Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Basement Membrane”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 91 records · Page 5Linked to original sources
PubMed1987

Samoyed hereditary glomerulopathy. Immunohistochemical staining of basement membranes of kidney for laminin, collagen type IV, fibronectin, and Goodpasture antigen, and correlation with electron microscopy of glomerular capillary basement membranes.

Recent immunofluorescence studies on the kidneys of most males with hereditary nephritis have demonstrated an absence of Goodpasture antigen (GPA) from glomerular capillary basement membranes (GCBM). In the present study, we used immunofluorescence to determine whether laminin, collagen type IV, fibronectin, and GPA could be detected in basement membranes of the kidneys of dogs with Samoyed hereditary glomerulopathy, which was previously shown to be a model for human hereditary nephritis. The results obtained were correlated with the appearance of GCBM by electron microscopy (EM). The rabbit polyclonal antibodies used (antilaminin, anti-collagen type IV, and antifibronectin) showed specificity for the appropriate antigens in a plate-binding radioimmunoassay. Serum from a patient with Goodpasture syndrome was used to detect the GPA component of dog GCBM. Laminin and collagen type IV were present in GCBM, mesangium, tubular basement membrane, vascular basement membrane, and Bowman's capsule of neonatal, unaffected, and affected male and carrier female dogs. Fibronectin was present in mesangial, perivascular, and interstitial regions of the kidneys of all dogs and, in addition, in GCBM of neonatal, affected male, and carrier female dogs. GPA was not detected in the kidneys of neonatal dogs and its absence from GCBM correlated with their immature appearance by EM. However, a fully formed, trilaminar GCBM was observed by 3 weeks of age in unaffected, affected male, and carrier female dogs, before the detection of GPA in GCBM, which occurred at 4 weeks in unaffected and carrier female dogs, but still not in affected males. In the unaffected dogs, the presence of GPA correlated with the persistence of a fully formed trilaminar GCBM, which lasted throughout life, while in the carrier females, the presence of GPA correlated with focal areas of multilaminar splitting of GCBM by EM. In the affected male dogs, although a trilaminer GCBM was seen by 3 weeks of age, the persistent absence of GPA correlated with the eventual onset of multilaminar splitting of GCBM. These immunofluorescence and EM results suggest that GPA is not required to form a trilaminar GCBM initially but is necessary subsequently to maintain its integrity. GPA is normally present in the C terminal (NC1) domain of the collagen type IV molecule. It is hypothesized that Samoyed hereditary glomerulopathy in dogs and human hereditary nephritis result from a defect in the NC1 domain.

Animals↗
PubMed2004

Human amniotic membrane, like corneal epithelial basement membrane, manifests the alpha5 chain of type IV collagen.

PURPOSE: To reexamine whether the alpha5 chain of type IV (alpha5[IV]) collagen, thought to be absent, is in fact present in human amniotic membrane. METHODS: Cryosections of human amniotic membrane obtained at Cesarean section were immunohistochemically examined for the presence of alpha5(IV), with or without inclusion of the denaturing step. Amniotic membrane was digested with collagenase to release the noncollagenous NC1 domain from the alpha-chain. The NC1 domain of alpha5(IV) was then assayed on Western blot analysis. Identical experiments were performed with human corneas and conjunctivae obtained from an American eye bank. RESULTS: The basement membrane of denatured samples of amniotic membrane and cornea stained positive for alpha5(IV). Without the denaturing step, only corneal samples were positive. With or without denaturing, conjunctival epithelium did not stain. Western blot analysis detected NC1 domains of alpha5(IV) in amniotic membrane and corneal samples. CONCLUSIONS: The basement membrane of amniotic membrane resembles that of corneal epithelium but not conjunctiva. Amniotic membrane may be an excellent substrate for corneal epithelial cells.

Amnion↗
PubMedDate not supplied

Assembly, stability and integrity of basement membranes in vivo.

