A study by immunofluorescence microscopy of the NC1 domain of collagen type IV in glomerular basement membranes of two patients with hereditary nephritis

1990 ◽  
Vol 416 (3) ◽  
pp. 205-212 ◽  
Author(s):  
Paul S. Thorner ◽  
Reuben Baumal ◽  
Allison Eddy ◽  
Paula M. Marrano
Keyword(s):  
Collagen Type ◽  
Immunofluorescence Microscopy ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Hereditary Nephritis ◽  
Type Iv ◽  
Nc1 Domain

scholarly journals Abnormalities in the NC1 domain of collagen type IV in GBM in canine hereditary nephritis

1989 ◽  
Vol 35 (3) ◽  
pp. 843-850 ◽  
Author(s):  
Paul Thorner ◽  
Reuben Baumal ◽  
Victor E.O. Valli ◽  
Don Mahuran ◽  
Roderick McInnes ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type Iv ◽  
Hereditary Nephritis ◽  
Type Iv ◽  
Nc1 Domain

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.

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 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.

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