Immunohistochemical Localization of Chondroitin Sulfate, Chondroitin Sulfate Proteoglycan, Heparan Sulfate Proteoglycan, Entactin, and Laminin in Basement Membranes of Postnatal Developing and Adult Rat Lungs

1993 ◽  
Vol 8 (3) ◽  
pp. 245-251 ◽  
Author(s):  
Philip L. Sannes ◽  
Kimberly K. Burch ◽  
Jody Khosla ◽  
Kevin J. McCarthy ◽  
John R. Couchman
Keyword(s):  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Immunohistochemical Localization ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Chondroitin Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Adult Rat ◽  
Rat Lungs

scholarly journals Codistribution of heparan sulfate proteoglycan, laminin, and fibronectin in the extracellular matrix of normal rat kidney cells and their coordinate absence in transformed cells.

1982 ◽  
Vol 94 (1) ◽  
pp. 28-35 ◽  
Author(s):  
E G Hayman ◽  
A Oldberg ◽  
G R Martin ◽  
E Ruoslahti
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Rat Kidney ◽  
Heparan Sulfate Proteoglycan ◽  
Chondroitin Sulfate Proteoglycan ◽  
Transformed Cells ◽  
Kidney Cells ◽  
Sulfate Proteoglycan ◽  
Normal Rat

We used antibodies raised against both a heparan sulfate proteoglycan purified from a mouse sarcoma and a chondroitin sulfate proteoglycan purified from a rat yolk sac carcinoma to study the appearance and distribution of proteoglycans in cultured cells. Normal rat kidney cells displayed a fibrillar network of immunoreactive material at the cell surface when stained with antibodies to heparan sulfate proteoglycan, while virally transformed rat kidney cells lacked such a surface network. Antibodies to chondroitin sulfate proteoglycan revealed a punctate pattern on the surface of both cell types. The distribution of these two proteoglycans was compared to that of fibronectin by double-labeling immunofluorescent staining. The heparan sulfate proteoglycan was found to codistribute with fibronectin, and fibronectin and laminin gave coincidental stainings. The distribution of chondroitin sulfate proteoglycan was not coincidental with that of fibronectin. Distinct fibers containing fibronectin but lacking chondroitin sulfate proteoglycan were observed. When the transformed cells were cultured in the presence of sodium butyrate, their morphology changed, and fibronectin, laminin, and heparan sulfate proteoglycan appeared at the cell surface in a pattern resembling that of normal cells. These results suggest that fibronectin, laminin, and heparan sulfate proteoglycan may be complexed at the cell surface. The proteoglycan may play a central role in assembly of such complexes since heparan sulfate has been shown to interact with both fibronectin and laminin.

The Association between Genes Polymorphisms of Heparan Sulfate Proteoglycan 2 (HSPG2) and Chondroitin Sulfate Proteoglycan 2 (CSPG2) and Intracranial Aneurysm Susceptibility: A Meta-Analysis

2020 ◽  
Author(s):  
Huahui LIU ◽  
Wen HUANG
Keyword(s):  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Harmful Effect ◽  
Heparan Sulfate Proteoglycan ◽  
Minor Allele ◽  
Chondroitin Sulfate Proteoglycan ◽  
Cochrane Library ◽  
Sulfate Proteoglycan ◽  
Increased Risk ◽  
Significant Difference

Background: We aimed to investigate whether the polymorphisms of gene heparan sulfate proteoglycan 2 (HSPG2) and chondroitin sulfate proteoglycan 2 (CSPG2) are associated with increased risk of intracranial aneurysms (IAs) susceptibility. Methods: The Cochrane Library, Medline, PubMed, and Embase databases were carefully searched for potential researches before Mar 30, 2018. The title, abstract, and full text were assessed to determine whether the paper was suitable for inclusion. The pooled odds ratios (ORs) with 95% confidence intervals (CIs) were presented to assess the associations between CSPG2 and HSPG2 polymorphisms and IAs susceptibility. Results: We enrolled 7 papers, 4 matched single nucleotide polymorphisms (SNPs) of CSPG2 (rs173686, rs251124) or HSPG2 (rs173686, rs251124), and a total of 8651 participations (3674 with IAs and 4977 for control). For the rs251124 polymorphism of CSPG2, the quantitative synthesis from 5 studies showed significant difference in the gene allele comparison of T vs. C (OR, 1.129; 95% CI, 1.029, 1.238; P=0.01). Similar results were found for rs3767137 of HSPG2 (A vs. G, OR, 0.842, 95% CI=0.759-0.935, P=0.001). However, for the rs173686 polymorphism of CSPG2 and rs7556412 polymorphism of HSPG2, no significant difference was found (P=0.259 and P=0.474, respectively) Conclusion: The SNPs rs251124 of CSPG2 and rs3767137 of HSPG2 had statistically significant associations with IAs susceptibility. The minor allele T of rs251124 demonstrated a harmful effect but the minor allele A of rs3767137 demonstrated a protective role with regard to the risk of IAs. However, no such associations were found in the SNPs rs173686 of CSPG2 and rs7556412 of HSPG2.

scholarly journals A monoclonal antibody that blocks the activity of a neurite regeneration-promoting factor: studies on the binding site and its localization in vivo.

