Domain Structure of Chondroitin Sulfate E Octasaccharides Binding to Type V Collagen

Takagaki, Keiichi; Munakata, Hidekazu; Kakizaki, Ikuko; Iwafune, Mito; Itabashi, Takeshi; Endo, Masahiko

doi:10.1074/jbc.m106479200

Cited by 59 publications

(34 citation statements)

References 50 publications

(51 reference statements)

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“…CD44 binding to type IV collagen and ␣1(IV)1263-1277 is dependent upon CS (21, 44). CS interaction with collagen requires a minimum oligosaccharide chain length and distinct sulfation pattern (76). Conversely, CS interferes with CD44 binding to HA (34).…”

Section: Discussionmentioning

confidence: 99%

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

Baronas-Lowell

Lauer‐Fields

Borgia³

et al. 2004

Journal of Biological Chemistry

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Tumor cell binding to components of the basement membrane is well known to trigger intracellular signaling pathways. Signaling ultimately results in the modulation of gene expression, facilitating metastasis. Type IV collagen is the major structural component of the basement membrane and is known to be a polyvalent ligand, possessing sequences bound by the ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , and ␣ 3 ␤ 1 integrins, as well as cell surface proteoglycan receptors, such as CD44/chondroitin sulfate proteoglycan (CSPG). The role of ␣ 2 ␤ 1 integrin and CD44/CSPG receptor binding on human melanoma cell activation has been evaluated herein using triple-helical peptide ligands incorporating the ␣1(IV)382-393 and ␣1(IV)1263-1277 sequences, respectively. Gene expression and protein production of matrix metalloproteinases-1 (MMP-1), -2, -3, -13, and -14 were modulated with the ␣ 2 ␤ 1 -specific sequence, whereas the CD44-specific sequence yielded significant stimulation of MMP-8 and lower levels of modulation of MMP-1, -2, -13, and -14. Analysis of enzyme activity confirmed different melanoma cell proteolytic potentials based on engagement of either the ␣ 2 ␤ 1 integrin or CD44/CSPG. These results are indicative of specific activation events that tumor cells undergo upon binding to select regions of basement membrane collagen. Based on the present study, triple-helical peptide ligands provide a general approach for monitoring the regulation of proteolysis in cellular systems.Melanoma is one of the most rapidly increasing malignancies in the world in both young and old patients, with over 50,000 newly diagnosed patients each year (1). 1 Mortality from cancer is frequently due to metastasis, given that surgical excision of the primary tumor considerably enhances the prognosis of a patient and prolongs survival (2). Metastasis is a complex series of finely coordinated events that results in cancer cells circulating in lymph and blood vascular systems to invade remote tissues and establish secondary sites of tumor growth (3). Extravasation of the tumor cell into secondary tissues requires alterations in cellular behaviors, resulting from specific adhesion to components of the basement membrane. Tumor cells respond to each of the various components of the ECM, 2 including the collagens; noncollagenous glycoproteins, such as fibronectin and laminin; and proteoglycans, such as decorin and syndecan (4). These interactions are known to occur through several families of cell surface receptors, including the integrins and cell surface proteoglycans.Integrins are heterodimeric proteins composed of one ␣ and one ␤ subunit and are the best described of the cell surface adhesion molecules. To date, there are 18 different ␣ subunits and 8 distinct ␤ subunits identified that combine to form at least 24 heterodimers (5-7). Although the specific integrin expression profile can fluctuate with tumor type and stage of progression, highly metastatic melanoma cells are known to up-regulate expression of, and ␣ 6 ␤ 4 integrins while down-regulating the expression ...

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Section: Discussionmentioning

confidence: 99%

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

Baronas-Lowell

Lauer‐Fields

Borgia³

et al. 2004

Journal of Biological Chemistry

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“…CSE binds to collagen type ll, V and Vlll, whereas heparin binds to collagen type V and lX, and other GAGs do not interact with any type of collagen [40]. The domain structure of CSE responsible for binding to type V collagen has been elucidated by Takagaki et al [41]. They found that three consecutive GlcAb1-3GalNAc (4S,6S) units were a prerequisite for the interaction.…”

Section: Discussionmentioning

confidence: 96%

Detection of chondroitin sulfate‐binding proteins on the membrane

Saito

Munakata

2004

Electrophoresis

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Chondroitin sulfate is a ubiquitous component of proteoglycans that is present both in the extracellular matrix and at the cell surface of various tissues. Until recently, chondroitin sulfate has attracted less attention than heparan sulfate and dermatan sulfate, owing to the limited number of known chondroitin sulfate-binding proteins. To determine the biological function of chondroitin sulfate, biotinylated probes were prepared and used to search for binding proteins. Chondroitin sulfates A, C, D, and E were biotinylated through either the uronic acid or the residual core peptide. Lysates from mouse Lewis lung carcinoma (3LL) cells were blotted onto a nitrocellulose membrane after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the membrane was treated with the biotinylated chondroitin sulfates. Among the chondroitin sulfate variants, the E type showed the most intense bands upon visualization of the membrane with avidin-conjugated alkaline phosphatase and the appropriate substrates. The binding of chondroitin sulfate E to proteins in the cell lysate was not affected by the A, C or D variants but was reduced by treatment with dermatan sulfate. Lysates from 3LL cells were also treated with biotinylated chondroitin sulfate E and, after two-dimensional (2-D) electrophoresis and blotting, several chondroitin sulfate E-binding proteins including lamins and heterogeneous nuclear ribonucleoproteins were identified by mass spectrometry.

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“…Recent remarkable research has revealed some specific biological properties of CS-E, [16][17][18][19][20][21] whereas sufficient amounts of CS-E have not been detected in other animals. In addition, CS composed exclusively of the Etype cannot be obtained naturally.…”

Section: Resultsmentioning

confidence: 99%

Sulfation Patterns and the Amounts of Chondroitin Sulfate in the Diamond Squid,Thysanoteuthis rhombus

Tamura

Arima

Imazu

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Domain Structure of Chondroitin Sulfate E Octasaccharides Binding to Type V Collagen

Cited by 59 publications

References 50 publications

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

Detection of chondroitin sulfate‐binding proteins on the membrane

Sulfation Patterns and the Amounts of Chondroitin Sulfate in the Diamond Squid,Thysanoteuthis rhombus

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