Basement membranes are layered structures of the extracellular matrix which separate cells of various kinds from the surrounding stroma. One of the frequently recurring questions about basement membranes is how these structures are formed in vivo. Up to a few years ago, it was thought that basement membranes were formed spontaneously by a process of self-assembly of their components. However, it has now become clear that cell membrane receptors for basement membrane components are essential factors for the formation and stability of basement membranes in vivo. The present review highlights the modern concepts of basement membrane formation.

Animals↗
PubMed1975

The basement membrane of the uterine cervix in dysplasia and squamous carcinoma: an immunofluorescent study with antibodies to basement membrane antigen.

Histological preparations with normal epithelium, dysplasia, carcinoma in situ and squamous invasive carcinoma of human cervix were studied by immunofluorescence using human sera containing antibodies against basement membrane material, against intercellular substance of squamous epithelium (ISSE) and against reticulin. A continuous basement membrane was observed in normal epithelium dysplasia and carcinoma in situ, but was faintly stained, discontinuous or even absent in specimens with invasive squamous carcinoma. Staining with anti-reticulin did not reveal any condensation in the basement membrane areas in any of the preparations examined. ISSE was demonstrated in the normal epithelium, dysplasia and carcinoma in situ as well as in invasive carcinoma.

Antigens↗
PubMed1983

Experimental autoimmune antiglomerular basement membrane antibody-induced glomerulonephritis. I. The effects of injecting sheep with human, homologous or autologous lung basement membranes and complete Freund's adjuvant.

We compared the effects of injecting human, homologous or autologous lung basement membrane (LBM) and complete Freund's adjuvant into 6-month-old sheep and injecting the same antigens into guinea pigs. All sheep receiving human LBM died of antiglomerular basement membrane (GBM) nephritis by Day 126. They had autoantibodies to antigenic determinants shared by fetal or adult sheep and human LBM and GBM and certain nonvascular basement membranes, but these autoantibodies did not localize in the lung in vivo or cause lung hemorrhages. No sheep injected with homologous or autologous LBM had any evidence of anti-GBM autoantibodies or nephritis or specific lung lesions. Their kidneys are indistinguishable by histologic, immunohistologic, and functional studies from kidneys of age-matched controls. Thus, sheep are very tolerant to their own LBM. Although all guinea pigs developed anti-GBM autoantibodies, they did not get anti-GBM nephritis or specific lung lesions. A hypothesis for the pathogenesis of Goodpasture's syndrome is presented.

Animals↗
PubMed2005

Glomerular basement membrane thickness in normal adults and its application to the diagnosis of thin basement membrane disease: an Indian study.

Microscopic hematuria of non-urologic origin warrants ultrastructural study of renal biopsy. Thinning and variations in the texture of glomerular basement membrane (GBM) are difficult to be recognized under light microscope; transmission electron microscope (TEM) therefore plays a vital role in identifying such changes. Ultrastructural morphometry is a valuable diagnostic aid when GBM is suspected of being abnormally thin. In an effort to determine the normal GBM thickness (GBMT) in Indian adults and to determine the cutoff value of GBMT for a diagnosis of thin basement membrane disease (TBMD), we determined GBM thickness in 25 normal adults. Postmortem biopsies of 25 normal adults (16 males and 9 females) aging between 18-58 years were included in the study. GBM thickness was determined through ultrastructural morphometry on accurately enlarged electron micrographs as harmonic mean of 50 orthogonal intercepts across the GBM in each case. Study revealed a mean GBM thickness of 321 nm with a standard deviation (SD) of 28 nm. Mean-2SD (321-56), that is 265 nm, was fixed as cutoff value of GBMT for the diagnosis of TBMD. A systematic split study of control subjects revealed thicker GBM (329+/-38 nm) in higher age group (35-60 years) as compared to GBMT (316+/-21 nm) in lower age group (18-30 years). Males in higher age group also revealed thicker GBM (males: 343+/-39 nm versus females: 300+/-12 nm). Ten patients with non-urologic hematuria and having GBMT<265 nm were diagnosed as cases of TBMD. Patients with TBMD revealed significantly attenuated GBM as compared to age and sex matched controls (214 +/- 40 nm versus 311 +/- 17 nm; p<0.0005). No overlap was observed in the distribution of GBMT in patients of TBMD and age and sex matched controls. Ultrastructural morphometry is the ultimate and appropriate method for diagnosing TBMD.

