Stimulation of mouse B cells by a factor that coisolates with T-cell proteoglycan

Levitt, Daniel; Olmstead, Linda

doi:10.1016/0008-8749(86)90269-8

Cited by 14 publications

(5 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This poses an interesting question as to the function of the proteoglycans produced by the nongranular cells. Similar to the scenario of the platelet proteoglycan acting as a carrier of platelet factor 4 [16], a T-cell proteoglycan has been shown to co-purify with a factor(s) that stimulates the proliferation and differentiation of B-cells [20]. It is possible that other members of this family of proteoglycans may also act as carriers for cytokines.…”

Section: Discussionmentioning

confidence: 93%

Expression pattern of a hematopoietic proteoglycan core protein gene during human hematopoiesis

et al. 1991

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 93%

Expression pattern of a hematopoietic proteoglycan core protein gene during human hematopoiesis

et al. 1991

View full text Add to dashboard Cite

“…Relevant also to the results presented here is the demonstration that human T-cells are growth-inhibited when cultured in the presence of xylosides (Christmas et al, 1988). Furthermore, a factor that stimulates B-cell proliferation and differentiation has been shown to co-purify with a Tcell CSPG (Levitt & Olmstead, 1986). The present investigation shows that ,8-D-xylosides cause effects leading ultimately to a decrease in the capacity of cells to proliferate.…”

Section: Discussionmentioning

confidence: 99%

The effect of β-d-xylosides on the proliferation and proteoglycan biosynthesis of monoblastic U-937 cells

Kolset

Sakurai

Ivhed

et al. 1990

Biochemical Journal

View full text Add to dashboard Cite

The monoblastic cell line U-937 was cultured in the presence of C-ethyl beta-D-xyloside (E-xyl), hexyl beta-D-thioxyloside (HX-xyl), p-nitrophenyl beta-D-xyloside, phenyl beta-D-xyloside or phenyl alpha-D-xyloside. All of the beta-D-xylosides inhibited proliferation, but HX-xyl was by far the most efficient, and had a maximum effect at 1 mM concentration. The inhibitory effect of HX-xyl could be reversed; after washing, the HX-xyl-treated cells proliferated with a pattern similar to that of control cells. For more detailed analysis of the effects of beta-D-xylosides on cell proliferation and chondroitin sulphate (CS)/chondroitin sulphate proteoglycan (CSPG) structure, a comparison between the effects of E-xyl and HX-xyl was made. Treating the cells with 1 mM-HX-xyl resulted in a large increase in CS synthesis, whereas 1 mM-E-xyl had only minor effects on the rate of PG/glycosaminoglycan synthesis. Sepharose CL-6B gel chromatography of medium and cell fractions from 35S-labelled cells revealed that HX-xyl treatment resulted in the expression of only free CS chains, whereas E-xyl exposure leads to the synthesis of both large and small CSPGs, as well as some free CS chains. The expression of elevated levels of free CS chains was clearly correlated to the inhibition of proliferation. The proliferation of U-937-4, a clone of U-937 synthesizing ten times more CSPG/CS than the parent line, was equally inhibited by HX-xyl treatment. With this clone, however, there was no stimulation of CS synthesis after xyloside exposure, indicating that the elevated level of CS evident after xyloside treatment of the parent cell line is not causing the inhibition of proliferation. Furthermore, the biosynthesis of hyaluronate was shown not to be implicated in the xyloside-induced decrease in proliferation. The inhibition of proliferation observed in the presence of 1 mM-HX-xyl did not lead to differentiation of the cells into macrophage-like cells, as is observed when the cells are cultured in the presence of phorbol esters, agents also known to inhibit proliferation of U-937 cells.

show abstract

“…In addition, the data present interesting ramifications in terms of the functions of lymphocyte proteoglycans and indicate a possible role for proteoglycans in the immune system. Such a role has been highlighted by recent reports that a factor that coisolates with T-cell proteoglycan as well as the T-cell proteoglycan itself is capable of stimulating B-cells (Levitt, 1987;Levitt and Olmstead, 1986).…”

Section: Discussionmentioning

confidence: 99%

“…Although the functions of lymphocyte-produced proteoglycans have not been elucidated, it is of interest to note that B cells are stimulated to proliferate by a factor that coisolates with a T-cell proteoglycan (Levitt and Olmstead, 1986). In addition, the invariant chain associated with the immune-associated (Ia) antigens of various lymphoid-like cells has been demonstrated to be the protein core of a chondroitin sulfate proteoglycan (Giacoletto, et al, 1986;Sant et al, 1985) and is intimately associated with antigen presentation (Sivak et al, 1987).…”

mentioning

confidence: 99%

Effect of mitogen and lymphokine stimulation on proteoglycan synthesis by lymphocytes

Bartold

Haynes

Vernon‐Roberts

1989

Journal Cellular Physiology

View full text Add to dashboard Cite

The ability of mouse thymocytes and peripheral blood lymphocytes from rats to synthesize and secrete proteoglycans in the presence of a variety of mitogens and lymphokines was studied in vitro, and it was confirmed that such lymphocytes synthesize and secrete significant quantities of proteoglycans. Mitogenic stimulation of the cells with phytohaemagglutanin (PHA) induced a fourfold increase in proteoglycan synthesis; stimulation with interleukin-1 stimulated proteoglycan synthesis up to fivefold. Proteoglycan synthesis could also be stimulated by culturing the cells in the presence of interleukin-2. To determine if this response was related to cell proliferation, the cells were cultured in the presence of PHA and either cyclosporine or prostaglandin E2, two agents that inhibit lymphocyte proliferation. Under these conditions, proteoglycan synthesis remained elevated, indicating that this effect may be independent of cell proliferation. Chemical analysis of the proteoglycans indicated them to be composed of chondroitin sulfate and heparan sulfate. Their molecular size was small compared with cartilage proteoglycans but similar to the small dermatan sulfate proteoglycans synthesized by fibroblasts. On the basis of molecular size, three proteoglycan population were identified, and their relative proportions were altered by mitogenic stimulation of the cells. Taken together, these findings imply that proteoglycan synthesis is intimately associated with lymphocyte activation and may be related to cellular function in immune responses.

show abstract

Stimulation of mouse B cells by a factor that coisolates with T-cell proteoglycan

Cited by 14 publications

References 42 publications

Expression pattern of a hematopoietic proteoglycan core protein gene during human hematopoiesis

Expression pattern of a hematopoietic proteoglycan core protein gene during human hematopoiesis

The effect of β-d-xylosides on the proliferation and proteoglycan biosynthesis of monoblastic U-937 cells

Effect of mitogen and lymphokine stimulation on proteoglycan synthesis by lymphocytes

Contact Info

Product

Resources

About