The 94- to 97-kDa mouse macrophage membrane protein that recognizes oxidized low density lipoprotein and phosphatidylserine-rich liposomes is identical to macrosialin, the mouse homologue of human CD68.

Ramprasad, Mysore P.; Fischer, Walter; Witztum, Joseph L.; Sambrano, Gilberto R.; Quehenberger, Oswald; Steinberg, Daniel

doi:10.1073/pnas.92.21.9580

Cited by 302 publications

(190 citation statements)

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“…Our conclusion that the Kupffer cell oxLDL receptor and macrosialin are identical implies that the oxLDL receptor on mouse peritoneal macrophages, which was described by Steinberg and co-workers [11,14], is the same receptor as the Kupffer cell oxLDL receptor described in this paper. The difference in molecular mass (94-97 kDa and 115-120 kDa respectively) between the two could then be explained by differences in glycosylation, since Rabinowitz and Gordon [17,18] showed that glycosylation of macrosialin can differ between different macrophage populations, and is dependent on the state of cell stimulation.…”

Section: Resultssupporting

confidence: 84%

“…Recently, Ramprasad et al [14] found evidence that the 94-97 kDa oxLDL receptor present on mouse peritoneal macrophages is identical with macrosialin. Macrosialin is the mouse homologue of human CD68, a heavily glycosylated protein present on macrophages.…”

Section: Resultsmentioning

confidence: 99%

“…Sparrow et al [10] and Ottnad and colleagues [11] reported the existence of a plasma-membrane protein of 94-97 kDa on mouse peritoneal macrophages that is able to bind oxLDL but not acLDL, and which can also interact with oxidized red blood cells and phosphatidylserine liposomes [12,13]. Recently, this receptor was identified as macrosialin, the mouse homologue of CD68 [14].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a receptor for oxidized low-density lipoproteins on rat Kupffer cells: similarity to macrosialin

Velzen¹,

Silva

Gordon

et al. 1997

Biochemical Journal

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Rat liver Kupffer cell membranes contain a protein that recognizes specifically oxidized low-density lipoproteins (oxLDL). Visualization after blotting under reducing conditions indicates that the receptor is a monomeric protein, with an estimated molecular mass of 115–120 kDa. N-Glycosidase F and endoglycosidase F treatment resulted in a fall in estimated molecular mass of 24 and 11 kDa respectively, whereas O-glycosidase was ineffective. No effect on the extent of interaction with oxLDL was noticed, suggesting that glycans are not essential for ligand recognition. Using a polyclonal antibody to mouse macrosialin, we visualized macrosialin on blot, and compared this glycoprotein with the oxLDL-binding protein. It appears that the two glycoproteins have a similar molecular mass and are comparably affected by treatment with the different glycosidases. Incubation with trypsin resulted in a reduction in the estimated molecular mass of about 25 kDa for both the oxLDL-binding protein and macrosialin. These results indicate that the oxLDL-binding protein and macrosialin are identical, suggesting a role for macrosialin in modified LDL catabolism.

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a receptor for oxidized low-density lipoproteins on rat Kupffer cells: similarity to macrosialin

Velzen¹,

Silva

Gordon

et al. 1997

Biochemical Journal

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“…TSP, or a 140-kDa COOH-terminal domain proteolytic fragment from this protein [13], forms a bridge between the M receptor complex and the PMN ligand specific for TSP. Finally, the lipid receptor responsible for PMN recognition, although not formally characterized, is specific for phosphatidylserine [14].…”

Section: Introductionmentioning

confidence: 99%

Macrophage phagocytosis of wound neutrophils

Meszaros

Reichner

Albina

1999

Journal of Leukocyte Biology

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Resolution of acute inflammation is thought to require the recognition and phagocytosis of apoptotic neutrophils (PMN) through receptorligand interactions with macrophages (M ). This hypothesis was tested in rat wounds by quantifying apoptosis in freshly harvested and aged-in-culture PMN taken from wounds 1-3 days after injury and by using these wound PMN as phagocytic targets for wound, immune-activated peritoneal, and resident peritoneal M . Less than 6% of freshly harvested PMN exhibited characteristics of apoptosis. On aging in culture, day 1 PMN did not undergo apoptosis, whereas 41 ؎ 1 and 29 ؎ 1% of day 2 and 3 PMN, respectively, developed apoptosis, which corresponded to increased ingestion by M .