Adolescent↗
PubMed1986

Structure and function of basement membrane proteoglycans.

Basement membranes contain at least three different proteoglycans. These are a large, low buoyant density heparan sulphate proteoglycan and two smaller, high density proteoglycans with either heparan sulphate or chondroitin sulphate side-chains. The large (Mr 400K-600K and small (Mr 130K) heparan sulphate proteoglycans were purified from the mouse EHS tumour. These proteoglycans are immunologically related by sharing some protein core antigenic determinants (epitopes) but do not cross-react with cell-surface heparan sulphate proteoglycans or with proteoglycans from interstitial connective tissue. This indicates that they belong to a distinct family of proteoglycans. Structural models were developed, based on electron microscopy and analytical ultracentrifugation, demonstrating that the small proteoglycan contains on average four heparan sulphate chains of about 30 nm in length, while the large proteoglycan consists of three long (about 90 nm) heparan sulphate chains connected to one end of a large core protein. Single heparan sulphate chains were isolated from the EHS tumour proteoglycans and from the corresponding proteoglycans from Reichert's membrane of the mouse embryo. The heparan sulphate from Reichert's membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin. The EHS tumour heparan sulphate showed a higher N-/O-sulphate ratio and a lower affinity for antithrombin.

Animals↗
PubMed1993

[Rapidly progressing glomerulonephritis with antibodies to glomerular capillary basement membrane].

Antiglomerular basement membrane glomerulonephritis was diagnosed in 14 patients (6 men and 8 women) aged 20 to 59 years. Five patients were found to have Goodpasture s syndrome. 5 rapidly progressive glomerulonephritis. 1 nephrotic syndrome, and 1 had mild glomerulonephritis. Blood pressure, proteinuria and haematuria were not severe in most patients. In 10 patients, the diagnosis was not established before end-stage renal failure had developed. Four patients died of lung haemorrhage, in 3 the haemorrhage was controlled by the treatment, in 3 renal failure without lung haemorrhage occurred, and in 3 renal function improved or was stable. The prognosis improved significantly after plasma exchange together with immunosuppression had been introduced.

Adult↗
PubMed1983

Intermolecular reducible cross-links in rat glomerular basement membrane.

Glomerular basement membrane (GBM) was purified from adult rats and treated with tritiated borohydride for analysis of the reducible cross-links. After acid hydrolysis, samples were subjected, with and without prior gel filtration on Biogel P-2, to a chromatographic system standardized with known cross-links. The major peak of radioactivity co-eluted with authentic di-hydroxylysinonorleucine (di-OHLNL) standard. Derivation of this cross-link from lysine was corroborated by demonstrating its presence in GBM purified after incubation of isolated glomeruli with [14c]-lysine and after in vivo injection of [14C]-lysine. GBM labeled in vitro with radioactive lysine also contained peaks co-eluting with hydroxylysinonorleucine and lysinonorleucine standards, as well as at unidentified positions in the chromatogram. The findings indicate that rat GBM contains lysine-derived cross-links, of which di-OHLNL is the major reduced form.

Amino Acids↗
PubMed1996

Type IV collagen in sponges, the missing link in basement membrane ubiquity.

Basement membrane structures, or their main component, type IV collagen, have been detected in all multicellular animal species, except sponges. We cancel this exception by the demonstration of type IV collagenous sequences in a new marine sponge species by cDNA and genomic DNA studies. One of these sequences is long enough to demonstrate the specific characteristics of type IV collagen chains. The 12 cysteines are at conserved positions in the carboxyl-terminal non-helical NCl domain, as are the interruptions in the carboxyl-terminal end of the triple helical domain. The gene organization of the region coding for the NCl domain is similar to that of the human genes COL4A2, COL4A4 and COL4A6. An additional, shorter sequence suggests the presence of a second chain. The expected tissue localization of this collagen has been confirmed using polyclonal antibodies raised against a sponge recombinant protein. These results demonstrate that type IV collagen is representated in all animal phyla. It is actually the only known ubiquitous collagen and it has at least two different alpha chains in all the species where it has been characterized.

