scholarly journals Basement membrane proteoglycan in various tissues: characterization using monoclonal antibodies to the Engelbreth-Holm-Swarm mouse tumor low density heparan sulfate proteoglycan.

1988 ◽  
Vol 106 (6) ◽  
pp. 2203-2210 ◽  
Author(s):  
M Kato ◽  
Y Koike ◽  
S Suzuki ◽  
K Kimata
Keyword(s):  
Monoclonal Antibodies ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Immunofluorescent Staining ◽  
Mouse Tumor ◽  
Low Density ◽  
Sulfate Proteoglycan ◽  
The Core ◽  
Core Proteins

The Engelbreth-Holm-Swarm mouse tumor has been found to produce at least two molecular species of heparan sulfate proteoglycan, a low density one (LD) and a high density one, which differ not only in core proteins but also in glycosaminoglycan structures (Kato, M., Y. Koike, Y. Ito, S. Suzuki, and K. Kimata. 1987. J. Biol. Chem. 262:7180-7188). With aim at investigating their distribution and possible functions in tissues, monoclonal antibodies were produced. Hybridomas obtained by fusion of NS-1 mouse myeloma cells with spleen cells from the rat immunized with a mixture of these proteoglycans were selected by their ability to react with the antigen. Two of them secreted monoclonal antibodies (IgG2a), designated HK-84 and HK-102, that recognize specifically the core protein moiety of LD. Immunofluorescent staining of various tissues (skeletal muscle, cardiac muscle, lung, brain, and kidney) with these monoclonal antibodies has demonstrated that the antigen molecules were present in all basement membranes of these tissues. SDS-PAGE of heparitinase-treated proteoglycan fractions prepared from these tissues and subsequent immunoblotting using these monoclonal antibodies have confirmed that the antigen molecule was LD, and further suggested that there was a tissue-specific variation in the core molecular size. Based on these results, we propose that LD may be an essential component in all basement membranes.

scholarly journals Origin and deposition of basement membrane heparan sulfate proteoglycan in the developing intestine.

1989 ◽  
Vol 109 (4) ◽  
pp. 1837-1848 ◽  
Author(s):  
P Simon-Assmann ◽  
F Bouziges ◽  
M Vigny ◽  
M Kedinger
Keyword(s):  
Basement Membrane ◽  
Heparan Sulfate ◽  
Developmental Stages ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Immunofluorescent Staining ◽  
Rat Tissues ◽  
Mouse Tumor ◽  
Sulfate Proteoglycan ◽  
Adult Mice

The deposition of intestinal heparan sulfate proteoglycan (HSPG) at the epithelial-mesenchymal interface and its cellular source have been studied by immunocytochemistry at various developmental stages and in rat/chick interspecies hybrid intestines. Polyclonal heparan sulfate antibodies were produced by immunizing rabbits with HSPG purified from the Engelbreth-Holm-Swarm mouse tumor; these antibodies stained rat intestinal basement membranes. A monoclonal antibody (mAb 4C1) produced against lens capsule of 11-d-old chick embryo reacted with embryonic or adult chick basement membranes, but did not stain that of rat tissues. Immunoprecipitation experiments indicated that mAb 4C1 recognized the chicken basement membrane HSPG. Immunofluorescent staining with these antibodies allowed us to demonstrate that distribution of HSPG at the epithelial-mesenchymal interface varied with the stages of intestinal development, suggesting that remodeling of this proteoglycan is essential for regulating cell behavior during morphogenesis. The immunofluorescence pattern obtained with the two species-specific HSPG antibodies in rat/chick epithelial/mesenchymal hybrid intestines developed as grafts (into the coelomic cavity of chick embryos or under the kidney capsule of adult mice) led to the conclusion that HSPG molecules located in the basement membrane of the developing intestine were produced exclusively by the epithelial cells. These data emphasize the notion already gained from previous studies, in which type IV collagen has been shown to be produced by mesenchymal cells (Simon-Assmann, P., F. Bouziges, C. Arnold, K. Haffen, and M. Kedinger. 1988. Development (Camb.). 102:339-347), that epithelial-mesenchymal interactions play an important role in the formation of a complete basement membrane.

Structure of low density heparan sulfate proteoglycan isolated from a mouse tumor basement membrane

1987 ◽  
Vol 197 (2) ◽  
pp. 297-313 ◽  
Author(s):  
Mats Paulsson ◽  
Peter D. Yurchenco ◽  
George C. Ruben ◽  
Jürgen Engel ◽  
Rupert Timpl
Keyword(s):  
Basement Membrane ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Mouse Tumor ◽  
Low Density ◽  
Sulfate Proteoglycan

scholarly journals Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes.

