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PubMed1983

Formation of a supramolecular complex is involved in the reconstitution of basement membrane components.

Basement membrane macromolecules, including type IV collagen, laminin, and heparan sulfate proteoglycan, do not aggregate when incubated alone. Rather, precipitation occurs in the presence of equimolar amounts of laminin and type IV collagen but variable amounts of heparan sulfate proteoglycan. This interaction requires native laminin and type IV collagen. Heparan sulfate proteoglycan increases the precipitation of laminin particularly in the presence of type IV collagen. Fibronectin does not cause type IV collagen to precipitate. These studies show that the components of basement membrane interact in a highly specific manner and suggest that such interactions may be involved in the deposition of basement membrane in situ.

Animals↗
PubMed2001

Expression of l-3-phosphoserine phosphatase is regulated by reconstituted basement membrane.

Reconstituted basement membrane (Matrigel) promotes differentiation of endometrial adenocarcinoma cells in vitro. However, little is known about the molecular basis of these in vitro differentiation processes. Using differential display RT-PCR to search for potential molecular markers we screened for genes which respond to contact to basement membrane by alteration of expression levels. Here we report that the cDNA MT32 represents an mRNA with a time dependent biphasic response pattern to contact to basement membrane. Characterizing MT32 revealed that the sequence of MT32 is identical to l-3-phosphoserine phosphatase. PCR analysis of l-3-phosphoserine phosphatase expression surprisingly revealed at least three variants of this enzyme. In summary, and in view of the literature, l-3-phosphoserine phosphatase and potential variants or family members represent molecular markers to study regulation of gene expression by components of the extracellular matrix. In conclusion, l-3-phosphoserine phosphatase(s) may be important in endometrial carcinogenesis since this enzyme synthesizes important metabolic intermediates which serve both as building blocks for peptide synthesis and for signal transducing molecules.

Base Sequence↗
PubMed2005

Salivary gland morphogenesis and basement membranes.

The basement membrane separates the epithelium from the surrounding mesenchyme and plays an essential role in the development of various epithelial-mesenchymal organs. Among these, the submandibular salivary gland (SMG) has been chosen to review the expression patterns and roles of the epithelial basement membrane and its components, in particular the laminins, during SMG morphogenesis. At the outset, a brief description of SMG development is provided with special reference to changes in the epithelial architecture and the epithelial basement membrane. The restricted expression patterns of various laminin isoforms in the developing SMGs are also summarized. Furthermore, an overview is given of several lines of experimental evidence that indicate significant but distinct roles for laminin-1 and laminin-10, their individual domains and their receptor-mediated signaling in SMG morphogenesis.

Animals↗
PubMed1980

The role of glycoprotein carbohydrate in the immunological reactivity of antistreptococcal cell-membrane and antiglomerular basement-membrane antisera.

Rabbit antisera to "carbohydrate-rich" antigens prepared from group-A, type-12 streptococcal cell-membrane and human glomerular basement-membrane were found to react by an indirect fluorescent-antibody test with the glomerular basement membrane of adult human kidney. This activity was absent or diminished in neonatal tissue. Removal of the carbohydrate epitopes from the adult tissue by means of carbohydrases removed the immunological activity. Antisera against the "carbohydrate-rich" antigens showed immunological reactivities distinctly different from those against the parent native immunogens--streptococcal cell membrane or glomerular basement membrane--which proved to be directed towards the portein epitopes.

Antigen-Antibody Reactions↗
PubMed1994

Basement membrane and carcinogenesis: ultrastructural observations in the basement membrane of the bladder epithelium in rats treated with N-butyl-N-(4-hydroxybutyl)nitrosamine (BBN).

This study investigated the structural alterations in the basement membrane (BM) of the bladder epithelium in rats treated with N-butyl-N-(4-hydroxybutyl)nitrosamine (BBN) using transmission electron microscopy. Following administration of BBN, thickening of the BM of the bladder epithelium was observed and remained almost constant from 4 to 20 weeks, although the pathological changes in the rat bladder epithelium induced by BBN altered over the same period of 20 weeks. The reason for this phenomenon can be explained by the increased interfacial area between the basal epithelial cells and the BM of the rat bladder epithelium due to an increase in the number and size of the microvilli on the basal cell surfaces adjacent to the BM. Our results also showed that the frequency of hemidesmosomes increased progressively during the period of carcinogenesis, especially in the lesions of noninvasive transitional cell carcinoma (TCC) in the rat bladder. It is suggested that the neosynthesis of BM components can be carried out both by benign hyperplastic cells and by noninvasive TCC cells of rat bladder. The alterations in the BM thickness may be affected by the changes in the number and size of the microvilli occurring on the basal cell surfaces adjacent to the BM. Both an increased frequency of hemidesmosomes and the neosynthesis of BM are closely related to cell proliferation during carcinogenesis.

