scholarly journals What is Known of the Production of Basement Membrane Components

1983 ◽  
Vol 31 (1A_suppl) ◽  
pp. 159-163 ◽  
Author(s):  
G.W. Laurie ◽  
C.P. Leblond
Keyword(s):  
Golgi Apparatus ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Secretory Granules ◽  
Basement Membranes ◽  
Type Iv ◽  
Stage Of Development ◽  
Membrane Components ◽  
Endodermal Cells ◽  
Basement Membrane Components

Immunohistochemistry was used to identify basement membrane components and examine their production by associated cells. Four substances were identified in a series of basement membranes in rats aged 20 days to 34 months, namely, type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin. They were then all localized to the basal lamina part of basement membranes and, presumably, are integrated within this layer. The production of type IV collagen was first examined in the embryonic endodermal cells associated with Reichert's membrane in the rat parietal yolk sac. The rough endoplasmic reticulum (rER), Golgi apparatus, and putative secretory granules of endodermal cells were immunostained, suggesting that these organelles participated in the biogenesis of type IV collagen. However, in rats aged 20 days or more, the cells associated with basement membranes were usually unstained. An exception was noted in the continually growing incisor tooth where the endothelial cells at the proliferating end usually showed immunostaining of rER and Golgi apparatus. It is, therefore, proposed that the formation of type IV collagen for basement membrane occurs at an early stage of development in the life of producer cells. Little is known of the formation of other basement membrane components during development, but there is immunohistochemical evidence that laminin and fibronectin are produced along the same secretory pathway as type IV collagen.

Differential deposition of basement membrane components during formation of the caudal neural tube in the mouse embryo

Development ◽  
1987 ◽  
Vol 99 (4) ◽  
pp. 509-519
Author(s):  
K.S. O'Shea
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Heparan Sulphate ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan ◽  
Secondary Neurulation ◽  
Type Iv ◽  
Posterior Neuropore ◽  
Membrane Components ◽  
Basement Membrane Components

The distribution of basement membrane and extracellular matrix components laminin, fibronectin, type IV collagen and heparan sulphate proteoglycan was examined during posterior neuropore closure and secondary neurulation in the mouse embryo. During posterior neuropore closure, these components were densely deposited in basement membranes of neuroepithelium, blood vessels, gut and notochord; although deposition was sparse in the midline of the regressing primitive streak. During secondary neurulation, mesenchymal cells formed an initial aggregate near the dorsal surface, which canalized and merged with the anterior neuroepithelium. With aggregation, fibronectin and heparan sulphate proteoglycan were first detected at the base of a 3- to 4-layer zone of radially organized cells. With formation of a lumen within the aggregate, laminin and type IV collagen were also deposited in the forming basement membrane. During both posterior neuropore closure and secondary neurulation, fibronectin and heparan sulphate proteoglycan were associated with the most caudal portion of the neuroepithelium, the region where newly formed epithelium merges with the consolidated neuroepithelium. In regions of neural crest migration, the deposition of basement membrane components was altered, lacking laminin and type IV collagen, with increased deposition of fibronectin and heparan sulphate proteoglycan.

scholarly journals Heterogenous distribution of type IV collagen, entactin, heparan sulfate proteoglycan, and laminin among renal basement membranes as demonstrated by quantitative immunocytochemistry.

1989 ◽  
Vol 37 (6) ◽  
pp. 885-897 ◽  
Author(s):  
M Desjardins ◽  
M Bendayan
Keyword(s):  
Heparan Sulfate ◽  
Type Iv Collagen ◽  
Protein A ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Sulfate Proteoglycan ◽  
Type Iv ◽  
Membrane Components ◽  
Convoluted Tubules ◽  
Basement Membrane Components

Type IV collagen, entactin, heparan sulfate proteoglycan, and laminin antigenic sites were revealed on various rat renal basement membranes by use of protein A-gold immunocytochemistry. The basement membranes of the proximal and distal convoluted tubules, those of Bowman's capsule and glomerulus, and the mesangial matrix were labeled for all the antigens but to differing extents. Control experiments confirmed the specificity of these labelings. Quantitative evaluation revealed an important heterogeneity for each antigen among the various basement membranes. This heterogeneity suggests that the basement membrane components must arrange themselves in different ways, possibly to account for differences in functional properties of the various renal structures.

scholarly journals Immunohistochemical evidence for the intracellular formation of basement membrane collagen (type IV) in developing tissues.

1980 ◽  
Vol 28 (12) ◽  
pp. 1267-1274 ◽  
Author(s):  
G W Laurie ◽  
C P Leblond ◽  
I Cournil ◽  
G R Martin
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Early Stage ◽  
Basement Membranes ◽  
Incisor Tooth ◽  
Rat Incisor ◽  
Type Iv ◽  
Stage Of Development ◽  
Basement Membrane Collagen ◽  
Membrane Collagen

Antibodies to type IV collagen obtained from the basement membrane of the mouse EHS tumor were incubated with sections of rat incisor teeth and other tissues for immunostaining by direct or indirect methods. In all locations, the immunostaining was pronounced in basement membranes in which it was restricted to the "basal lamina" layer, from which "bridges" often extended to nearby basal laminae. Usually no immunostaining was detectable in the cells associated with the basement membranes. However, examination of the capillaries at the posterior extremity of the rat incisor tooth, where tissues are at an early stage of development, showed immunostaining not only of the basement membrane, but also of the endothelial cells. The staining was localized in rough endoplasmic reticulum cisternae, some Golgi saccules and their peripheral distensions, and structures believed to be secretory granules. These findings suggest that the synthesis of type IV collagen proceeds along the classical secretory pathways through rough endoplasmic reticulum and Golgi apparatus. At the same time, immunostaining was usually lacking in the cells of the capillaries that had migrated about 2 mm away from the posterior end of the incisor tooth and also in the cells of most other tissues examined, even though the associated basal laminae were reactive. It is, therefore, presumed that the production of type IV collagen may be high in cells at an early stage of development and that any later production and turnover of basement membrane collagen can only be minimal.

