LibQUAL+ Survey 2004 @ Queen's University Library : analysis of results

Queen's University Library was one of 202 libraries, including 57 members of the Association of Research Libraries (ARL), to survey its users in spring 2004 using the LibQUAL+ survey instrument. LibQUAL+ was designed by ARL to assist libraries in assessing the quality of their services and identifying areas for improvement. # Overall: Queen's scored higher than the average for all ARL participants and 1st among the 2004 Canadian participants. This relatively high rating is due to very high scores in the dimensions of Library as Place and Affect of Service. However, there is considerable need for improvement in the area of Information Control where Queen's rated well below the ARL average. # Affect of Service: Queen's strong overall ratings are supported by the many respondent comments praising customer service throughout the system. The ratings and survey comments indicate greatest appreciation by faculty and more experienced students (e.g. graduate students) for the instruction and on-site services provided by the libraries. The ratings also indicate that undergraduates, growing up with the web, want and expected to be able to access library resources independently and do not value these services as highly. The comments also indicated some specific areas for improvement throughout the library system. # Library as Place : All Queen's libraries except for Law ranked well above the ARL and Canadian averages. Overall, Library as Place ranked lowest in importance among the service dimensions for all ARL participants including Queen's. Comparative analysis of LibQUAL results since the survey began shows a decline in “desired” ratings for Library as Place. However, undergraduates continue to give strong "desired" ratings to certain aspects of Library as Place and a relatively high rating for "minimum expected" service. The comments from Queen's survey respondents and ARL's analyses of focus groups indicate that undergraduates value the library much more as a place to study and work with peers rather than for its on-site resources and services. # Information Control: This is the area in greatest need of attention. While it ranked highest in importance for all user groups by a wide margin, Queen's performed poorly in this category. Overall, Queen's ranked far below both the ARL average and the top three Canadian scores. However, the major dissatisfaction was concentrated in the humanities/social sciences (Stauffer primary users) and the health sciences (Bracken primary users) where the overall rating of perceived service quality ranked below the minimum expected service rating. Primary users of the Education, Engineering/Science and Law libraries rated this service dimension higher than the ARL average. The great success of the Canadian National Site License Program (CNSLP) is reflected in the high overall rating generated by Engineering/Science Library users. The low ratings from the humanities and social sciences are supported by respondents' comments and are generally consistent with other ARL participants.

Analysis of Lipoprotein(a) Catabolism

Elevated plasma concentrations of lipoprotein(a) [Lp(a)] have been identified as an independent risk factor for vascular diseases including coronary heart disease and stroke. In the current study, we have examined the binding and degradation of recombinant forms of apolipoprotein(a) [r-apo(a)], the unique kringle-containing moiety of Lp(a), using a cultured cell model. We found that the incubation of human hepatoma (HepG2) cells with an iodinated 17 kringle-containing (17K) recombinant form of apo(a) resulted in a two-component binding system characterized by a high affinity (Kd = 12 nM), low capacity binding site, and a low affinity (Kd = 249 nM), high capacity binding site. We subsequently determined that the high affinity binding site on HepG2 cells corresponds to the LDL receptor. In the HepG2 cell model, association of apo(a) with the LDL receptor was shown to be dependent on the formation of Lp(a) particles from endogenous LDL. Using an apo(a) mutant incapable of binding to the high affinity site through its inability to form Lp(a) particles (17KΔLBS7,8), we further demonstrated that the LDL receptor does not participate in Lp(a) catabolism. The low affinity binding component observed on HepG2 cells, familial hypercholesterolemia (FH) fibroblasts and human embryonic kidney (HEK) 293 cells may correspond to a member(s) of the plasminogen receptor family, as binding to this site(s) was decreased by the addition of the lysine analogue epsilon-aminocaproic acid. The lysine-dependent nature of the low affinity binding site was further confirmed in HepG2 binding studies utilizing r-apo(a) species with impaired lysine binding ability. We observed a reduction maximum binding capacity for 17K r-apo(a) variants lacking the strong lysine binding site (LBS) in kringle IV type 10 (17KΔAsp) and the very weak LBS in kringle V (17KΔV). Degradation of Lp(a)/apo(a) was found to be mediated exclusively by the low affinity component on both HepG2 cells and FH fibroblasts. Fluorescence confocal microscopy, using the 17K r-apo(a) variant fused to green fluorescent protein, further confirmed that degradation by the low affinity component on HepG2 cells does not proceed by the activity of cellular lysosomes. Taken together, these data suggest a potentially significant route for Lp(a)/apo(a) clearance in vivo.