Animals↗
PubMed1986

Antibodies to basement membrane heparan sulfate proteoglycans bind to the laminae rarae of the glomerular basement membrane (GBM) and induce subepithelial GBM thickening.

Antibodies specific for the core protein of basement membrane HSPG (Mr = 130,000) were administered to rats by intravenous injection, and the pathologic consequences on the kidney were determined at 3 min to 2 mo postinjection. Controls were given antibodies against gp330 (the pathogenic antigen of Heymann nephritis) or normal rabbit IgG. The injected anti-HSPG(GBM) IgG disappeared rapidly (by 1 d) from the circulation. The urinary excretion of albumin increased in a dose-dependent manner during the first 4 d, was increased 10-fold at 1-2 mo, but remained moderate (mean = 12 mg/24 h). By immunofluorescence the anti-HSPG(GBM) was seen to bind rapidly (by 3 min) to all glomerular capillaries, and by immunoperoxidase staining the anti-HSPG was seen to bind exclusively to the laminae rarae of the GBM where it remained during the entire 2-mo observation period. C3 was detected in glomeruli immediately after the injection (3 min), where it bound exclusively to the lamina rara interna; the amount of C3 bound increased up to 2 h but decreased rapidly thereafter, and was not detectable after 4 d. Mononuclear and PMN leukocytes accumulated in glomerular capillaries, adhered to the capillary wall, and extended pseudopodia through the endothelial fenestrae to contact in the LRI of the GBM where the immune deposits and C3 were located. At 1 wk postinjection, staining for C3 reappeared in the glomeruli of some of the rats, and by this time most of the rats, including controls injected with normal rabbit IgG, had circulating anti-rabbit IgG (by ELISA) and linear deposits of rat IgG along the GBM (by immunofluorescence). Beginning at 9 d, there was progressive subepithelial thickening of the GBM which in some places was two to three times its normal width. This thickening was due to the laying down of a new layer of basement membrane-like material on the epithelial side of the GBM, which gradually displaced the old basement membrane layers toward the endothelium. The results show that the core proteins of this population of basement membrane HSPG (Mr = 130,000), which are ubiquitous components of basement membranes, are exposed to the circulation and can bind anti-HSPG(GBM) IgG in the laminae rarae of the GBM. Binding of these antibodies to the GBM leads to changes (C3 deposition, leukocyte adherence, moderate proteinuria, GBM thickening) considered typical of the acute phase of anti-GBM glomerulonephritis. Antibody binding interferes with the normal turnover of the GBM, presumably by affecting the biosynthesis and/or degradation of basement membrane components.

Animals↗
PubMed2000

Distinct antitumor properties of a type IV collagen domain derived from basement membrane.

Vascular basement membrane is an important structural component of blood vessels. During angiogenesis this membrane undergoes many alterations and these changes are speculated to influence the formation of new capillaries. Type IV collagen is a major component of vascular basement membrane, and recently we identified a fragment of type IV collagen alpha2 chain with specific anti-angiogenic properties (Kamphaus, G. D., Colorado, P. C., Panka, D. J., Hopfer, H., Ramchandran, R., Torre, A., Maeshima, Y., Mier, J. W., Sukhatme, V. P., and Kalluri, R. (2000) J. Biol. Chem. 275, 1209-1215). In the present study we characterize two different antitumor activities associated with the noncollagenous 1 (NC1) domain of the alpha3 chain of type IV collagen. This domain was previously discovered to possess a C-terminal peptide sequence (amino acids 185-203) that inhibits melanoma cell proliferation (Han, J., Ohno, N., Pasco, S., Monboisse, J. C., Borel, J. P., and Kefalides, N. A. (1997) J. Biol. Chem. 272, 20395-20401). In the present study, we identify the anti-angiogenic capacity of this domain using several in vitro and in vivo assays. The alpha3(IV)NC1 inhibited in vivo neovascularization in matrigel plug assays and suppressed tumor growth of human renal cell carcinoma (786-O) and prostate carcinoma (PC-3) in mouse xenograft models associated with in vivo endothelial cell-specific apoptosis. The anti-angiogenic activity was localized to amino acids 54-132 using deletion mutagenesis. This anti-angiogenic region is separate from the 185-203 amino acid region responsible for the antitumor cell activity. Additionally, our experiments indicate that the antitumor cell activity is not realized until the peptide region is exposed by truncation of the alpha3(IV)NC1 domain, a requirement not essential for the anti-angiogenic activity of this domain. Collectively, these results effectively highlight the distinct and unique antitumor properties of the alpha3(IV)NC1 domain and the potential use of this molecule for inhibition of tumor growth.

