scholarly journals Heparan Sulfate Proteoglycans and Viral Attachment: True Receptors or Adaptation Bias?

Viruses ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 596 ◽  
Author(s):  
Cagno ◽  
Tseligka ◽  
Jones ◽  
Tapparel
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Blood Coagulation ◽  
Biological Activities ◽  
Extracellular Matrix Proteins ◽  
Heparan Sulfate Proteoglycans ◽  
Matrix Proteins ◽  
Cell Homeostasis ◽  
Viral Attachment

Heparan sulfate proteoglycans (HSPG) are composed of unbranched, negatively charged heparan sulfate (HS) polysaccharides attached to a variety of cell surface or extracellular matrix proteins. Widely expressed, they mediate many biological activities, including angiogenesis, blood coagulation, developmental processes, and cell homeostasis. HSPG are highly sulfated and broadly used by a range of pathogens, especially viruses, to attach to the cell surface.

scholarly journals The heparan sulfate and its diverse biological activities

2014 ◽  
Vol 27 (4) ◽  
pp. 209-212
Author(s):  
Iwona Kaznowska-Bystryk
Keyword(s):  
Extracellular Matrix ◽  
Growth Factors ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Biological Function ◽  
Molecular Level ◽  
Biological Activities ◽  
Therapeutic Strategies ◽  
Detailed Knowledge ◽  
And Storage

Abstract Heparan sulfate (HS) is one of the most common glycosaminoglycan (GAG) in mammals. It is composed of relatively simple disaccharide subunits, which, by further modification, such as sulfation and epimerization, potentially offer huge diversity in biological function. GAG chains of different length, different patterns of sulfation, and other modifications, depending on location, generate unique forms. Due to polyanion charges, these compounds can interact with other molecules, such as proteins, cytokines, chemokines and growth factors, both on the cell surface and inside the extracellular matrix. These interactions serve protective and storage functions for the compounds, safeguarding them from proteolysis. In this way, HS is involved in numerous signaling pathways, and in growth and differentiation processes. Disrupted interactions between the HS and growth factors, cytokines or other proteins have been observed in various disorders, among these Alzheimer’s disease, epilepsy, atherosclerosis, diabetes, and cancer processes. Detailed knowledge of these relationships at the molecular level will allow researchers to understand the mechanisms underlying these disorders and enable the development of effective therapeutic strategies.

scholarly journals Relationship of heparan sulfate proteoglycans to the cytoskeleton and extracellular matrix of cultured fibroblasts.

1984 ◽  
Vol 99 (5) ◽  
pp. 1743-1753 ◽  
Author(s):  
A Woods ◽  
M Höök ◽  
L Kjellén ◽  
C G Smith ◽  
D A Rees
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Focal Adhesions ◽  
Dermal Fibroblasts ◽  
Heparan Sulfate Proteoglycans ◽  
Immunofluorescent Staining ◽  
Rat Embryo ◽  
Double Labeling ◽  
Cultured Fibroblasts

The distribution of heparan sulfate proteoglycans (HSPG) on cultured fibroblasts was monitored using an antiserum raised against cell surface HSPG from rat liver. After seeding, HSPG was detected by immunofluorescence first on cell surfaces and later in fibrillar deposits of an extracellular matrix. Cell surface HSPG aligned with microfilament bundles of rat embryo fibroblasts seen by phase-contrast microscopy but was diffuse on transformed rat dermal fibroblasts (16C cells) which lack obvious stress fibers. Focal adhesions isolated from either cell type and monitored by interference reflection microscopy showed a concentration of HSPG labeling with respect to the rest of the membrane. Increased labeling in these areas was also seen for fibronectin (FN) by using an antiserum that detects both plasma and cell-derived FN. Double immunofluorescent staining of fully adherent rat embryo fibroblast cells showed some co-distribution of HSPG and FN, and this was confirmed by immunoelectron microscopy, which detected HSPG at localized areas of dorsal and ventral cell membranes, overlapping cell margins, and in the extracellular matrix. During cell shape changes on rounding and spreading, HSPG and FN may not co-distribute. Double labeling for actin and either HSPG or FN showed a closer correlation of actin with HSPG than with FN. The studies are consistent with HSPG being closely involved in a transmembrane cytoskeletal-matrix interaction; the possibility that HSPG coordinates the deposition of FN and other matrix components with cytoskeletal organization is discussed.

scholarly journals Candida albicans and Candida glabrata triosephosphate isomerase – a moonlighting protein that can be exposed on the candidal cell surface and bind to human extracellular matrix proteins

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Dorota Satala ◽  
Grzegorz Satala ◽  
Marcin Zawrotniak ◽  
Andrzej Kozik
Keyword(s):  
Extracellular Matrix ◽  
Cell Wall ◽  
Cell Surface ◽  
Triosephosphate Isomerase ◽  
Dissociation Constants ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Host Proteins ◽  
Interaction Sites ◽  
Catalytic Active Site

Abstract Background Triosephosphate isomerase (Tpi1) is a glycolytic enzyme that has recently been reported also to be an atypical proteinaceous component of the Candida yeast cell wall. Similar to other known candidal “moonlighting proteins”, surface-exposed Tpi1 is likely to contribute to fungal adhesion during the colonization and infection of a human host. The aim of our present study was to directly prove the presence of Tpi1 on C. albicans and C. glabrata cells under various growth conditions and characterize the interactions of native Tpi1, isolated and purified from the candidal cell wall, with human extracellular matrix proteins. Results Surface plasmon resonance measurements were used to determine the dissociation constants for the complexes of Tpi1 with host proteins and these values were found to fall within a relatively narrow range of 10− 8-10− 7 M. Using a chemical cross-linking method, two motifs of the Tpi1 molecule (aa 4–17 and aa 224–247) were identified to be directly involved in the interaction with vitronectin. A proposed structural model for Tpi1 confirmed that these interaction sites were at a considerable distance from the catalytic active site. Synthetic peptides with these sequences significantly inhibited Tpi1 binding to several extracellular matrix proteins suggesting that a common region on the surface of Tpi1 molecule is involved in the interactions with the host proteins. Conclusions The current study provided structural insights into the interactions of human extracellular matrix proteins with Tpi1 that can occur at the cell surface of Candida yeasts and contribute to the host infection by these fungal pathogens.

Extracellular matrix proteins control the growth of cerebellar medulloblastoma cells

2004 ◽  
Vol 216 (03) ◽  
Author(s):  
U Schüller ◽  
W Hartmann ◽  
A Koch ◽  
K Schilling ◽  
OD Wiestler ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Cerebellar Medulloblastoma
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