scholarly journals Comparative distribution of laminin, type IV collagen, and fibronectin in the rat glomerulus.

1982 ◽  
Vol 30 (9) ◽  
pp. 874-886 ◽  
Author(s):  
P J Courtoy ◽  
R Timpl ◽  
M G Farquhar
Keyword(s):  
Type Iv Collagen ◽  
Rat Kidney ◽  
Basement Membranes ◽  
Kidney Cortex ◽  
Mesangial Matrix ◽  
Lamina Densa ◽  
Rat Kidney Cortex ◽  
Type Iv ◽  
Attachment Proteins ◽  
Cryostat Sections

The distribution of laminin, type IV collagen, and fibronectin was investigated in the rat kidney cortex by immunolabeling. It was demonstrated by immunofluorescence on both unfixed cryostat sections and fixed ultracryomicrotome sections, by immunoperoxidase on fixed cryostat sections, and by immunoferritin on isolated glomerular basement membranes (GBM). This multifaceted approach provided complementary and convergent results. Distinct patterns were found for each antigen in the glomerulus and remaining kidney cortex. Laminin was localized predominantly in the GBM, where it was concentrated in the laminae rarae. Staining also occurred to a lesser extent in the mesangial matrix. Type IV collagen was evenly distributed in the lamina densa of the GBM and in the mesangial matrix. Fibronectin was most abundant in the mesangial matrix, but it could also be detected in the peripheral GBM, where it was localized in the laminae rarae. Labeling for fibronectin was particularly prominent at the endothelial-mesangial interface. The findings indicate that the three layers of the GBM differ in their composition: The lamina densa contains type IV collagen and the laminae rarae contain the two attachment proteins, fibronectin and laminin. The mesangial matrix stains for all three antigens, but it is also heterogeneous and can be subdivided into several domains--i.e., the endothelial-mesangial matrix, which is particularly rich in fibronectin, the intermesangial matrix, which contains mainly type IV collagen and fibronectin, and the GBM (where it continues over the mesangial regions), which stains most heavily for laminin.

scholarly journals Effects of experimental nephrosis on basement-membrane components and enzymes of collagen biosynthesis in rat kidney

1985 ◽  
Vol 226 (1) ◽  
pp. 243-250 ◽  
Author(s):  
A Jukkola ◽  
J Risteli ◽  
H Autio-Harmainen ◽  
L Risteli
Keyword(s):  
Membrane Proteins ◽  
Basement Membrane ◽  
Indirect Immunofluorescence ◽  
Type Iv Collagen ◽  
Rat Kidney ◽  
Kidney Tissue ◽  
Kidney Cortex ◽  
Collagen Biosynthesis ◽  
Type Iv ◽  
Basement Membrane Proteins

The aim of the present study was to find out whether the basement-membrane proteins laminin and type IV collagen are involved in the development of aminonucleoside-induced nephrosis. These proteins were measured by specific radioimmunoassays in serum, urine and kidney-cortex samples, and they were localized in the glomeruli by indirect immunofluorescence. Nephrosis was induced in rats with a single intraperitoneal injection of puromycin aminonucleoside. Serum laminin concentrations, detected by a radioimmunoassay for the P2 domain of the protein, increased to reach a maximum at days 5-7, and they remained elevated until at least day 14. The increase preceded the development of proteinuria, suggesting a role for laminin in glomerular function. Concomitant with proteinuria, increasing amounts of laminin antigenicity were also found in the urine. The size of the laminin antigen in serum was estimated by gel filtration, and the serum forms were found to contain both the P1 and the P2 regions of the intact laminin molecule. On the other hand, there were no changes in the serum or urinary concentrations of type-IV-collagen-derived antigens, as detected by a radioimmunoassay for the 7S collagen domain of this protein. The total content of laminin in kidney cortex, measured after digestion of the tissue with trypsin and collagenase, was, at day 9, still comparable with normal values, and the distribution of both basement-membrane proteins in the glomeruli, studied by indirect immunofluorescence, was similar to that in the controls. The tissue damage induced by aminonucleoside, however, seems to stimulate collagen biosynthesis, as the activities of prolyl 4-hydroxylase, lysyl hydroxylase and galactosylhydroxylysyl glucosyltransferase in kidney tissue increased significantly, with maxima at days 8-10.

scholarly journals An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin.