Bleomycin and cyclophosphamide increase pulmonary type IV procollagen mRNA in mice

1990 ◽  
Vol 259 (2) ◽  
pp. L47-L52
Author(s):  
D. G. Hoyt ◽  
J. S. Lazo
Keyword(s):  
Gene Expression ◽  
Steady State ◽  
Pulmonary Fibrosis ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Subcutaneous Infusion ◽  
Type Iv ◽  
Steady State Levels ◽  
Membrane Components ◽  
Basement Membrane Components

Constant 7-day subcutaneous infusion of bleomycin (100 mg/kg) induces pulmonary fibrosis in C57Bl/6N mice, whereas BALB/cN mice are relatively resistant. In contrast, cyclophosphamide (200 mg/kg, ip) induces fibrosis in BALB/cN mice, whereas C57Bl/6N mice are resistant. The effect of these drugs on the pulmonary levels of mRNA encoding the major basement membrane components, laminin and type IV collagen, relative to poly (A+)RNA was determined in both C57Bl/6N and BALB/cN mice. In the sensitive C57Bl/6N mice, bleomycin increased alpha 1IV and alpha 2IV procollagen mRNA/poly (A+)RNA twofold in the absence of increases in laminin A, B1, and B2 mRNA/poly (A+)RNA. In the relatively resistant BALB/cN mice, bleomycin did not alter alpha 1IV procollagen mRNA/poly (A+)RNA and only transiently increased laminin A, B1, B2, and alpha 2IV procollagen mRNA/poly (A+)RNA. Similarly, cyclophosphamide increased alpha 1IV and alpha 2IV procollagen mRNA/poly (A+)RNA twofold in the sensitive BALB/cN mice and not in C57Bl/6N mice. Laminin mRNAs/poly (A+)RNA were not increased by cyclophosphamide in either strain. Thus, in these models, pulmonary fibrosis is preceded by a coordinate increase in steady-state levels of mRNA encoding basement membrane procollagen but is not associated with an increase in laminin gene expression

Immunohistochemical Distribution of Basement Membrane Type IV Collagen and Laminin in Synovial Sarcoma

1993 ◽  
Vol 79 (6) ◽  
pp. 427-432 ◽  
Author(s):  
Marcello Guarino
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Spindle Cell ◽  
Epithelial Tissue ◽  
Cell Component ◽  
Spindle Cell Component ◽  
Type Iv ◽  
Synovial Sarcomas ◽  
Membrane Components ◽  
Basement Membrane Components

Aims To investigate the distribution of basement membrane components type IV collagen and laminin in synovial sarcomas. Methods Paraffin sections from four synovial sarcomas were studied by the peroxidase-antiperoxldase procedure using specific antibodies to type IV collagen and laminin. Results Type IV collagen and laminin immunoreactivity was confined around epithelial areas in biphasic tumors. Several interruptions and discontinuities of the linear basement membrane profile were seen in sites of transition between mesenchymal and epithelial tissue. Moreover, a spot-like immunoreactivity was often observed in the spindle cell component of biphasic tumors. Monophasic tumors were either negative or showed a pericellular staining for both type IV collagen and laminin. Conclusions The distribution of basement membrane components is clearly related to the formation of epithelial elements in biphasic synovial sarcoma. The spot-like immunoreactivity of the spindle cell component, and the basement membrane interruptions at the boundary between mesenchymal and epithelial tissue, are both consistent with early basement membrane formation by developing epithelium. These findings support the concept that synovial sarcomas are basically soft tissue carcinosarcomas and that the epithelial component of the tumors develops by conversion of mesenchyme to epithelium.

Production and polarized secretion of basement membrane components by glomerular epithelial cells

1992 ◽  
Vol 262 (1) ◽  
pp. F131-F137 ◽  
Author(s):  
Y. Natori ◽  
Y. M. O'Meara ◽  
E. C. Manning ◽  
A. W. Minto ◽  
J. S. Levine ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Enzyme Linked Immunosorbent Assay ◽  
Type Iv ◽  
Polarized Secretion ◽  
Glomerular Epithelial Cells ◽  
Basolateral Side ◽  
Membrane Components ◽  
Basement Membrane Components

To study the formation of basement membrane by glomerular epithelial cells (GECs), production and secretion of type IV collagen and laminin by rat GECs in culture were evaluated. GECs produced two chains of type IV collagen (180 and 170 kDa) in the ratio of approximately 2 to 1, when immunoprecipitated with antibody to type IV collagen of mouse Engelbreth-Holm-Swarm (EHS) sarcoma. GECs also produced proteins that were precipitated by antibody to EHS laminin, i.e., two bands each in the positions of the A and B chains of mouse laminin. On enzyme-linked immunosorbent assay (ELISA), type IV collagen and laminin were found mainly in the cell-associated fraction and in the subepithelial culture medium. Confluent GECs on membrane filters formed a tight barrier against the flux of macromolecules. Under these conditions, 80% of newly synthesized and secreted matrix proteins were detected in the basolateral medium. Moreover, treatment with ammonium chloride, which is known to affect polarized secretion, caused both type IV collagen and laminin to be secreted via the basolateral and apical surfaces in similar amounts. These results indicate that cultured GECs are polarized and that they produce and secrete basement membrane components via the basolateral side.

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