Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions

Tumova, Sarka; Woods, Anne; Couchman, John R.

doi:10.1016/s1357-2725(99)00116-8

Cited by 339 publications

(278 citation statements)

References 141 publications

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“…The conserved carboxyl-terminal tetrapeptide sequence present in all syndecans binds certain PDZ domaincontaining proteins, such as syntenin (42) and calcium/ calmodulin-dependent serine protein kinase (43), which may function as membrane scaffold proteins that bind signaling and structural proteins to the plasma membrane. Syndecans have also been implicated in adhesion-dependent signaling (35). Previous immunohistochemical analysis of syndecan-1 and -4 in NHK culture revealed that syndecan-1 and -4 are both expressed by keratinocytes at cell-cell junctions and underneath the cell body suggesting involvement in adhesion (44,45).…”

Section: Discussionmentioning

confidence: 99%

Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Okamoto

Bachy

Odenthal³

et al. 2003

Journal of Biological Chemistry

101

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Basal keratinocytes of the epidermis adhere to their underlying basement membrane through a specific interaction with laminin-5, which is composed by the association of ␣3, ␤3, and ␥2 chains. Laminin-5 has the ability to induce either stable cell adhesion or migration depending on specific processing of different parts of the molecule. One event results in the cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5) of the ␣3 chain. In this study, we recombinantly expressed the human ␣3LG4/5 fragment in mammalian cells, and we show that this fragment induces adhesion of normal human keratinocytes and fibrosarcoma-derived HT1080 cells in a heparan-and chondroitin sulfate-dependent manner. Immunoprecipitation experiments with Na 2 35 SO 4 -labeled keratinocyte and HT1080 cell lysates as well as immunoblotting experiments revealed that the major proteoglycan receptor for the ␣3LG4/5 fragment is syndecan-1. Syndecan-4 from keratinocytes also bound to ␣3LG4/5. Furthermore we could show for the first time that unprocessed laminin-5 specifically binds syndecan-1, while processed laminin-5 does not. These results demonstrate that the LG4/5 modules within unprocessed laminin-5 permit its cell binding activity through heparan and chondroitin sulfate chains of syndecan-1 and reinforce previous data suggesting specific properties for the precursor molecule.Laminins (LNs) 1 are extracellular matrix glycoproteins composed of ␣, ␤, and ␥ chains assembled into a cross-shaped heterotrimer (␣␤␥) by forming a triple-stranded coiled-coil structure through their ␣-helical domains. At present, 15 heterotrimers termed LN-1 to LN-15 have been described with different subunit composition selected from five individual ␣ chains (␣1-␣5), three ␤ chains (␤1-␤3), and three ␥ chains (␥1-␥3) (1, 2). All LN ␣ chains comprise a large globular domain in their carboxylterminal region (G domain), which consists of five homologous globular subdomains of about 200 amino acids each (LG1-LG5). LN-5, with chain composition ␣3␤3␥2, is a component of basement membranes underlying specialized epithelia with secretory or protective function (3). In skin, LN-5 is synthesized by keratinocytes initially as a high molecular mass precursor protein of 460 kDa of which the ␣3 and ␥2 chains undergo specific processing to smaller forms after being secreted and deposited into the extracellular matrix (ECM) (4, 5). Processing of the ␣3 chain consists of cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5) (6, 7). An additional cleavage within the aminoterminal domain IIIa of the ␣3 chain occurs subsequently and may also be important for LN-5 function (8, 9). Processing of the ␥2 chain occurs at the amino terminus with loss of a 50-kDa domain (9 -11). Processed LN-5 is the major component of anchoring filaments in skin (12) where it mediates cell adhesion via interaction of the ␣3 carboxyl-terminal LG1-3 triplet domain with both ␣ 3 ␤ 1 and ␣ 6 ␤ 4 integrins (13-16). Several studies have suggested that processed LN-5 functions both in the nuclea...

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Section: Discussionmentioning

confidence: 99%

Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Okamoto

Bachy

Odenthal³

et al. 2003

Journal of Biological Chemistry

101

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“…The variable ectodomain, which is exposed to the extracellular environment, contains 3-5 HS chains and is attached to the cell membrane via a hydrophobic transmembrane segment (5,6). In addition, there is an intracellular domain containing peptide sequences that serve as substrates for cellular kinases, enabling syndecans to act as signaling molecules (7,8).…”

mentioning

confidence: 99%

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Patterson

Gardner

Shaw

et al. 2005

Arthritis & Rheumatism

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“…In recent years, it has become widely accepted that especially the sulfation pattern of HS domains regulates specific interactions with HS-binding proteins (Bernfield et al, 1999;Tumova et al, 2000). Binding of fibroblast growth factor-2 requires 2-O sulfation of iduronic acid residues, whereas additional 6-O sulfation of the glucosamine residue is required for the binding of fibroblast growth factor-1 (Kreuger et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…Each HS disaccharide unit, consisting of a glucosamine and an uronic acid residue, can be modified by Ndeacetylation, N-sulfation, 2-O-, 3-O-, and/ or 6-O-sulfation and C-5 epimerization. The concert of these modifications potentially makes HS a very informationdense biopolymer, to which several proteins may bind in a monosaccharide sequence-specific way (Salmivirta et al, 1996;Bernfield et al, 1999;Tumova et al, 2000;Turnbull et al, 2001;Gallagher, 2001). In developmental processes, however, the functions of HS have remained mostly underappreciated until recently (Perrimon and Bernfield, 2000).…”

Section: Introductionmentioning

confidence: 99%

Spatiotemporal distribution of heparan sulfate epitopes during myogenesis and synaptogenesis: A study in developing mouse intercostal muscle

Jenniskens¹,

Hafmans²,

Veerkamp³

et al. 2002

Developmental Dynamics

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Formation of a basal lamina (BL) ensheathing developing skeletal muscle cells is one of the earliest events in mammalian skeletal muscle myogenesis. BL-resident heparan sulfate proteoglycans have been implicated in various processes during myogenesis, including synaptic differentiation. However, attention has focused on the proteoglycan protein core, ignoring the glycosaminoglycan moiety mainly because of a lack of appropriate tools. Recently, we selected a panel of anti-heparan sulfate antibodies applied here to study the spatiotemporal distribution of specific heparan sulfate (HS) epitopes during myogenesis. In mouse intercostal muscle at embryonic day (E14), formation of acetylcholine receptor clusters at synaptic sites coincides with HS deposition. Although some HS epitopes show a general appearance throughout the BL, one epitope preferably clusters at synaptic sites but does so only from E16 onward. During elongation and maturation of primary myotubes, a process preceding secondary myotube development, significant changes in the HS epitope constitution of both synaptic and extrasynaptic BL were observed. As a whole, the data presented here strengthen previous observations on developmental regulation by BL components, and add to the putative roles of specific HS epitopes in myogenesis and synaptogenesis.

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Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions

Cited by 339 publications

References 141 publications

Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Normal Human Keratinocytes Bind to the α3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1

Induction of a CXCL8 binding site on endothelial syndecan‐3 in rheumatoid synovium

Spatiotemporal distribution of heparan sulfate epitopes during myogenesis and synaptogenesis: A study in developing mouse intercostal muscle

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