Membrane-associated chondroitin sulfate proteoglycan and fibronectin mediate the binding of hemopoietic progenitor cells to stromal cells

Minguell, José J.; Hardy, Cheryl L.; Tavassoli, Mehdi

doi:10.1016/0014-4827(92)90364-e

Cited by 35 publications

(29 citation statements)

References 31 publications

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“…Plates were incubated with each protein for 1 h at room temperature followed by an additional incubation period (1 h) with D-PBS containing 1% BSA to saturate non-specific binding sites (Minguell et al, 1992a).…”

Section: Cell Adherence Assaymentioning

confidence: 99%

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Modifications in the synthesis of membrane‐associated chondroitin sulfate proteoglycans in hemopoietic progenitor cells are accompanied by alterations in their adhesive properties

Conget

Minguell

1994

Journal Cellular Physiology

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In vitro studies in our laboratory have indicated that murine hemopoietic progenitor cell (HPC) lines, irrespective of their differentiation stage, synthesize and accumulate in the cell membrane a unique species of chondroitin sulfate proteoglycan (CS-PG). It has been postulated that CS-PG participates in HPC adhesion to pericellular stromal fibronectin by interacting with its heparin-promoting binding region. To further support this contention, we first attempted to modify CS-PG synthesis in HPC by the use of chlorate and p-nitrophenyl beta-D-xyloside, which inhibit sulfation and glycosaminoglycan (GAG) addition in proteoglycans, respectively. We then studied the effect that these modifications may have in the adhesive capacity of HPC to interact with fibronectin and its cell- and heparin-promoting binding chymotryptic fragments. Treatment with chlorate which resulted in a decreased sulfation of membrane-associated 35 S-labeled CS-PG, as judged by ion exchange chromatography, did not affect HPC adhesion to fibronectin or its fragments. However, beta-xyloside treatment which reduces the abundance of membrane-associated CS-PG, as evidenced by molecular sieve chromatography, produced a major and specific decrease in HPC adhesion to the heparin-promoting binding fragment of fibronectin. These results indicate that CS-PG are involved in HPC interaction with fibronectin, in a mode that seems to be dependent on the differentiation stage of HPC.

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Section: Cell Adherence Assaymentioning

confidence: 99%

“…INC. and Minguell, 1991;Minguell et al, 1992a). The participation of membrane-associated CS-PG in HPC adhesiveness has been suggested by the observation that the stability of this membrane component is enhanced upon binding of progenitor to stroma (Minguell and Tavassoli, 1989).…”

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confidence: 94%

Modifications in the synthesis of membrane‐associated chondroitin sulfate proteoglycans in hemopoietic progenitor cells are accompanied by alterations in their adhesive properties

Conget

Minguell

1994

Journal Cellular Physiology

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“…It has been found in in vitro experiments with fibronectin-coated microtiter plates that the CD49d (VLA-4) and CD49e (VLA-5) antigens on CD34+ blasts are in a nonfunctional state [68], When activated with phorbol myristate acetate (PMA, 1 ng/ml), adherence to fibronectin could be demonstrated. In addition to glyco protein matrix elements, proteoglycans such as heparan sulfate [69,70], hyaluronate/CD44 [71], chondroitin sul fate [72], and other galactosyl-and mannosyl-specific lec tins [48] may all be involved in the adhesion of normal hematopoietic progenitors to marrow. Siczkowski et al [73] teoglycans are composed of glycosaminoglycan chains co valently bound to a core protein with the nature of the repeating disaccharide units of the GAG moiety deter mining some of the structural characteristics of the pro teoglycan.…”

Section: Cell-matrix Interactionsmentioning

confidence: 99%

Expression and Function of Adhesion Receptors in Acute Myelogenous Leukemia: Parallels with Normal Erythroid and Myeloid Progenitors

Liesveld¹

1997

Acta Haematol

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A variety of adhesion receptors are expressed on the blast cells in patients with acute myelogenous leukemia. The panel of receptors expressed demonstrates heterogeneity just as there is morphologic, histochemical, cytogenetic, and molecular genetic variation between various cases of acute myelogenous leukemia. The adhesion receptors expressed contain representatives of all the main classes of adhesion receptors, but often there is no correlation of the adhesion receptor phenotype with the morphologic or clinical features of acute myelogenous leukemia. These receptors function in interactions of myelogenous leukemia blasts with the cellular and matrix components of the marrow microenvironment, and there is evidence that they are involved in blast release from marrow and in homing of blasts to extrameduilary sites. Evidence is starting to accumulate suggesting that adhesive interactions may influence the proliferation and survival of leukemic cells, but the precise role that these molecules play in the generation and sustenance of the leukemic state remains undetermined.

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“…However, our knowledge on the heparan sulphate proteoglycans, involved in the interaction of haematopoietic-progenitor and stromal cell lines, is still limited. In fact, there are only few reports on proteoglycans from haematopoietic-bone-marrow cells [24,[37][38][39][40][41][42][43][44] pointing to stromal cells, rather than haematopoietic-stem cells or progenitor cells, as the source of heparan sulphate proteoglycans [24,[37][38][39][40][42][43][44]. Recently, we have analysed the expression of heparan sulphate proteoglycans in several murine and human haematopoietic-progenitor and stromal cell lines [43].…”

Section: Discussionmentioning

confidence: 99%

Expression of glypican-4 in haematopoietic-progenitor and bone-marrow-stromal cells

Siebertz

Stöcker

Drzeniek

et al. 1999

Biochemical Journal

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Heparan sulphate proteoglycans and the extracellular matrix of bone-marrow-stromal cells are important components of the microenvironment of haematopoietic tissues and are involved in the interaction of haematopoietic stem and stromal cells. Previous studies have emphasized the role of heparan sulphate proteoglycan synthesis by bone-marrow-stromal cells. In the present study we describe the expression of glypican-4 (GPC-4), belonging to the glypican family, in bone-marrow-stromal cells and haematopoietic-progenitor cells of human and murine origin. Expression of GPC-4 was shown on the mRNA-level by reverse transcription-PCR and Northern blot analysis. Amplification products were cloned and sequenced, to confirm these results. To analyze the expression of GPC-4 on the protein level, polyclonal antibodies against selected peptides were raised in rabbits. Western blot analysis showed expression of GPC-4 as a heparan sulphate proteoglycan in the human haematopoietic-progenitor cell line TF-1 and normal human bone marrow. These results were confirmed by FACS analysis of TF-1 cells. Furthermore, GPC-4-positive progenitor cells and stromal cells were enriched from normal human bone marrow by magnetic-cell sorting and analysed by confocal laser-scanning microscopy.

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Membrane-associated chondroitin sulfate proteoglycan and fibronectin mediate the binding of hemopoietic progenitor cells to stromal cells

Cited by 35 publications

References 31 publications

Modifications in the synthesis of membrane‐associated chondroitin sulfate proteoglycans in hemopoietic progenitor cells are accompanied by alterations in their adhesive properties

Modifications in the synthesis of membrane‐associated chondroitin sulfate proteoglycans in hemopoietic progenitor cells are accompanied by alterations in their adhesive properties

Expression and Function of Adhesion Receptors in Acute Myelogenous Leukemia: Parallels with Normal Erythroid and Myeloid Progenitors

Expression of glypican-4 in haematopoietic-progenitor and bone-marrow-stromal cells

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