1994 ◽  
Vol 126 (5) ◽  
pp. 1319-1327 ◽  
Author(s):  
G P Kaushal ◽  
P D Walker ◽  
S V Shah
Keyword(s):  
Extracellular Matrix ◽  
Proteinase Inhibitors ◽  
Rat Kidney ◽  
Gel Filtration ◽  
Biochemical Properties ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Type Iv ◽  
Extracellular Matrix Components

We have purified to homogeneity the enzyme in the kidney cortex which accounts for the vast majority of matrix-degrading activity at neutral pH. The purified enzyme has an apparent molecular mass of 350 kD by gel filtration and of 85 kD on SDS-PAGE under reducing conditions; and it degrades laminin, type IV collagen and fibronectin. The enzyme was inhibited by EDTA and 1,10-phenanthroline, but not by other proteinase inhibitors. The enzyme was not activated by organomercurials or by trypsin and was not inhibited by tissue inhibitors of metalloproteinases indicating that it is distinct from the other matrix-degrading metalloproteinases. Unexpectedly, the amino acid sequence of the NH2-terminal and two internal peptides of the enzyme showed complete homology to those alpha subunits of rat meprin, an enzyme previously shown to degrade azocasein and insulin B chain but not known to degrade extracellular matrix components. Immunoprecipitation studies, Western blot analyses and other biochemical properties of the purified enzyme confirm that the distinct matrix-degrading enzyme is indeed meprin. Our data also demonstrate that meprin is the major enzyme in the renal cortex capable of degrading components of the extracellular matrix. The demonstration of this hitherto unknown function of meprin suggests its potential role in renal pathophysiology.

scholarly journals Immunogold quantitation of laminin, type IV collagen, and heparan sulfate proteoglycan in a variety of basement membranes.

1988 ◽  
Vol 36 (3) ◽  
pp. 271-283 ◽  
Author(s):  
D S Grant ◽  
C P Leblond
Keyword(s):  
Heparan Sulfate ◽  
Type Iv Collagen ◽  
Collagen Iv ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Enamel Organ ◽  
Sulfate Proteoglycan ◽  
Lamina Densa ◽  
Type Iv ◽  
Reichert's Membrane

A series of basement membranes was immunolabeled for laminin, type IV collagen, and heparan sulfate proteoglycan in the hope of comparing the content of these substances. The basement membranes, including thin ones (less than 0.3 micron) from kidney, colon, enamel organ, and vas deferens, and thick ones (greater than 2 micron), i.e., Reichert's membrane, Descemet's membrane, and EHS tumor matrix, were fixed in formaldehyde, embedded in Lowicryl, and treated with specific antisera or antibodies followed by anti-rabbit immunoglobulin bound to gold. The density of gold particles, expressed per micron2, was negligible in controls (less than or equal to 1.1), but averaged 307, 146, and 23, respectively, for laminin, collagen IV, and proteoglycan over the thick basement membranes (except for Descemet's membranes, over which the density was 16, 5, and 34, respectively) and 117, 72, and 64, respectively, over the lamina densa of the thin basement membranes. Lower but significant reactions were observed over the lamina lucida. Interpretation of the gold particle densities was based on (a) the similarity between the ultrastructure of most thick basement membranes and of the lamina densa of most thin basement membranes, and (b) the biochemical content of the three substances under study in the EHS tumor matrix (Eur J Biochem 143:145, 1984). It was proposed that thick basement membranes (except Descemet's) contained more laminin and collagen IV but less heparan sulfate proteoglycan than the lamina densa of thin basement membranes. In the latter, there was a fair variation from tissue to tissue, but a tendency towards a similar molar content of the three substances.

scholarly journals Deletion of the Laminin α4 Chain Leads to Impaired Microvessel Maturation

2002 ◽  
Vol 22 (4) ◽  
pp. 1194-1202 ◽  
Author(s):  
Jill Thyboll ◽  
Jarkko Kortesmaa ◽  
Renhai Cao ◽  
Raija Soininen ◽  
Ling Wang ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Histological Examination ◽  
Peripheral Nerves ◽  
Type Iv Collagen ◽  
Neonatal Period ◽  
Basement Membranes ◽  
Lamina Densa ◽  
Newborn Mice ◽  
Type Iv ◽  
Developing Muscle

ABSTRACT The laminin α4 chain, a component of laminin-8 and -9, is expressed in basement membranes, such as those beneath endothelia, the perineurium of peripheral nerves, and around developing muscle fibers. Laminin α4-null mice presented with hemorrhages during the embryonic and neonatal period and had extensive bleeding and deterioration of microvessel growth in experimental angiogenesis, as well as mild locomotion defects. Histological examination of newborn mice revealed delayed deposition of type IV collagen and nidogen into capillary basement membranes, and electron microscopy showed discontinuities in the lamina densa. The results demonstrate a central role for the laminin α4 chain in microvessel growth and, in the absence of other laminin α chains, in the composition of endothelial basement membranes.

scholarly journals Increase of Na/Pi-cotransport encoding mRNA in response to low Pi diet in rat kidney cortex.

