Endocytosis of sulphated proteoglycans by cultured skin fibroblasts

Prinz, Roswitha; Schwermann, Jochen; Buddecke, Eckhart; Figura, Kurt Von

doi:10.1042/bj1760671

Cited by 41 publications

(17 citation statements)

References 20 publications

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“…The uptake of fluorescein-labelled proteoglycan ( Fig. 5) (Kresse et al, 1975;Prinz et al, 1978;. These reports suggest that proteoglycans and glycosaminoglycans are recognized by two different receptor species.…”

Section: Discussionmentioning

confidence: 85%

Endocytosis and degradation of chondroitin sulphate by liver endothelial cells

Smedsrød¹,

Kjellén²,

Pertoft³

1985

Biochemical Journal

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Section: Discussionmentioning

confidence: 85%

Endocytosis and degradation of chondroitin sulphate by liver endothelial cells

Smedsrød¹,

Kjellén²,

Pertoft³

1985

Biochemical Journal

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“…The number and size of lysosomes in cultured smooth muscle cells have been shown to increase as the serum concentration of the culture medium is increased (1). Lysosomes isolated from other cell types such as polymorphonuclear leukocytes have been found to contain chondroitin sulfate (23,24), and lysosomes of human fibroblasts in culture will accumulate sulfated mucopolysaccharides (25) and sulfated proteoglycans (26) from the medium.…”

Section: Discussionmentioning

confidence: 99%

Lysosomal composition in cultured vascular smooth muscle cells: electron probe analysis.

James-Kracke¹,

Sloane²,

Shuman³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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Spherical electron-dense organelles in the perinuclear region of cultured guinea pig aortic smooth muscle cells were identified as lysosomes by their ability to accumulate acridine orange and by cytochemical demonstration of their acid phosphatase content. The number and size of lysosomes increased in subcultured cells. The elemental composition of the lysosomes was quantitated by electron probe analysis of whole freeze-dried cells and of cryosections. In lysosomes at this stage in their development, the sulfur concentration was higher than that in the cytoplasm and the K/Na concentration ratio was similar to that in the cytoplasm.In a recent study of the elemental composition of cultured aortic smooth muscle cells, we observed numerous electron-dense spherical organelles (dark bodies) concentrated in the perinuclear region. Fowler et al. (1) had previously reported a substantial increase in the number of lysosomes in subcultured vascular smooth muscle cells; therefore, we suspected that the dark bodies were of lysosomal origin. Because the composition of lysosomes in situ has not been previously quantitated, we present here the results of electron probe analysis of the elemental composition of dark bodies in intact cells and in cryosections of the cells. The identity of the dark bodies (lysosomes) was established by their uptake of acridine orange (2) and their cytochemically demonstrable reaction product for acid phosphatase, a lysosomal enzyme (3). METHODSCulturing and Freezing of Cells. Smooth muscle cells from guinea pig aortic medial explants were cultured on stainless steel grids attached to Falcon culture dishes by a sheet of Formvar. Cells were serially passaged by trypsinization (0.25% wt/vol) in Ca-and Mg-free basic salt solution (GIBCO) or single cells were separated with collagenase and elastase as described by Ives et al. (4). The culture medium was prepared from minimal essential medium (GIBCO) with 2.25 g of NaHCO3 per liter of medium, 2mM glutamine, 106 units of penicillin, 250 ,g of Fungizone, 105 ,ug of streptomycin, and 1 mg of ascorbic acid per liter and 10% (vol/vol) fetal calf serum; it was equilibrated in a moist atmosphere of air mixed with CO2 to adjust the pH to approximately 7.4. For electron probe analysis (see below) of whole cells, the grids were removed before the cells became confluent and were attached to stainless steel wire handles twisted into clips. The cells were oxygenated at 37°C in a beaker of culture medium for 30 min. Each grid was plunged intoThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in

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“…The receptor-mediated endocytosis of homologous proteoglycans by cultured cells requires the interaction between a specific receptor site located in coated or non-coated pits [15] on the cell surface and a recognition site on the protein core of the proteoglycan molecule [14]. The chemical features of the proteoglycan-specific cell surface receptor are unknown.…”

Section: Discussionmentioning

confidence: 99%

“…Correspondence to E. Buddecke the extracellular compartment by endocytosis [12-151. Endocytosis was found to be a specific and saturable process involving specific binding of proteoglycan molecules to cell surface receptors [14,151. The endocytosed proteoglycans are delivered to the lysosomal compartment for enzymatic degradation.…”

mentioning

confidence: 99%

“…From bovine arterial tissue a high-molecular-mass proteoglycan-hyaluronate complex and a low-molecular-mass proteoglycan monomer have been isolated [6 -91, but widely different relative molecular masses have been recognized for both the proteoglycan-hyaluronate complex ( M , 0.8 -2.6 x lo6) and the proteoglycan monomer ( M , [8][9][10][11][12][13][14][15][16][17][18][19][20] x lo6).…”

mentioning

confidence: 99%

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High‐uptake and low‐uptake forms of proteoglycans secreted by arterial smooth muscle cells

Schmidt

Buddecke

1985

European Journal of Biochemistry

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1 . Cultured arterial smooth muscle cells synthesize and secrete two types of sulfated proteoglycans, designated as proteoglycan A and B, into the culture medium. They are isolated as immunologically distinct monomers with relative molecular masses of 280 x 103 and 180 x lo3 and are characterized as chondroitin-sulfate-rich (A) and dermatan-sulfate-rich (B) proteoglycans. Both proteoglycan A and B were labelled with [3sS]sulfate and used for studies of endocytosis.2. Uptake of proteoglycan B by arterial smooth muscle cells shows saturable kinetics. At saturation (500 pM) one cell may endocytose up to 1.5 x 10' proteoglycan B molecules/h. Proteoglycan A is internalized at a 10-fold lower rate. No saturation kinetics were observed at high proteoglycan A concentrations (500 FM).3. Endocytosis of proteoglycan B in the presence of an excess of proteoglycan A and vice versa suggest that proteoglycan A and B do not compete for the same receptor site. Free hyaluronate or chondroitin sulfate do not inhibit the uptake of proteoglycan B or A.4. The results suggest that proteoglycan B is internalized by arterial smooth muscle cells via a high-affinity receptor-mediated process, whereas proteoglycan A is taken up by fluid endocytosis and/or by low-affinity endocytotic processes.

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Endocytosis of sulphated proteoglycans by cultured skin fibroblasts

Cited by 41 publications

References 20 publications

Endocytosis and degradation of chondroitin sulphate by liver endothelial cells

Endocytosis and degradation of chondroitin sulphate by liver endothelial cells

Lysosomal composition in cultured vascular smooth muscle cells: electron probe analysis.

High‐uptake and low‐uptake forms of proteoglycans secreted by arterial smooth muscle cells

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