Angiogenesis Inhibitors↗
PubMed1984

Effect of diabetes on in vivo metabolism of [35S]-labeled glomerular basement membrane.

Glomerular basement membrane (GBM) was labeled in vivo by the injection of tracer amounts of [35S]-sulfate into normal and streptozotocin-diabetic rats. The biosynthesis and turnover of sulfated glycosaminoglycans in the GBM was determined from the specific activity of [35S] after pronase digestion of basement membranes purified from glomeruli isolated 1-7 days after injection. Peak radiolabeling of both normal and diabetic GBM occurred 24 h after injection and, when corrected for differences in serum sulfate specific activities, was less in diabetic than in normal samples. The specific activity of GBM sulfate, expressed as cpm/microgram uronic acid, progressively diminished over the ensuing period of study in both normal and diabetic samples. The rate of decrease in specific activity of [35S]-labeled GBM was not significantly different in diabetic preparations compared with that in normal controls. The findings are compatible with diminished sulfation and/or production but normal turnover of glycosaminoglycans in the renal GBM in experimental diabetes.

Animals↗
PubMed1976

Isolation and characterization of an epithelial basement membrane glycoprotein from murine kidney and further characterization of an epithelial basement membrane glycoprotein secreted by murine teratocarcinoma cells in vitro.

A glycoprotein component of epithelial basement membranes (EBM) has been isolated from murine kidney homogenates by extraction with 0.05 M phosphate buffer, pH 7.2, precipitation with (NH4)2SO4 and chromatography on controlled pore glass. Antiserum produced against this glycoprotein reacts specifically with the basement membranes of renal glomeruli and tublules. The EBM glycoprotein of renal origin is antigenically identical with a glycoprotein component of epithelial basement membrane secreted by a murine teratocarcinoma grown in vitro, and the amino acid composition of the two EBM glycoproteins is markedly similar. Both glycoproteins were isolated as high molecular weight aggregates. Disaggregation with sodium dodecyl sulfate and 2-mercaptoethanol resulted in release of monomers of 32 000 and 34 000 daltons for kidney EBM glycoprotein and teratocarcinoma EBM glycoprotein, respectively. The difference in molecular weight is apparently due to increased amounts of fucose, mannose, N-acetylglucosamine and sialic acid in the glycoprotein secreted by the teratocarcinoma. In addition, both EBM glycoproteins contain galactose, glucose and N-acetylgalactosamine.

Amino Acids↗
PubMed1983

Experimental autoimmune glomerulonephritis induced by anti-glomerular basement membrane antibody. II. Effects of injecting heterologous, homologous, or autologous glomerular basement membranes and complete Freund's adjuvant into sheep.

The effects of injecting human, rabbit, rat, or single-kidney homologous glomerular basement membrane (GBM) or autologous GBM, each in complete Freund's adjuvant (CFA), into 15- to 18-month-old sheep are compared. All sheep receiving heterologous GBM and 3 of 6 sheep receiving homologous GBM had anti-GBM nephritis, but such sheep did not bind autoantibodies or have Goodpasturelike lesions in their lungs. Sheep given injections of human GBM had autoantibodies to antigenic determinants shared by fetal or adult sheep and human GBM, by lung basement membranes, and by certain nonvascular basement membranes. Sheep given homologous GBM had two populations of autoantibodies: one was neither species- nor organ-specific; the other was sheep-specific. No sheep given autologous GBM had any evidence of anti-GBM autoantibodies or nephritis. Their kidneys were indistinguishable by histologic, immunohistologic, and functional studies from CFA-treated controls. Thus, sheep seem very tolerant to autologous GBM. These findings suggest that human anti-GBM nephritis may occur if the GBM is altered so that it becomes cross-reacting and induces autoantibodies, as does homologous GBM.

Animals↗
PubMed1994

Basement membrane and tumor invasion: ultrastructural observations in the basement membrane of rat bladder with invasive transitional cell carcinoma induced by N-butyl-N-(4-hydroxybutyl)nitrosamine.

