior to cell seeding (Fig. 3). Fibronectin and IgG, on the other hand, were derived either from the medium or secreted from the cells, and each was associated with the cells or the cell edge (Fig. 4,5). Notably, detection of all three peptides was reduced over time, and this may be interpreted as secondary conditioning of the surface by HUVEC secreted products.

scholarly journals In Situ Localization of Gelatinolytic Activity in the Extracellular Matrix of Metastases of Colon Cancer in Rat Liver Using Quenched Fluorogenic DQ-gelatin

2003 ◽  
Vol 51 (6) ◽  
pp. 821-829 ◽  
Author(s):  
Olaf R.F. Mook ◽  
Claudia Van Overbeek ◽  
Eleonora G. Ackema ◽  
Febe Van Maldegem ◽  
Wilma M. Frederiks
Keyword(s):  
Colon Cancer ◽  
Extracellular Matrix ◽  
Rat Liver ◽  
Collagen Type ◽  
Basement Membranes ◽  
Gelatinolytic Activity ◽  
Collagen Type Iv ◽  
Type Iv

Matrix metalloproteinases (MMPs) such as gelatinases are believed to play an important role in invasion and metastasis of cancer. In this study we investigated the possible role of MMP-2 and MMP-9 in an experimental model of colon cancer metastasis in rat liver. We demonstrated with gelatin zymography that the tumors contained MMP-2 and MMP-9, but only MMP-2 was present in the active form. Immunolocalization of MMP-2 showed that the protein was localized at basement membranes of colon cancer cells and in intratumor stroma, associated with extracellular matrix (ECM) components. However, zymography and immunohistochemistry (IHC) do not provide information on the localization of MMP activity. Therefore, we developed an in situ zymography technique using the quenched fluorogenic substrate DQ-gelatin in unfixed cryostat sections. The application of DQ-gelatin in combination with a gelled medium allows precise localization of gelatinolytic activity. Fluorescence due to gelatinolytic activity was found in the ECM of tumors and was localized similarly to both MMP-2 protein and collagen type IV, its natural substrate. The localization of MMP-2 activity and collagen type IV at similar sites suggests a role of MMP-2 in remodeling of ECM of stroma in colon cancer metastases in rat liver.

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