Time-dependent pericellular expression of collagen type IV, laminin, and heparan sulfate proteoglycan in myofibroblasts

1992 ◽  
Vol 105 (3) ◽  
pp. 169-172 ◽  
Author(s):  
P. Betz ◽  
A. Nerlich ◽  
J. Wilske ◽  
J. Tübel ◽  
I. Wiest ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Collagen Type ◽  
Heparan Sulfate Proteoglycan ◽  
Time Dependent ◽  
Collagen Type Iv ◽  
Sulfate Proteoglycan ◽  
Type Iv

scholarly journals Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc

1993 ◽  
Vol 268 (15) ◽  
pp. 10881-10887
Author(s):  
D. Reinhardt ◽  
K. Mann ◽  
R. Nischt ◽  
J.W. Fox ◽  
M.L. Chu ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Binding Sites ◽  
Collagen Type ◽  
Heparan Sulfate Proteoglycan ◽  
Collagen Type Iv ◽  
Sulfate Proteoglycan ◽  
Type Iv

scholarly journals Expression of the Heparan Sulfate Proteoglycan, Perlecan, during Mouse Embryogenesis and Perlecan Chondrogenic Activity In Vitro

1999 ◽  
Vol 145 (5) ◽  
pp. 1103-1115 ◽  
Author(s):  
M.M. French ◽  
S.E. Smith ◽  
K. Akanbi ◽  
T. Sanford ◽  
J. Hecht ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Collagen Type ◽  
Heparan Sulfate Proteoglycan ◽  
Surrounding Tissue ◽  
Collagen Type Iv ◽  
Type Ii ◽  
Sulfate Proteoglycan ◽  
Collagen Type Ii ◽  
Murine Embryonic Fibroblast

Expression of the basement membrane heparan sulfate proteoglycan (HSPG), perlecan (Pln), mRNA, and protein has been examined during murine development. Both Pln mRNA and protein are highly expressed in cartilaginous regions of developing mouse embryos, but not in areas of membranous bone formation. Initially detected at low levels in precartilaginous areas of d 12.5 embryos, Pln protein accumulates in these regions through d 15.5 at which time high levels are detected in the cartilage primordia. Laminin and collagen type IV, other basal lamina proteins commonly found colocalized with Pln, are absent from the cartilage primordia. Accumulation of Pln mRNA, detected by in situ hybridization, was increased in d 14.5 embryos. Cartilage primordia expression decreased to levels similar to that of the surrounding tissue at d 15.5. Pln accumulation in developing cartilage is preceded by that of collagen type II. To gain insight into Pln function in chondrogenesis, an assay was developed to assess the potential inductive activity of Pln using multipotential 10T1/2 murine embryonic fibroblast cells. Culture on Pln, but not on a variety of other matrices, stimulated extensive formation of dense nodules reminiscent of embryonic cartilaginous condensations. These nodules stained intensely with Alcian blue and collagen type II antibodies. mRNA encoding chondrocyte markers including collagen type II, aggrecan, and Pln was elevated in 10T1/2 cells cultured on Pln. Human chondrocytes that otherwise rapidly dedifferentiate during in vitro culture also formed nodules and expressed high levels of chondrocytic marker proteins when cultured on Pln. Collectively, these studies demonstrate that Pln is not only a marker of chondrogenesis, but also strongly potentiates chondrogenic differentiation in vitro.

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.

Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen

1986 ◽  
Vol 189 (1) ◽  
pp. 205-216 ◽  
Author(s):  
G.W. Laurie ◽  
J.T. Bing ◽  
H.K. Kleinman ◽  
J.R. Hassell ◽  
M. Aumailley ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Heparan Sulfate ◽  
Binding Sites ◽  
Type Iv Collagen ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Type Iv ◽  
Membrane Type

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 Basement membrane-like matrix of teratocarcinoma-derived endodermal cells: presence of laminin and heparan sulfate in the matrix at points of attachment to cells.

1983 ◽  
Vol 31 (1) ◽  
pp. 35-45 ◽  
Author(s):  
I Leivo
Keyword(s):  
Cell Membrane ◽  
Basement Membrane ◽  
Heparan Sulfate ◽  
Type Iv Collagen ◽  
Heparan Sulfate Proteoglycan ◽  
Ruthenium Red ◽  
Basement Membranes ◽  
Sulfate Proteoglycan ◽  
Type Iv ◽  
The Matrix

Teratocarcinoma-derived endodermal PYS-2 cells are known to synthesize an extracellular matrix containing the basement membrane molecules laminin, type IV collagen, and heparan sulfate proteoglycan as major constituents (I. Leivo, K. Alitalo, L. Risteli, A. Vaheri, R. Timpl, J. Wartiovaara, Exp Cell Res 137:15-23, 1982). Immunoferritin techniques with specific antibodies were used in the present study to define the ultrastructural localization of the above constituents in the fibrillar network. Laminin was detected in matrix network adjacent to the basal cell membrane and in protruding matrix fibrils that connect the matrix to the cell membrane. Ruthenium red-stainable heparinase-sensitive 10- to 20-nm particles were often present at the junction of the attachment fibrils and the matrix network, or along the attachment fibrils. A corresponding distribution of ferritin label was observed for basement membrane heparan sulfate proteoglycan. Type IV collagen was found in the matrix network but not in the attachment fibrils. The results suggest that the PYS-2 cells are connected to their pericellular matrix by fibrils containing laminin associated with heparan sulfate-containing particles. These results may also have relevance for the attachment of epithelial cells to basement membranes.

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