scholarly journals Elevated glucose decreases the content of a basement membrane associated heparan sulphate proteoglycan in proliferating cultured porcine mesangial cells

Diabetologia ◽  
1992 ◽  
Vol 35 (2) ◽  
pp. 183-186 ◽  
Author(s):  
B. Olgem�ller ◽  
S. Schwaabe ◽  
K. D. Gerbitz ◽  
E. D. Schleicher
Keyword(s):  
Basement Membrane ◽  
Mesangial Cells ◽  
Heparan Sulphate ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan ◽  
Elevated Glucose

scholarly journals Development of an Enzyme Immunoassay Specific for a Core Protein Epitope of a Novel Small Basement Membrane Associated Heparan Sulphate Proteoglycan from Human Kidney

1997 ◽  
Vol 35 (2) ◽  
Author(s):  
Georg Stöcker ◽  
Elmar Stickeler ◽  
Silke Switalla ◽  
Dagmar-Christiane Fischer ◽  
Helmut Greiling ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Enzyme Immunoassay ◽  
Core Protein ◽  
Heparan Sulphate ◽  
Human Kidney ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan

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 Biosynthesis of sulphated macromolecules by rabbit lens epithelium. II. Relationship to basement membrane formation.

1984 ◽  
Vol 99 (3) ◽  
pp. 861-869 ◽  
Author(s):  
J G Heathcote ◽  
R R Bruns ◽  
R W Orkin
Keyword(s):  
Basement Membrane ◽  
Type I Collagen ◽  
Heparan Sulphate ◽  
Significant Proportion ◽  
Type I ◽  
Heparan Sulphate Proteoglycan ◽  
Membrane Formation ◽  
Sulphate Proteoglycan ◽  
Type Iv ◽  
Rabbit Lens

Rabbit lens epithelial cells display a similar "cobblestone" morphology and produce the same complement of sulphated macromolecules (also see Heathcote, J.G., and R.W. Orkin, 1984, J. Cell Biol., 99:852-860) whether grown on plastic or glass, dried films of gelatin or type IV collagen with laminin, or on gels of type I collagen. There was no evidence of basement membrane formation by these cells when they were grown on plastic, glass, or dried films. In contrast, cultures that had been grown on gels deposited a discrete basement membrane that followed the contours of the basal surfaces of the cells and in addition, they secreted amorphous basement membrane-like material that diffused into the interstices of the gel and associated with the collagen fibrils of the gel. A significant proportion (approximately 70%) of the heparan sulphate proteoglycan fraction that was secreted into the culture medium (fraction MI) when the cells were grown on plastic became associated with the cell-gel layer in the gel cultures. Further, when basement membrane was isolated by detergent extraction, greater than 90% of the 35S-labeled material present was in this heparan sulphate proteoglycan.

scholarly journals Isolation and partial characterization of heparan sulphate proteoglycan from the human glomerular basement membrane

1989 ◽  
Vol 264 (2) ◽  
pp. 457-465 ◽  
Author(s):  
L P W J van den Heuvel ◽  
J van den Born ◽  
T J A M van de Velden ◽  
J H Veerkamp ◽  
L A H Monnens ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Molecular Mass ◽  
Core Protein ◽  
Mammalian Species ◽  
Heparan Sulphate ◽  
Basement Membranes ◽  
Heparan Sulphate Proteoglycan ◽  
Average Molecular Mass ◽  
Sulphate Proteoglycan ◽  
Core Proteins

Heparan sulphate proteoglycan was solubilized from human glomerular basement membranes by guanidine extraction and purified by ion-exchange chromatography and gel filtration. The yield of proteoglycan was approx. 2 mg/g of basement membrane. The glycoconjugate had an apparent molecular mass of 200-400 kDa and consisted of about 75% protein and 25% heparan sulphate. The amino acid composition was characterized by a high content of glycine, proline, alanine and glutamic acid. Hydrolysis with trifluoromethanesulphonic acid yielded core proteins of 160 and 110 kDa (and minor bands of 90 and 60 kDa). Alkaline NaBH4 treatment of the proteoglycan released heparan sulphate chains with an average molecular mass of 18 kDa. HNO2 oxidation of these chains yielded oligosaccharides of about 5 kDa, whereas heparitinase digestion resulted in a more complete degradation. The data suggest a clustering of N-sulphate groups in the peripheral regions of the glycosaminoglycan chains. A polyclonal antiserum raised against the intact proteoglycan showed reactivity against the core protein. It stained all basement membranes in an intense linear fashion in immunohistochemical studies on frozen kidney sections from man and various mammalian species.

