The compliance rate at our institution is very low. We identified a few factors affecting adherence to respiratory hygiene measures that are of potential use in targeting groups and formulating recommendations.
and polycystin-2 are involved in autosomal dominant polycystic kidney disease by unknown mechanisms. These two proteins are located in primary cilia where they mediate mechanosensation, suggesting a link between cilia function and renal disease. In this study, we sought to characterize the subcellular localization of polycystin-L, a closely related member of polycystin-2, in epithelial renal cell lines. We have shown that endogenous polycystin-L subcellular distribution is different in proliferative and nonproliferative cultures. Polycystin-L is found mostly in the endoplasmic reticulum in subconfluent cell cultures, while in confluent cells it is redistributed to sites of cell-cell contact and to the primary cilium as is polycystin-1. Subcellular fractionation confirmed a common distribution of polycystin-L and polycystin-1 in the fractions corresponding to those containing the plasma membrane of postconfluent cells. Reciprocal coimmunoprecipitation experiments showed that polycystin-L was associated with polycystin-1 in a common complex in both subconfluent and confluent cell cultures. Interestingly, we also identified a novel site for a polycystin member (polycystin-L) in unciliated cells, the centrosome, which allowed us to reveal an involvement of polycystin-L in cell proliferation. cilia; cell proliferation; autosomal polycystic kidney disease POLYCYSTINS ARE A NOVEL class of transmembrane proteins, whose founding members were polycystin-1 (PC1) and polycystin-2, coded by PKD1 and PKD2, respectively. To date, eight mammalian polycystins have been discovered and can be separated into two categories according to their predicted structure. The first is the PC1-like subfamily which includes PC1 (10,19,20), and the protein products of PKD1L1 (57), PKD1L2, PKD1L3 (25), and PKDREJ (18). Each of these has 11 predicted transmembrane-spanning regions, a large extracellular NH 2 terminus and a short cytoplasmic COOH terminus. The second is the polycystin-2-like subfamily which includes polycystin-2 (33) and the products of PKDL/PKD2L (40, 54) and PKD2L2 (15,52). Their predicted protein structure, containing six transmembrane-spanning regions with intracellular NH 2 and COOH termini, has such a strong similarity to the transient receptor potential (TRP) channels, that the polycystin-2-like subfamily is now included in the TRP superfamily (TRPP) (17,36,37).
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