This study describes ultrastructural alterations in the basement membrane (BM) of rat bladder with invasive transitional cell carcinoma (TCC) induced by N-butyl-N-(4-hydroxybutyl)nitrosamine. Various alterations including thickening, degradation and neosynthesis were found in the bladder BM of one rat with invasive TCC. Focal destruction of both the BM lamina zones was found in addition to partially degraded BMs showing focal degradation and loss of only the BM lamina rara. Neosynthesis of complete BM including the lamina rara and lamina densa was observed surrounding the nests of carcinoma cells deep in the stroma, while neosynthesis of incomplete BM including only a lamina densa-like structure was also found around carcinoma cells which had just crossed the BM into the adjacent stroma from the original tumor masses. There was an increased hemidesmosomal frequency in some areas of thickened BM, and focal loss of hemidesmosome in the areas of degraded BM. It is suggested that BM degradation may take place in two steps, and that BM neosynthesis may also be a two-step process in invasive TCC of rat bladder.

Animals↗
PubMed1988

Production and immunohistochemical characterization of monoclonal antibodies directed against renal basement membranes of rats.

Basement membranes were separated from rat glomeruli and purified by mild procedures, which led to a highly enriched basement membrane fraction. Here, the production and characterization of five monoclonal antibodies against tubular and glomerular basement membranes are described. These antibodies were analyzed immunohistochemically on frozen sections of rat, bovine, and human kidneys as well as on rat embryos. One monoclonal antibody (BM O II) exclusively recognized the glomerular basement membranes, another one (BM O VII) bound to tubular basement membranes and to Bowman's capsule. Three antibodies (BM O IV, BM M II, BM M III) recognized their antigens in both glomerular and tubular basement membranes as well as in mesangial cells. The BM O II antibody showed a stringent species specificity and bound only to glomerular basement membranes of the rat. The other four antibodies cross-reacted with human and bovine glomerular basement membrane and mesangial antigens; they also bound to other tissues in the developing rat embryo. Antibody binding to specific purified components of the basement membranes such as collagen type IV, laminin, heparan sulphate proteoglycan, and fibronectin was investigated by enzyme-linked immunosorbent assay (ELISA). None of these antibodies reacted with any of these known basement membrane components, indicating that the antibodies may serve as useful tools in future investigations of so far unidentified components of basement membranes.

Animals↗
PubMed1999

High-resolution ultrastructural comparison of renal glomerular and tubular basement membranes.

BACKGROUND/AIMS: Glomerular basement membranes (GBM) and tubular basement membranes (TBM) consist of a fine meshwork composed mainly of type IV collagen. Each segment of tubules has specialized physiologic functions, and thus we investigated the ultrastructure of various basement membranes in rat kidneys. METHODS: Since purifying basement membranes from different tubule segments is technically challenging, we employed tissue negative staining rather than conventional negative staining to compare the ultrastructures of proximal and distal TBM and GBM in normal rats. We also assessed the distribution of extracellular matrix components including type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin in the basement membranes by immunohistochemistry. RESULTS: TBM and GBM of normal rats showed a fine meshwork structure consisting of fibrils forming small round to oval pores. Short- and long-pore diameters in proximal tubules were 3.3 +/- 0.5 and 3.9 +/- 0.6 nm, respectively, and in distal tubules 3.5 +/- 0.7 and 4.3 +/- 0.8 nm, respectively. For GBM the respective diameters were 2.5 +/- 0.5 and 3.0 +/- 0.5 nm. Immunohistochemical analysis showed no significant difference in distribution of extracellular matrix components between proximal and distal TBM. However, immunofluorescence scores of alpha1 chain of type IV collagen, fibronectin, and laminin were higher in the TBM than in the GBM. On the other hand, heparan sulfate proteoglycan was higher in the GBM. CONCLUSION: Ultrastructural differences in renal basement membranes may be related to differences in physiologic function in each segment.

Animals↗
PubMed1985

Basement membranes in cancer.

Basement membranes are ubiquitous tissue constituents which occur as supportive structure adjacent to epithelium, endothelium, mesothelium and also around smooth as well as striated muscle cells, Schwann cells and fat cells. In various types of cancer, basement membranes have been extensively studied by electron microscopy. Often basement membrane interruptions were seen in invasive neoplasms but in some tumors the neoplastic cells were surrounded by a continuous basal lamina. Recent immunocytochemical studies have shown that in invasive carcinomas the neoplastic cells often lack a continuous basement membrane. This may be caused by catabolic activity of invasive tumor cells, which have been shown to produce specific collagenases, or by insufficient production and/or extracellular assembly of basement membrane components by the neoplastic epithelial cells. In diagnostic histopathology, immunocytochemical staining of basement membrane components such as type IV collagen and laminin may help to distinguish between noninvasive (benign or in situ) and invasive lesions. Furthermore, in carcinomas the extent of the expression of basement membrane components may be correlated with the degree of differentiation of the neoplastic cells. Finally, in soft tissue tumors, basement membrane staining may be helpful for the differentiation of basement membrane producing neoplasms (e.g. of vascular, neural, smooth muscle or striated muscle origin) from non-basement membrane producing neoplasms (e.g. of fibroblastic origin).