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“…Many receptors could be involved in BSDL uptake and transcytosis throughout Int407 cells (Ramprasad et al, 1995;Adachi et al, 1997;Dhaliwal and Steinbrecher, 1999;Shirai et al, 1999;Cai et al, 2001;Lobo et al, 2001;Werder et al, 2001;Gillotte-Taylor et al, 2001). Among them the lectin-like oxidized LDL receptor or LOX-1, a 50-kDa protein detected in nearly all tissues examined (Sawamura et al, 1997) has retained our attention.…”

Section: Lox-1 Implication In Bsdl Transcytosismentioning

confidence: 99%

Lectin-like Ox-LDL Receptor Is Expressed in Human INT-407 Intestinal Cells: Involvement in the Transcytosis of Pancreatic Bile Salt–dependent Lipase

Bruneau

Richard

Silvy

et al. 2003

MBoC

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We have recently shown that the pancreatic bile salt-dependent lipase (BSDL) can be taken up by intestinal cells and transported to the blood circulation. This mechanism likely involves (specific) receptor(s) able to bind BSDL and located at the apical intestinal cell membrane. In this study, using Int407 human intestinal cells cultured to form a tight epithelium, we attempted to characterize (the) BSDL receptor(s). We found that an apical 50-kDa protein was able to bind BSDL. Further, we have demonstrated that Int407 cells expressed the lectin-like oxidized-LDL receptor (LOX-1), the upregulation of which by oxidized-LDL potentiates the transcytosis of BSDL, whereas carrageenan and to a lesser extent polyinosinic acid and fucoidan decrease the enzyme transcytosis. The mAb JTX92, which blocks the LOX-1 receptor function, also impaired the BSDL transcytosis. To confirm these results, the cDNA encoding the human intestinal receptor LOX-1 has been cloned, inserted into vectors, and transfected into Int407 cells. Overexpression of LOX-1 by these cells leads to a substantial increase in the BSDL transcytosis. Globally, these data support the view that LOX-1 could be an intestinal receptor for BSDL, which is implicated in the transcytosis of this enzyme throughout Int407 cells. INTRODUCTIONThe bile salt-dependent lipase (BSDL, EC 3.1.1.13), also referred to as carboxyl ester lipase or bile salt-stimulated lipase, is a lipolytic enzyme, synthesized and secreted by the exocrine pancreas (Lombardo, 2001). The secretion of this digestive enzyme requires the participation of the Grp94 molecular chaperone (Bruneau and Lombardo, 1995;Bruneau et al., 1998). Once in the lumen of the duodenum, BSDL, in concert with other pancreatic lipolytic enzymes and preduodenal lipase, acts to complete the digestion of dietary lipids. Indeed, upon activation by primary bile salts, BSDL catalyzes the duodenal hydrolysis of cholesterol esters into free cholesterol and fatty acids before their absorption by intestinal cells (Howles et al., 1996;Weng et al., 1999). Although controversial (Howles et al., 1996), BSDL could also participate in the intestinal free cholesterol absorption (LopezCandales et al., 1993), acting as a cholesterol transfer protein (Myers-Payne et al., 1995), or as a cholesterol reesterifying enzyme after cholesterol absorption by intestinal cells (Bhat and Brockman, 1982).A fraction of BSDL, possibly associated with Grp94, reaches the vicinity of microvilli and upon binding to the surface of intestinal cells is internalized and transported up to the blood compartment (Bruneau et al., , 2000a(Bruneau et al., , 2000b(Bruneau et al., , 2003. Consequently, BSDL has been reported in the plasma of normolipidemic patients where it associates with apolipoprotein B-containing lipoproteins such as low-density lipoprotein (LDL), chylomicron and very-low-density lipoprotein (VLDL; Bruneau et al., 2003).The pathway of BSDL throughout intestinal cells has been recently delineated using Int407 cells (Bruneau et al., 2001), which do not e...

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The 94- to 97-kDa mouse macrophage membrane protein that recognizes oxidized low density lipoprotein and phosphatidylserine-rich liposomes is identical to macrosialin, the mouse homologue of human CD68.

Abstract: The 94-to 97-kDa mouse macrophage membrane protein that recognizes oxidized low density lipoprotein and phosphatidylserine-rich liposomes is identical to macrosialin, the mouse homologue of human CD68

Cited by 302 publications

References 41 publications

Characterization of a receptor for oxidized low-density lipoproteins on rat Kupffer cells: similarity to macrosialin

Characterization of a receptor for oxidized low-density lipoproteins on rat Kupffer cells: similarity to macrosialin

Macrophage phagocytosis of wound neutrophils

Lectin-like Ox-LDL Receptor Is Expressed in Human INT-407 Intestinal Cells: Involvement in the Transcytosis of Pancreatic Bile Salt–dependent Lipase

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