Biology and pathology of the pericellular heparan sulphate proteoglycans

1991 ◽  
Vol 19 (4) ◽  
pp. 816-820 ◽  
Author(s):  
Guido David
Keyword(s):  
Heparan Sulphate ◽  
Heparan Sulphate Proteoglycans

scholarly journals What Are the Potential Roles of Nuclear Perlecan and Other Heparan Sulphate Proteoglycans in the Normal and Malignant Phenotype

2021 ◽  
Vol 22 (9) ◽  
pp. 4415
Author(s):  
Anthony J. Hayes ◽  
James Melrose
Keyword(s):  
Gene Expression ◽  
Nuclear Envelope ◽  
Annulus Fibrosus ◽  
Heparan Sulphate ◽  
Cell Types ◽  
Malignant Cell ◽  
Cytoskeletal Proteins ◽  
Nucleus Pulposus Cells ◽  
Malignant Phenotype ◽  
Heparan Sulphate Proteoglycans

The recent discovery of nuclear and perinuclear perlecan in annulus fibrosus and nucleus pulposus cells and its known matrix stabilizing properties in tissues introduces the possibility that perlecan may also have intracellular stabilizing or regulatory roles through interactions with nuclear envelope or cytoskeletal proteins or roles in nucleosomal-chromatin organization that may regulate transcriptional factors and modulate gene expression. The nucleus is a mechano-sensor organelle, and sophisticated dynamic mechanoresponsive cytoskeletal and nuclear envelope components support and protect the nucleus, allowing it to perceive and respond to mechano-stimulation. This review speculates on the potential roles of perlecan in the nucleus based on what is already known about nuclear heparan sulphate proteoglycans. Perlecan is frequently found in the nuclei of tumour cells; however, its specific role in these diseased tissues is largely unknown. The aim of this review is to highlight probable roles for this intriguing interactive regulatory proteoglycan in the nucleus of normal and malignant cell types.

Heparan sulphate proteoglycans in Alzheimer's disease and amyloid‐related disorders

2003 ◽  
Vol 2 (8) ◽  
pp. 482-492 ◽  
Author(s):  
Jack van Horssen ◽  
Pieter Wesseling ◽  
Lambert PWJ van den Heuvel ◽  
Robert MW de Waal ◽  
Marcel M Verbeek
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Heparan Sulphate ◽  
Heparan Sulphate Proteoglycans

scholarly journals Recent Insights into Cell Surface Heparan Sulphate Proteoglycans and Cancer

F1000Research ◽  
2016 ◽  
Vol 5 ◽  
pp. 1541 ◽  
Author(s):  
John R Couchman ◽  
Hinke Multhaupt ◽  
Ralph D. Sanderson
Keyword(s):  
Cell Surface ◽  
Core Protein ◽  
Tumour Progression ◽  
Heparan Sulphate ◽  
Cell Behaviour ◽  
Surface Receptors ◽  
Protein Ligands ◽  
Proliferation And Differentiation ◽  
Cell Processes ◽  
Heparan Sulphate Proteoglycans

A small group of cell surface receptors are proteoglycans, possessing a core protein with one or more covalently attached glycosaminoglycan chains. They are virtually ubiquitous and their chains are major sites at which protein ligands of many types interact. These proteoglycans can signal and regulate important cell processes, such as adhesion, migration, proliferation, and differentiation. Since many protein ligands, such as growth factors, morphogens, and cytokines, are also implicated in tumour progression, it is increasingly apparent that cell surface proteoglycans impact tumour cell behaviour. Here, we review some recent advances, emphasising that many tumour-related functions of proteoglycans are revealed only after their modification in processes subsequent to synthesis and export to the cell surface. These include enzymes that modify heparan sulphate structure, recycling of whole or fragmented proteoglycans into exosomes that can be paracrine effectors or biomarkers, and lateral interactions between some proteoglycans and calcium channels that impact the actin cytoskeleton.