1994 ◽  
Vol 269 (9) ◽  
pp. 6637-6639
Author(s):  
A. Werner ◽  
S.A. Kempson ◽  
J. Biber ◽  
H. Murer
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Cytochrome P-450K of rat kidney cortex microsomes: Further studies on its interaction with fatty acids

1973 ◽  
Vol 158 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Åke Ellin ◽  
Sten Orrenius ◽  
Åke Pilotti ◽  
Carl-Gunnar Swahn
Keyword(s):  
Fatty Acids ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

scholarly journals Studies on the orientation of brush-border membrane vesicles

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Freeze Fracture ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Immunological Methods ◽  
Kidney Cortex ◽  
Asymmetric Distribution ◽  
Rat Kidney Cortex

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.

Type IV Collagen Immunostaining Is a Simple, Reliable Diagnostic Tool for Distinguishing Between Adenomatous and Normal Pituitary Glands

2007 ◽  
Vol 131 (6) ◽  
pp. 931-935 ◽  
Author(s):  
Jason Jarzembowski ◽  
Ricardo Lloyd ◽  
Paul McKeever
Keyword(s):  
Pituitary Adenomas ◽  
Type Iv Collagen ◽  
Basement Membranes ◽  
Immunohistochemical Detection ◽  
Secondary Effects ◽  
Hormone Production ◽  
Clonal Population ◽  
Normal Gland ◽  
Type Iv ◽  
Pituitary Glands

Abstract Context.—Pituitary adenomas are clinically diagnosed based on radiologic studies and/or secondary effects of hormone production. Definitive pathologic identification relies on immunohistochemical detection of a clonal population of hormone-producing cells. However, not all adenomas secrete hormones, so performing a battery of stains is inefficient. Reports have shown decreased type IV collagen in the stroma of other epithelial tumors. Objective.—To validate type IV collagen immunohistochemistry as a diagnostic method. Design.—We immunostained 27 adenomas and 19 normal pituitaries. The areas with the sparsest type IV collagen fibers were viewed at 3 magnifications (×10, ×20, and ×40 objectives), counting 1, 3, or 10 microscopic fields. A field was scored as “traversable” if a path existed from any point on the periphery of the field to a point on the approximately opposite periphery that did not cross any stained fibers. Results were compared with reticulin staining and to the existing diagnosis previously determined by histology, hormone immunostaining, and clinical correlation. Results.—Adenomas have less type IV collagen in their basement membranes, leading to sparser, trabecular staining in neoplasms versus a more rigid meshwork pattern in normal glands. One might envision the stained fibers as maze walls—one can traverse medium-powered fields in an adenoma, but one hits dead ends and gets trapped in those of a normal gland. Finding a single representative ×10 field to be traversable was 97.5% sensitive and 96.5% specific for an adenoma. Reticulin staining yielded identical results. Conclusions.—Type IV collagen immunostaining is a simple and reliable method of diagnosing pituitary adenomas.

The relationship between emerging neural crest cells and basement membranes in the trunk of the mouse embryo: a TEM and immunocytochemical study

Development ◽  
1986 ◽  
Vol 98 (1) ◽  
pp. 251-268
Author(s):  
J. Sternberg ◽  
S. J. Kimber
Keyword(s):  
Neural Crest ◽  
Neural Tube ◽  
Cell Shape ◽  
Type Iv Collagen ◽  
Neural Crest Cell ◽  
Basement Membranes ◽  
Type Iv ◽  
Transmission Electron ◽  
The Relationship ◽  
Crest Cell

The earliest stage of neural crest cell (NCC) migration is characterized by an epitheliomesenchymal transformation, as the cells leave the neural tube. There is evidence that in a number of cell systems this transformation is accompanied by alteration or depletion of associated basement membranes. This study examines the ultrastructural relationship between mouse NCCs and adjacent basement membranes during the earliest stages of migration from the neural tube. Basement membranes were identified by transmission electron microscopy (TEM) and immunofluorescence using antibodies to type-IV collagen. The ultrastructural features of NCCs and their relationship with surrounding tissues were also examined using TEM. In the dorsal region of the neural tube, from which NCCs originate, the basement membrane was depleted or absent, and with the immunofluorescence technique it was shown that this pattern was reflected in a deficit of type-IV collagen. TEM observations indicated that ultrastructurally NCCs differ from their neuroepithelial neighbours only in overall cell shape and their relationship to other cells and the extracellular matrix.

Endogenous Kallikrein Inhibitor in Rat Kidney Cortex-Effect of Glucocorticoid Administration

1986 ◽  
pp. 361-365 ◽  
Author(s):  
Kodo Ito ◽  
Kenichi Yamada ◽  
Setsuko Yoshida ◽  
Keiji Hasunuma ◽  
Yasushi Tamura ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Kallikrein Inhibitor ◽  
Glucocorticoid Administration
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