scholarly journals Characterization of proteoglycans synthesized by human adult glomerular mesangial cells in culture

1991 ◽  
Vol 277 (1) ◽  
pp. 81-88 ◽  
Author(s):  
G J Thomas ◽  
R M Mason ◽  
M Davies
Keyword(s):  
Culture Medium ◽  
Mesangial Cells ◽  
Cell Layer ◽  
Heparan Sulphate ◽  
Glomerular Mesangial Cells ◽  
Heparan Sulphate Proteoglycan ◽  
Dermatan Sulphate ◽  
Sulphate Proteoglycan ◽  
Human Adult ◽  
Core Proteins

1. The newly synthesized proteoglycans from human adult glomerular mesangial cells labelled in vitro for 24 h with [35S]sulphate have been characterized using biochemical and immunological techniques. 2. The following proteoglycans were identified (% of total synthesized). (i) A large chondroitin sulphate proteoglycan, CSPG-I, Mr approximately 1 x 10(6) (10.6%). This proteoglycan consisted of a protein core of Mr approximately 4 x 10(5) and glycosaminoglycan chains of Mr 2.5 x 10(4), and was present in both the cell layer and the culture medium. (ii) A major small dermatan sulphate proteoglycan, DSPG-I, Mr 3.5 x 10(5) (46%), which was mainly located in the culture medium. (iii) A second minor small dermatan sulphate, DSPG-II, Mr approximately 2 x 10(5) (9.8%). This molecule was exclusively located in the culture medium. (iv) A large heparan sulphate proteoglycan, HSPG-I, Mr 8 x 10(5) (3.3%). (v) A second large heparan sulphate proteoglycan HSPG-II, Mr approximately 6 x 10(5) (23%). HSPG-I and HSPG-II were extracted from both the culture medium and the cell layer. 3. Western blot analysis of the core proteins released by chondroitin ABC lyase treatment of DSPG-I and DSPG-II identified these dermatan sulphate proteoglycans as biglycan and decorin respectively. Both DSPG-I and DSPG-II had core proteins of Mr 45,000. 4. The cell-layer-associated forms of CSPG-I, HSPG-I and HSPG-II were accessible to limited trypsin treatment, bound to octyl-Sepharose and could be inserted into liposomes, indicating a possible cell membrane location. 5. Pulse-chase experiments indicated that the cell-layer-associated [35S]proteoglycans undergo limited metabolism to inorganic [35S]sulphate, the majority of which is accounted for by the degradation of HSPG-II and to a lesser extent DSPG-I.

Increased basement membrane heparan sulphate proteoglycan in serum of diabetic rats

1988 ◽  
Vol 48 (4) ◽  
pp. 379-380 ◽  
Author(s):  
M. Paulsson ◽  
R. Timpl ◽  
D. Brock ◽  
H. Neubauer
Keyword(s):  
Basement Membrane ◽  
Heparan Sulphate ◽  
Diabetic Rats ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan

Urinary Heparan Sulphate Proteoglycan Excretion is Abnormal in Insulin Dependent Diabetes

1995 ◽  
Vol 32 (6) ◽  
pp. 557-560 ◽  
Author(s):  
J P H Shield ◽  
M Carradus ◽  
J E Stone ◽  
L P Hunt ◽  
J D Baum ◽  
...  
Keyword(s):  
Young Adults ◽  
Basement Membrane ◽  
Heparan Sulphate ◽  
Diabetic Control ◽  
Insulin Dependent Diabetes ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan ◽  
Normal Individuals ◽  
Patients With Diabetes ◽  
Insulin Dependent

Urinary excretion of heparan sulphate proteoglycan (HSPG), the main anionic component of the glomerular basement membrane (GBM), was estimated in 30 adolescents and young adults with insulin dependent diabetes (IDDM), 10 with microalbuminuria and 20 sex matched, diabetic controls of similar age without evidence of microalbuminuria. A further 10 non-diabetic control subjects were also examined. Both groups of patients with diabetes had significantly elevated excretion of HSPG when compared to normal individuals. There was no difference in HSPG excretion between diabetic subjects with and without microalbuminuria.

Perlecan basement membrane heparan sulphate proteoglycan

1998 ◽  
pp. 237-240
Author(s):  
Shirley Ayad ◽  
Ray Boot-Handford ◽  
Martin J. Humphries ◽  
Karl E. Kadler ◽  
Adrian Shuttleworth
Keyword(s):  
Basement Membrane ◽  
Heparan Sulphate ◽  
Heparan Sulphate Proteoglycan ◽  
Sulphate Proteoglycan
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