1989 ◽  
Vol 109 (6) ◽  
pp. 3199-3211 ◽  
Author(s):  
A Heremans ◽  
B van der Schueren ◽  
B de Cock ◽  
M Paulsson ◽  
J J Cassiman ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Monoclonal Antibodies ◽  
Epithelial Cell ◽  
Heparan Sulfate ◽  
Core Protein ◽  
Structural Features ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Lung Fibroblasts ◽  
Sulfate Proteoglycan

Cultured human lung fibroblasts produce a large, nonhydrophobic heparan sulfate proteoglycan that accumulates in the extracellular matrix of the monolayer (Heremans, A., J. J. Cassiman, H. Van den Berghe, and G. David. 1988. J. Biol. Chem. 263: 4731-4739). A panel of four monoclonal antibodies, specific for four distinct epitopes on the 400-kD core protein of this extracellular matrix heparan sulfate proteoglycan, detects similar proteoglycans in human epithelial cell cultures. Immunohistochemistry of human tissues with the monoclonal antibodies reveals that these proteoglycans are concentrated at cell-matrix interfaces. Immunogold labeling of ultracryosections of human skin indicates that the proteoglycan epitopes are nonhomogeneously distributed over the width of the basement membrane. Immunochemical investigations and amino acid sequence analysis indicate that the proteoglycan from the fibroblast matrix shares several structural features with the large, low density heparan sulfate proteoglycan isolated from the Engelbreth-Holm-Swarm sarcoma. Thus, both epithelial cell sheets and individual mesenchymal cells accumulate a large heparan sulfate proteoglycan(s) at the interface with the interstitial matrix, where the proteoglycan may adopt a specific topological orientation with respect to this matrix.

scholarly journals Monoclonal antibodies against the protein core and glycosaminoglycan side chain of glomerular basement membrane heparan sulfate proteoglycan: characterization and immunohistological application in human tissues.

1994 ◽  
Vol 42 (1) ◽  
pp. 89-102 ◽  
Author(s):  
J van den Born ◽  
L P van den Heuvel ◽  
M A Bakker ◽  
J H Veerkamp ◽  
K J Assmann ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Heparan Sulfate ◽  
Core Protein ◽  
Kidney Tissue ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Side Chain ◽  
Human Tissues ◽  
Sulfate Proteoglycan ◽  
Intense Staining

We raised monoclonal antibodies (MAb) against the core protein and the heparan sulfate (HS) side chain of heparan sulfate proteoglycan (HSPG) from glomerular basement membranes (GBM). Anti-HSPG-core MAb were obtained after immunization of mice with HSPG purified from human GBM and the anti-HS MAb after immunization of mice with HSPG from rat glomeruli, which crossreacted with human HS and GBM HSPG. The specificity of the MAb was demonstrated by ELISA studies, Western blotting, inhibition experiments, and indirect immunofluorescence (IF) on kidney cryostat sections pre-treated with glycosaminoglycan (GAG)-degrading enzymes. Indirect IF on normal human kidney tissue showed prominent GBM staining for both MAb, with variable staining of the other renal basement membranes (BMs). By indirect immunoelectron microscopy (IEM), most intense staining was observed at the endothelial side of the GBM for both MAb, although the staining patterns were not identical. Both MAb were used to localize HSPG in human tissues by indirect IF. They bound to antigens present in the BMs of most tissues examined, including those of epithelia and endothelia. Differences between both MAb were observed for BMs of muscle cells, since the anti-HSPG core protein MAb (JM-72) staining was negative, whereas the anti-HS MAb (JM-403) clearly stained these structures. Comparison of our staining patterns in human tissues with the distribution of other anti-BM HSPG antibodies suggests that there are at least two types of BM HSPG, which have common epitopes on the HS side chains recognized by JM-403.

Monoclonal antibodies to heparan sulfate proteoglycan: Development and application to the study of normal tissue and pathologic human kidney biopsies

1988 ◽  
Vol 18 (1) ◽  
pp. 9-25 ◽  
Author(s):  
Eva Kemeny ◽  
Howard M. Fillit ◽  
Shridhar Damle ◽  
Ram Mahabir ◽  
Nicholas A. Kefalides ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Heparan Sulfate ◽  
Normal Tissue ◽  
Human Kidney ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan

scholarly journals The core protein of the matrix-associated heparan sulfate proteoglycan binds to fibronectin.

1990 ◽  
Vol 265 (15) ◽  
pp. 8716-8724
Author(s):  
A Heremans ◽  
B De Cock ◽  
J J Cassiman ◽  
H Van den Berghe ◽  
G David
Keyword(s):  
Heparan Sulfate ◽  
Core Protein ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
The Core ◽  
The Matrix
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