No abstract

A self-hardening calcium-phosphate cement (CPC) containing Ca(4)(PO(4))(2)O and CaHPO(4) has been shown in clinical studies to be efficacious for repairing bone defects. This and several other similar CPCs harden in 10 min with the use of a phosphate solution as the liquid and form hydroxyapatite (HA) as the product. The present study investigated the properties of water-free, glycerol-containing CPC pastes that are stable in the package and would harden only after being delivered to a defect site where glycerol-tissue fluids exchange occurs. Premixed CPC pastes were prepared by combining cement liquids containing glycerol and various amounts of hydroxypropyl methylcellulose/Na(2)HPO(4), with CPC powders that contained (1) Ca(4)(PO(4))(2)O and CaHPO(4), (2) alpha-Ca(3)(PO(4))(2) and CaCO(3), or (3) CaHPO(4) and Ca(OH)(2). The hardening times and 1-d and 7-d diametral tensile strengths were measured on samples that hardened in an in vitro model that allowed exchange of glycerol and physiologic-like solution (PLS) through fritted glass slides at 37 degrees C. All pastes had excellent washout resistance; they remained intact and hardened while immersed in PLS and formed HA as products. Newman-Keuls multiple comparison tests indicated that the Na(2)HPO(4) amount, not the hydroxypropyl methylcellulose (HMC) amount, significantly (p < 0.05) affected the strength and hardening time. Although the premixed CPCs generally have longer hardening times and lower strengths, these pastes have excellent washout resistance before hardening and can be prepared in advance under well-controlled conditions.

Abstract-LR11, a member of the LDL receptor family, is highly expressed in vascular smooth muscle cells (SMCs) of the hyperplastic intima, and induces enhanced migration of SMCs in vitro via its upregulation of urokinase-type plasminogen activator receptor (uPAR) expression. In this study, we have delineated the mechanism by which LR11 elevates the expression levels of uPAR in SMCs. Secretion of soluble LR11 is induced in SMCs during the rapidly proliferating phase, and the secreted LR11 induces the migration activities of SMCs. Both the cell-anchored and secreted forms of LR11 have the capacity to bind to and form complexes with uPAR. LR11-overexpressing cells show significantly enhanced uPAR binding, but decreased uPAR internalization. LR11 colocalizes with uPAR on the cell surface and inhibits the LDL receptor-related protein (

No abstract

No abstract

No abstract

Abstract-Since the molecular identification of the low density lipoprotein receptor (LDLR), an ever increasing number of related proteins have been discovered. These receptors belonging to the LDLR family are thought to play key roles in lipoprotein metabolism in a variety of tissues, including the arterial wall. We have discovered that the expression of a 250-kDa mosaic LDLR-related protein, which we termed LR11 for the presence of 11 LDLR ligand-binding repeats, is markedly induced in smooth muscle cells in the hyperplastic intima of animal models used for the study of atherosclerosis. Here, we demonstrate that the human LR11, when overexpressed in hamster cells, binds and internalizes 39-kDa receptor-associated protein (RAP), an in vitro ligand for all receptors belonging to the LDLR family. Furthermore, LR11 binds the apolipoprotein E (apoE)-rich lipoproteins, ␤-very low density lipoproteins (VLDLs), with a high affinity similar to that of other members, such as the LDLR and VLDL receptor. RAP and ␤-VLDL compete with each other; however, other serum lipoproteins are not able to inhibit their binding. LR11 shows specific binding of apoE-enriched HDL prepared from human cerebrospinal fluid as well as of ␤-VLDL, suggesting that the apoE content of lipoproteins is most likely important for mediating the high-affinity binding to the receptor. LR11-overexpressing cells are able to internalize and degrade the bound ␤-VLDL; these cells also show increased accumulation of cholesteryl esters when incubated with ␤-VLDL. Incubation for 48 hours with ␤-VLDL of LR11-overexpressing cells, but not of control cells, promotes the appearance of numerous intracellular lipid droplets. Taken together, LR11, a mosaic LDLR family member whose expression in smooth muscle cells is markedly induced in atheroma, has all the properties of a receptor for the endocytosis of lipoproteins, particularly for the incorporation of apoE-rich lipoproteins. Key Words: LDL receptors Ⅲ atherosclerosis Ⅲ smooth muscle cells Ⅲ ␤-VLDL R eceptors belonging to the LDL receptor (LDLR) family are thought to play key roles in lipoprotein metabolism in a variety of tissues, including the arterial wall. [1][2][3][4] Recent extensive histochemical studies have shown that receptors belonging to the LDLR family, as well as scavenger receptors mediating the incorporation of modified lipoproteins such as oxidized LDL, show marked induction of their expression during the formation of atherosclerotic lesions. [5][6][7][8][9] For instance, 1 LDLR family member, the so-called VLDL receptor (VLDLR/LR8), has been shown to be highly expressed in smooth muscle cells (SMCs), macrophages, and endothelial cells in rabbit atherosclerotic lesions. 7-9 Furthermore, VLDLR/LR8 has been shown not to be downregulated during ␤-VLDL-induced foam cell formation in vitro, and overexpression of the receptor in fibroblasts causes excessive lipid droplet accumulation in the transformed cells. 10 We and others have discovered and molecularly characterized a novel, unusually complex, and hi...

No abstract