Amino Acid Sequence↗
PubMed1980

Differential solubility and subunit composition of rat glomerular basement membrane.

Glomerular basement membrane (GBM) was prepared from 2- to 3-month-old Sprague-Dawley rats by differential sieving and sonication. 80% of the membrane was soluble in 1% sodium dodecyl sulphate (SDS) and 1% 2-mercaptoethanol. The soluble fraction was resolved into 15 bands in the molecular weight range 30,000 to 300,000 by SDS-polyacrylamide gel electrophoresis. The major bands present had apparent molecular weights of 100,000 and 148,000. Treatment of GBM with SDS alone solubilised mainly low molecular weight components (45,000-150,000) but when the residue was treated with SDS and 2-mercaptoethanol higher molecular weight material was solubilised. Partial solubilisation of GBM was also achieved with pepsin. Digestion for 18 h at 4 degrees C resulted in 20% of the membrane being solubilised but this was increased to 55% at 10 degrees C. The amino-acid composition of pepsin-soluble GBM was more collagen-like than the residue remaining after enzyme digestion. Although the residue was more polar than whole GBM it still contained significant amounts of glycine and hydroxyproline and could be further subfractionated with SDS into a soluble fraction, the amino acid content of which was similar to whole GBM and a collagenous residue containing 317 residues/1,000 of glycine. When pepsin solubilised GBM was subjected to horizontal electrophoresis in SDS-polyacrylamide slab gels the principal bands migrated in the pro-alpha-chain region. This material was heterogeneous and in addition to the principal components, 6 components with apparent molecular weights less than 95,000 were present together with high molecular weight material in the gamma and beta regions of the gel. The band pattern of the pepsin-insoluble material was similar although the intensities of some individual bands varied significantly from that of the pepsin-soluble material. Rat GBM can therefore be fractionated by treatment with SDS alone, SDS together with 2-mercaptoethanol and pepsin digestion. The data reported is compatible with the presence of a mixture of collagen-like and polar regions rather than a major single collagenous component (type IV collagen).

Amino Acids↗
PubMed1990

Isolation and characterization of mouse glomerular basement membrane.

Glomerular basement membrane (GBM) antigens used for immunological studies have until now been isolated from human and rat glomeruli but not from mice. However, given the growing awareness of extracellular matrix species-specificity, the need for a purification method of mouse GBM exists. We now report the purification of GBM from isolated mouse glomeruli. 10 ml 0.01 M phosphate buffered saline (PBS) containing 1.25% Fe3O4 was perfused through the aortae of (C57BL10 x DBA/2)F1 mice over 1 min, kidneys were decapsulated and passed through a 0.075 mm mesh metal screen and collected. After pelletting and washing, the tube was placed against one pole of a magnet and the pelleted glomeruli were washed. This procedure was repeated three times. The glomerular suspension was examined by light microscopy, sonicated, and lyophilized. In suspension no free fragments of tubuli or Bowman's capsule were present as observed by light microscopy. Mouse GBM was prepared from the isolated glomeruli using a modification of earlier described methods for human and rat GBM by enzymatic digestion. Elisa studies showed the presence of laminin, type IV collagen, and fibronectin. Monoclonal antibody directed against tubular epithelial antigen gp160 did not react to either mouse or rat GBM. Sera and glomerular eluates from (C57BL10 x DBA/2)F1 mice suffering from chronic graft-versus-host autoimmune disease gave a higher signal against mouse GBM than against rat GBM. Normal rabbit serum, normal mouse serum and normal mouse eluate did not show significant activity against mouse GBM. Immunoblotting showed the presence of both laminin B1 and B2 chains as well as type IV collagen alpha 1 and alpha 2 subunits. In summary, we describe a method by which it is possible to extract mouse GBM with a high purity.

Animals↗
PubMed1982

In vivo biosynthesis and turnover of 35S-labeled glomerular basement membrane.