Ultrastructural localization of keratinocyte surface associated heparan sulphate proteoglycans in human epidermis

1987 ◽  
Vol 87 (3) ◽  
pp. 243-250 ◽  
Author(s):  
R. H. Tammi ◽  
A. M. H. Hyyryl�inen ◽  
H. I. Maibach ◽  
M. I. Tammi
Keyword(s):  
Heparan Sulphate ◽  
Ultrastructural Localization ◽  
Human Epidermis ◽  
Heparan Sulphate Proteoglycans

118. CHARACTERISATION OF HEPARAN SULPHATE PROTEOGLYCANS IN THE MATURING CUMULUS OOCYTE COMPLEX

2009 ◽  
Vol 21 (9) ◽  
pp. 37
Author(s):  
L. N. Watson ◽  
M. Sasseville ◽  
R. B. Gilchrist ◽  
D. L. Russell
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Cell Surface ◽  
Transforming Growth Factor ◽  
Heparan Sulphate ◽  
Cumulus Cells ◽  
Receptor Interaction ◽  
Heparan Sulphate Proteoglycans ◽  
Tgfβ Superfamily

Many growth factors including members of the transforming growth factor beta (TGFβ) superfamily and epidermal growth factor (Egf)-like ligands signal via interactions with heparan sulphate proteoglycans (HSPGs). Cell surface HSPGs can act by sequestering ligands at their site of action, by presenting a ligand to its signalling receptor, or by preventing ligand-receptor interaction. The oocyte secreted factors (OSF) growth differentiation factor 9 and bone morphogenetic protein 15 are members of the TGFβ superfamily that act selectively on cumulus cells. Conversely Egf-like ligands are secreted by mural granulosa cells and transmit LH-induced signals to cumulus cells. We investigated the possibility that HSPGs contribute to the spatially restricted responses these signals exert on cumulus cells. Syndecan-1 and Glypican-1 are cell surface HSPGs that are involved in numerous biological processes, including growth factor regulation, cell proliferation and differentiation. Microarray analysis showed Syndecan-1 and Glypican-1 mRNA expression induced 6-fold (P=10-9) and 3-fold (P=10-7) respectively in Egf+FSH stimulated cumulus oocyte complexes (COCs). Furthermore, Syndecan-1 and Glypican-1 mRNA were induced 27- and 16-fold respectively in COCs after hCG treatment of mice. Syndecan-1 and Glypican-1 protein was localised specifically to the COC through immunohistochemical analysis. In Vitro Maturation (IVM) of oocytes is a valuable alternative to gonadotropin mediated superovulation, but IVM COCs are less competent than those matured in vivo. Several components of the COC have been shown to be altered in IVM, including the chondroitin sulphate proteoglycan Versican. COCs from mice that underwent IVM in the presence of Egf+FSH and cilostamide for 16 hours had >16 fold reduced mRNA for Syndecan-1 when compared with In Vivo matured COCs. The lack of Syndecan-1 in IVM COCs could reduce signalling capacity of growth factors including OSFs. This may contribute to the reduced capacity of IVM oocytes to fertilise and produce a healthy embryo, and ultimately, a healthy offspring.

scholarly journals Heparan Sulfate Proteoglycans Regulate Responses to Oocyte Paracrine Signals in Ovarian Follicle Morphogenesis

Endocrinology ◽  
2012 ◽  
Vol 153 (9) ◽  
pp. 4544-4555 ◽  
Author(s):  
Laura N. Watson ◽  
David G. Mottershead ◽  
Kylie R. Dunning ◽  
Rebecca L. Robker ◽  
Robert B. Gilchrist ◽  
...  
Keyword(s):  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Cell Function ◽  
Ovarian Follicle ◽  
Heparan Sulphate ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Distinct Cell ◽  
Heparan Sulphate Proteoglycans

