Expression cloning of a functional glycoprotein ligand for P-selectin

Sako, Dianne; Chang, Xiao-Jia; Barone, K M; Vachino, G; White, Holly M.; Shaw, Gray D.; Veldman, Geertruida M.; Bean, Kevin M.; Ahern, Tim J.; Furie, Bruce; Cumming, Dale A.; Larsen, G R

doi:10.1016/0092-8674(93)90327-m

Cited by 692 publications

(505 citation statements)

References 33 publications

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“…These mucin-associated antigens are known to bind endothelial cells through the P-and E-selectins, and the cell-adhesion molecule, ICAM-1 (Regimbald et al, 1996). The Pselectin ligand (PSGL-1) (Sako et al, 1993) presents a structure similar to MUC1 and MUC4 and carries within its repetitive domain O-glycosidic chains with terminal sugars comparable to those of MUC1 and MUC4 in tumoral situations. Therefore, in addition to favouring the release of PC cells, MUC1 and MUC4 also facilitate their extravasation into and/or from the circulation (Burdick et al, 1997).…”

Section: Implication Of Mucins In the Pathogenesis Of Pcmentioning

confidence: 99%

Multiple roles of mucins in pancreatic cancer, a lethal and challenging malignancy

et al. 2004

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Mucins are members of an expanding family of large multifunctional glycoproteins. Pancreatic mucins have important biological functions, including the protection, lubrication, and moisturisation of the surfaces of epithelial tissues lining ductal structures within the pancreas. Several lines of evidence support the notion that deregulated mucin production is a hallmark of inflammatory and neoplastic disorders of the pancreas. Herein, we discuss the factors that contribute to the lethality of pancreatic cancer as well as the key role played by mucins, particularly MUC1 and MUC4, in the development and progression of the disease. Aspects pertaining to the aberrant expression and glycosylation of mucins are discussed, with special emphasis on their potential impact on the design and implementation of adequate diagnostic and therapeutic strategies for combating this lethal malignancy.

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Section: Implication Of Mucins In the Pathogenesis Of Pcmentioning

confidence: 99%

Multiple roles of mucins in pancreatic cancer, a lethal and challenging malignancy

et al. 2004

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“…In addition to the O-linked structures discussed above, the PSGL-1 sequence also contains three sites for N-glycosidic glycosylation and results from previous studies suggest that the molecule may contain significant amounts of N-linked oligosaccharides [9]. The nature of these structures, however, has not been determined.…”

Section: Introductionmentioning

confidence: 97%

“…PSGL-1 is a ligand capable of binding P-, Eand L-selectin [7][8][9][10][11][12][13]. The molecule is expressed on several cell types, including human leukocytes and the human myeloid cell line HL-60 [7], [10], [14].…”

Section: Introductionmentioning

confidence: 99%

“…The molecule is expressed on several cell types, including human leukocytes and the human myeloid cell line HL-60 [7], [10], [14]. Moreover, successful cloning from an HL-60 cDNA library has revealed that PSGL-1 is a type I membrane glycoprotein with a domain structure similar to that of many cell surface mucins [9], [15]. The amino acid sequence contains a mucin domain composed of 15 serine/threonine rich decameric repeat sequences that are believed to be extensively substituted with O-linked oligosaccharides [9], [10], [16].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, successful cloning from an HL-60 cDNA library has revealed that PSGL-1 is a type I membrane glycoprotein with a domain structure similar to that of many cell surface mucins [9], [15]. The amino acid sequence contains a mucin domain composed of 15 serine/threonine rich decameric repeat sequences that are believed to be extensively substituted with O-linked oligosaccharides [9], [10], [16]. PSGL-1 is expressed only in quite limited quantities on the surface of ligand-carrying cells, hence purification in amounts sufficient for characterization of oligosaccharide structures at individual sites it not practical using current technology [17].…”

Section: Introductionmentioning

confidence: 99%

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Partial characterization of the N-linked oligosaccharide structures on P-selectin glycoprotein ligand-1 (PSGL-1)

Aeed¹,

Geng

Asa³

et al. 2001

Cell Res

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PSGL-1, a specific ligand for P-, E-and L-selectin, was isolated from in vivo [ 3 H]-glucosamine labeled HL-60 cells by a combination of wheat germ agglutinin-agarose and P-or E-selectin-agarose chromatography. N-linked oligosaccharides were released from the purified, denatured ligand molecule by peptide: N-glycosidase F treatment and, following separation by Sephacryl S-200 chromatography, partially characterized using lectin, ion-exchange and size-exclusion chromatography in combination with glycosidase digestions. The data obtained suggest that the N-glycans on PSGL-1 are predominantly core-fucosylated, multiantennary complex type structures with extended, poly-N-acetyllactosamine containing outer chains. A portion of the outer chains appears to be substituted with fucose indicating that the N-glycans, in addition to the Oglycans on PSGL-1, may be involved in selectin binding.

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Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src

Soltesz

Powers

Geng³

et al. 1997

Int. J. Cancer

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Adhesion of metastatic cancer cells at secondary sites is known to be regulated by several families of adhesion proteins , including selectins and integrins. Colon carcinoma cells have been shown to tether to and roll on both stimulated endothelial cells and purified E-selectin. We have demonstrated that HT-29 human colon carcinoma cells adhere specifically to an E-selectin-IgG chimera. Upon adhesion to E-selectin, the amount of tyrosine phosphorylation of several proteins in HT-29 cell lysates increases compared with cells in bovine serum albumin-coated wells on phosphotyrosine Western blots; this increase is statistically significant. This effect is specific for adhesion to E-selectin, since addition of an E-selectin blocking monoclonal antibody (MAb), E3, to the wells causes a statistically significant decrease in tyrosine phosphorylation relative to E-selectin alone on phosphotyro-sine Western blots. One protein that is affected this way has been identified as c-src. Kinase assays show a dose-dependent and statistically significant decrease in c-src activity upon adhesion to E-selectin, which correlates with an increase in phosphorylation of Tyr 527, the negative regulatory tyrosine. CnBr digestion of 32 P-labeled c-src shows an increase in phosphorylation of tyrosine 527 after adhesion to E-selectin. Our results may identify a signaling pathway involving the E-selectin ligand on HT-29 cells and c-src. Int.

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Expression cloning of a functional glycoprotein ligand for P-selectin

Cited by 692 publications

References 33 publications

Multiple roles of mucins in pancreatic cancer, a lethal and challenging malignancy

Multiple roles of mucins in pancreatic cancer, a lethal and challenging malignancy

Partial characterization of the N-linked oligosaccharide structures on P-selectin glycoprotein ligand-1 (PSGL-1)

Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src

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