Renal glomerular basement membrane was labeled in vivo by the injection of tracer amounts of radioactive sulfate into normal adult rats. The biosynthesis and turnover of [35S]glycosaminoglycans in purified basement membrane was determined from the specific activity of 35S in pronase digests of basement membranes isolated 1-7 days after injection. Peak radioactive labeling occurred 24 h after injection following which the specific activity of basement membrane sulfate, expressed as cpm/microgram uronic acid, progressively declined over the ensuing period of study. The biologic half-life of radioactive sulfate in basement membrane was estimated at about 7 days, which is within the range previously reported for [35S]glycosaminoglycans in whole renal cortex. The findings indicate that 35S-labeled components of glomerular basement membrane have a relatively rapid turnover.

Animals↗
PubMed1993

"In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin.

We have studied the soluble fragments obtained from bovine lens capsules after digestion by the cysteine proteinases cathepsins B, B-like and L. These proteinases liberated collagen IV, laminin and fibronectin fragments, as shown by immunoblotting. Sodium dodecyl sulfate treatment of digested capsules gave a soluble material used for subsequent fractionation and immunochemical study. Comparison of both results demonstrate the ability of these cathepsins to degrade a basement membrane at near neutral pH values. The differences observed in the size and the number of fragments suggest that the three proteinases exhibit similar specificities in basement membrane digestion, as shown previously. Nevertheless, cathepsin L seems to be more effective than cathepsins B and B-like. From this study, cysteine proteinases could be associated to basement membrane destruction. Soluble cysteine proteinase digests of bovine lens capsules showed several bands of gelatinolytic activity by gelatin zymography. Three major bands of 77, 60 and 45 kDa were seen whatever the cysteine proteinase used. These bands were identified as fibronectin fragments. Thus cysteine proteinases can activate the latent proteinase fibronectin from basement membrane leading to a new "metastatic cascade". This would be an important factor in the "in vivo" basement membrane dissolution observed during tumor invasion.

Animals↗
PubMed2003

Thin basement membrane nephropathy.

Thin basement membrane nephropathy. Thin basement membrane nephropathy (TBMN) is the most common cause of persistent glomerular bleeding in children and adults, and occurs in at least 1% of the population. Most affected individuals have, in addition to the hematuria, minimal proteinuria, normal renal function, a uniformly thinned glomerular basement membrane (GBM) and a family history of hematuria. Their clinical course is usually benign. However, some adults with TBMN have proteinuria >500 mg/day or renal impairment. This is more likely in hospital-based series of biopsied patients than in the uninvestigated, but affected, family members. The cause of renal impairment in TBMN is usually not known, but may be due to secondary focal segmental glomerulosclerosis (FSGS) or immunoglobulin A (IgA) glomerulonephritis, to misdiagnosed IgA disease or X-linked Alport syndrome, or because of coincidental disease. About 40% families with TBMN have hematuria that segregates with the COL4A3/COL4A4 locus, and many COL4A3 and COL4A4 mutations have now been described. These genes are also affected in autosomal-recessive Alport syndrome, and at least some cases of TBMN represent the carrier state for this condition. Families with TBMN in whom hematuria does not segregate with the COL4A3/COL4A4 locus can be explained by de novo mutations, incomplete penetrance of hematuria, coincidental hematuria in family members without COL4A3 or COL4A4 mutations, and by a novel gene locus for TBMN. A renal biopsy is warranted in TBMN only if there are atypical features, or if IgA disease or X-linked Alport syndrome cannot be excluded clinically. In IgA disease, there is usually no family history of hematuria. X-linked Alport syndrome is much less common than TBMN and can often be identified in family members by its typical clinical features (including retinopathy), a lamellated GBM without the collagen alpha3(IV), alpha4(IV), and alpha5(IV) chains, and by gene linkage studies or the demonstration of a COL4A5 mutation. Technical difficulties in the demonstration and interpretation of COL4A3 and COL4A4 mutations mean that mutation detection is not used routinely in the diagnosis of TBMN.

Basement Membrane↗