In the ovarian follicle, oocyte-secreted factors induce cumulus-specific genes and repress mural granulosa cell specific genes to establish these functionally distinct cell lineages. The mechanism establishing this precise morphogenic pattern of oocyte signaling within the follicle is unknown. The present study investigated a role for heparan sulphate proteoglycans (HSPG) as coreceptors mediating oocyte secreted factor signaling. In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated. Heparin also blocked phosphorylation of SMAD2. Exogenous growth differentiation factor (GDF)-9 reversed these heparin effects; furthermore, GDF9 strongly bound to heparin sepharose. These observations indicate that heparin binds endogenous GDF9 and disrupts interaction with heparan sulphate proteoglycan coreceptor(s), important for GDF9 signaling. The expression of candidate HSPG coreceptors, Syndecan 1–4, Glypican 1–6, and Betaglycan, was examined. An ovulatory dose of human chorionic gonadotropin down-regulated Betaglycan in cumulus cells, and this regulation required GDF9 activity; conversely, Betaglycan was significantly increased in luteinizing mural granulosa cells. Human chorionic gonadotropin caused very strong induction of Syndecan 1 and Syndecan 4 in mural granulosa as well as cumulus cells. Glypican 1 was selectively induced in cumulus cells, and this expression appeared dependent on GDF9 action. These data suggest that HSPG play an essential role in GDF9 signaling and are involved in the patterning of oocyte signaling and cumulus cell function in the periovulatory follicle.

scholarly journals Gangliosides of myelosupportive stroma cells are transferred to myeloid progenitors and are required for their survival and proliferation

2006 ◽  
Vol 394 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Ana L. Ziulkoski ◽  
Cláudia M. B. Andrade ◽  
Pilar M. Crespo ◽  
Elisa Sisti ◽  
Vera M. T. Trindade ◽  
...  
Keyword(s):  
Growth Factors ◽  
Heparan Sulphate ◽  
Myeloid Cells ◽  
Target Cells ◽  
Reporter System ◽  
Gm Csf ◽  
Heparan Sulphate Proteoglycans ◽  
Α Chain ◽  
Major Ganglioside ◽  
Myeloid Progenitors

In previous studies, we have shown that the myelopoiesis dependent upon myelosupportive stroma required production of growth factors and heparan-sulphate proteoglycans, as well as generation of a negatively charged sialidase-sensitive intercellular environment between the stroma and the myeloid progenitors. In the present study, we have investigated the production, distribution and role of gangliosides in an experimental model of in vitro myelopoiesis dependent upon AFT-024 murine liver-derived stroma. We used the FDC-P1 cell line, which is dependent upon GM-CSF (granulocyte/macrophage colony-stimulating factor) for both survival and proliferation, as a reporter system to monitor bioavailability and local activity of GM-CSF. GM3 was the major ganglioside produced by stroma, but not by myeloid cells, and it was required for optimal stroma myelosupportive function. It was released into the supernatant and selectively incorporated into the myeloid progenitor cells, where it segregated into rafts in which it co-localized with the GM-CSF-receptor α chain. This ganglioside was also metabolized further by myeloid cells into gangliosides of the a and b series, similar to endogenous GM3. In these cells, GM1 was the major ganglioside and it was segregated at the interface by stroma and myeloid cells, partially co-localizing with the GM-CSF-receptor α chain. We conclude that myelosupportive stroma cells produce and secrete the required growth factors, the cofactors such as heparan sulphate proteoglycans, and also supply gangliosides that are transferred from stroma to target cells, generating on the latter ones specific membrane domains with molecular complexes that include growth factor receptors.

MHC proteins and heparan sulphate proteoglycans regulate murine cytomegalovirus infection

1995 ◽  
Vol 73 (4) ◽  
pp. 308-315 ◽  
Author(s):  
PATRICIA PRICE ◽  
RICHARD JN ALLCOCK ◽  
DEIRDRE R COOMBE ◽  
GEOEFREY R SHELLAM ◽  
JAMES McCLUSKEY
Keyword(s):  
Cytomegalovirus Infection ◽  
Heparan Sulphate ◽  
Murine Cytomegalovirus ◽  
Heparan Sulphate Proteoglycans
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