Basement Membrane↗
PubMed1975

Basement membranes: structural and biosynthetic considerations.

Basement membranes are extracellular matrices synthesized by a variety of cells including the basal cells of the epidermis; the respiratory, gastrointestinal, and glandular epithelium; the capillary endothelium; the epithelial cells of the glomerulus, the renal tubule, and the lens capsule; and the endothelium of Descemet's membrane. Basement membranes in the mature animal are free of lipids, DNA, and proteoglycans and are composed of dissimilar protein subunits. One of these is a procollagen-like molecule associated with a noncollagenous matrix glycoprotein. The proportion of the latter component varies among basement membranes. These various subunits are stabilized by hydrogen bonds, disulfide bonds, and aldehyde-derived cross-links which are so extensive that they render the basement membranes highly insoluble. Immunochemical studies indicate three distinct antigenic components which correspond to the collagenous moiety, its nonhelical extension, and the matrix glycoprotein. The collagen component of basement membranes, free of the nonhelical extension, is composed of three identical alpha-chains. It is highly rich in hydroxylysine, 3- and 4-hydroxyproline and contains 4 to 8 residues of half-cystine. It contains 38 residues of glucosyl-galactosyl-hydroxylysine per chain and minimal amounts of mannose, glucosamine, and fucose. Newly synthesized basement membrane collagen is secreted in the extracellular space as the precursor molecule "procollagen." This molecule does not undergo conversion to collagen but interacts with the matrix glycoprotein to give rise to the appropriate structure.

Amino Acids↗
PubMed1986

Basement membrane as a spatial organizer of polarized epithelia. Exogenous basement membrane reorients pancreatic epithelial tumor cells in vitro.

The authors have previously described a transplantable pancreatic acinar carcinoma that comprises cells which reorganize and display normal epithelial orientation only when in contact with basement membrane (BM) in vivo. In the present study, they investigated whether exogenous acellular BM or collagenous stroma (prepared from human amnion) was sufficient to reorient pancreatic acinar tumor cells in vitro. Mechanically dispersed tumor cells could not spontaneously attach to standard culture substrata; yet they adhered to exogenous intact BM or to dishes coated with purified laminin or Type IV collagen. Cell contact with amniotic BM resulted in tumor cell shape changes, assembly of intracellular actin into fibrous bundles, and restoration of normal epithelial cell-cell interactions. Computerized morphometry confirmed that tumor cells exhibited a normal polarized distribution of lipid droplets, nuclei, Golgi complexes, and zymogen granules (from base to apex) within 6 hours of culture on BM. Adhering zonules and microvilli were observed only along apical tumor cell surfaces, although full junctional complexes and distinct membrane domains did not reform. Similar attachment, cytoskeletal alterations, and reorientation occurred in the absence of protein synthesis (25 micrograms/ml cycloheximide). In contrast, tumor cells that were maintained on amniotic stroma remained round, displayed circumferential rings of actin, and appeared randomly oriented. Thus, BM may normally serve to integrate and maintain individual cells within a polarized epithelium.

Amnion↗
PubMed1994

Specific changes in the basement membrane of the proximal tubules in the murine polycystic kidney detected by the novel anti-basement membrane monoclonal antibody D28.

In order to analyze renal abnormalities in mice with polycystic kidney disease (PKD), we produced a series of monoclonal antibodies reactive with the murine kidney by hybridizing P3U1 myeloma cells with spleen cells from DBA/2 mice immunized with the kidney of adult-type PKD mice, DBA/2FG-pcy. One clone, D28, reacted specifically with the basement membrane of the proximal tubules of DBA/2 mice and DBA/2FG-pcy mice. It did not react with other parts of the murine kidney nor with other tissues such as the skin, ovary, fallopian tube, testis, lung and small intestine. While other components such as collagen IV, laminin and the core protein of proteoglycan could be found, the D28 epitope could not be found in the basement membrane of renal cysts formed in adult-type (DBA/2FG-pcy) and infant-type (C57BL/6J-cpk) PKD mice. The D28 epitope did not, however, disappear from the basement membrane of proximal tubules in other types of renal abnormalities. These results suggest that the formation of renal cysts in the proximal tubules is associated with an alteration to the proximal tubule-specific structure of the basement membrane. The D28 monoclonal antibody should prove a useful tool with which to analyze basement membrane-associated abnormalities in genetic PKD.

Animals↗