1986 ◽  
Vol 103 (4) ◽  
pp. 1383-1398 ◽  
Author(s):  
A Y Chiu ◽  
W D Matthew ◽  
P H Patterson
Keyword(s):  
Monoclonal Antibody ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Rat Tissues ◽  
Sulfate Proteoglycan ◽  
Adult Rat ◽  
The Central Nervous System ◽  
Cold Spring

Work from several laboratories has identified a proteoglycan complex secreted by a variety of non-neuronal cells that can promote neurite regeneration when applied to the surface of culture dishes. Using a novel immunization protocol, a monoclonal antibody (INO) was produced that blocks the activity of this outgrowth-promoting factor (Matthew, W. D., and P. H. Patterson, 1983, Cold Spring Harbor Symp. Quant. Biol. 48:625-631). We have used the antibody to analyze the components of the active site and to localize the complex in vivo. INO binding is lost when the complex is dissociated; if its components are selectively reassociated, INO binds only to a complex containing two different molecular weight species. These are likely to be laminin and heparan sulfate proteoglycan, respectively. On frozen sections of adult rat tissues, INO binding is present on the surfaces of glial cells of the peripheral, but not the central, nervous system. INO also binds to the basement membrane surrounding cardiac and skeletal muscle cells, and binding to the latter greatly increases after denervation. In the adrenal gland and kidney, INO selectively reacts with areas rich in basement membranes, staining a subset of structures that are immunoreactive for both laminin and heparan sulfate proteoglycan. In general, the outgrowth-blocking antibody binds to areas known to promote axonal regeneration and is absent from areas known to lack this ability. This suggests that this complex, which is active in culture, may be the physiological substrate supporting nerve regeneration in vivo.

Immunohistochemical localization of heparan sulfate proteoglycan in human gastrointestinal tract

2001 ◽  
Vol 115 (5) ◽  
pp. 373-380 ◽  
Author(s):  
Mariko Oshiro ◽  
Kenzo Ono ◽  
Yasuhiko Suzuki ◽  
Hiroyoshi Ota ◽  
Tsutomu Katsuyama ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Heparan Sulfate ◽  
Immunohistochemical Localization ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Human Gastrointestinal Tract

Selective distributions of proteoglycans and their ligands in pericellular matrix of cultured fibroblasts. Implications for their roles in cell-substratum adhesion

1993 ◽  
Vol 106 (1) ◽  
pp. 55-65 ◽  
Author(s):  
M. Yamagata ◽  
S. Saga ◽  
M. Kato ◽  
M. Bernfield ◽  
K. Kimata
Keyword(s):  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
The Other ◽  
Stress Fibers ◽  
Chondroitin Sulfate Proteoglycan ◽  
Pericellular Matrix ◽  
Sulfate Proteoglycan ◽  
Cultured Fibroblasts ◽  
Focal Contacts ◽  
The Difference

We showed previously that a large chondroitin sulfate proteoglycan, PG-M (also known as versican), inhibits cell-substratum adhesion, while basement membrane heparan sulfate proteoglycan (recently named perlecan) does not (Yamagata et al. (1989) J. Biol. Chem. 264, 8012–8018). To extend our understanding of the adhesive function of these proteoglycans, we examined the pericellular localization of the proteoglycans and their ligands and also that of some matrix receptors and cytoskeletal molecules in various fibroblast culture systems. PG-M was abundant in the subcellular space of fibroblasts, but was excluded selectively from focal contacts where vinculin, integrins and fibronectin were localized. Hyaluronan, CD44 and tenascin were distributed similarly as PG-M. In contrast, perlecan was associated with fibronectin and was included in focal contacts. Syndecan-1, a membrane heparan sulfate/chondroitin sulfate proteoglycan, was associated with fibronectin at the cell surface, partly at focal contacts and in association with stress fibers. Thus, complexes of PG-M with hyaluronan, tenascin and CD44, are not involved in focal contacts. On the other hand, perlecan and syndecan-1 together with fibronectin may participate in focal contacts. The difference in localization between these proteoglycans may be related to their glycosaminoglycan content and to their distinctive roles in cell-substratum adhesion.

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