Effect of an occupation-based cultural heritage intervention in long-term geriatric care: a two-group control study.

OBJECTIVE: We investigated the effectiveness of an occupation-based cultural heritage intervention to facilitate adaptation to relocation into long-term care (LTC) facilities as measured by quality of life, activity engagement, and social participation. METHOD: We used a quasi-experimental nonequivalent control group design with pre- and posttests. Residents receiving the cultural intervention were compared with residents in a typical activity group. Eight sessions, two per week for 4 wk, were facilitated by certified occupational therapy assistants. RESULTS: Twenty-nine participants completed the group sessions. Quality-of-life scores improved significantly over time for both groups. Statistically, a greater percentage of time was spent in discretionary than obligatory time, pretest and posttest, with no significant difference between groups. CONCLUSION: The study demonstrated effectiveness of a structured, occupation-based social group intervention that improved quality of life, an indicator of adaptation. It also provided a description of activity patterns and social participation of LTC residents.

Voices of elders: culture and person factors of residents admitted to long-term care facilities.

PURPOSE: The aim of this study was to investigate person and environment factors of elders that facilitate adaptation to relocation to long-term care skilled nursing facilities. Results represent findings from Phase 1 of three phases of a 2-year study to develop and test a cultural heritage intervention to improve adaptation to nursing home relocation. DESIGN: Qualitative interviews were conducted with 23 newly admitted Caucasians and African Americans residing in skilled nursing facilities. FINDINGS/RESULTS: Themes that emerged include (a) spirituality, death and dying, and philosophy of life; (b) life experiences with change; (c) cultural heritage; (d) health; (e) ethnicity; (f) social support, family and friends; (g) long-term care facility (LTCF) relationships; (h) LTCF system maintenance; and (i) LTCF support of personal growth. Comparison of African Americans and Caucasians showed more similarities than differences between the groups. DISCUSSION: Implications for research, clinical practice, and cultural heritage interventions for LTCF adaptation are discussed.

The effect of patients' race on provider treatment choices in coronary care: a literature review for model development.

This selective literature review provides insight into the depth and breadth of the problem of unequal medical treatment of Blacks compared with Whites, with particular focus on coronary heart disease. Poor health outcomes among Blacks, when compared with Whites, are well documented, and these disparities are linked to lower quality of and less aggressive medical treatment. It is not clear why these disparities in treatment occur. This review provides theoretical frameworks that attempt to explain the effect of race on treatment and presents an analysis of the quality and strength of existing evidence of racial disparity related to coronary care. Based on the review, implications for policy makers and providers are identified.

The Essex-Lopresti injury: More than just a pain in the wrist.

As the scope of plastic surgical practice expands to include disorders of the carpus and wrist, it has become increasingly important for plastic surgeons to understand pathoanatomy that has not traditionally been considered an integral component of training. The Essex-Lopresti injury consists of a radial head fracture with associated injury to the forearm interosseus membrane and longitudinal instability of the distal radioulnar joint. Early recognition of this disorder usually results in a predictable and satisfactory outcome. However, when this disorder is unrecognized, late reconstruction is challenging and unpredictable, and treatment may be misdirected to the wrist alone if the forearm and elbow are not considered as a component of this injury. The present report describes the importance of examining the elbow in all cases of wrist pain. As well, the literature is reviewed regarding the differences in treatment of acute and chronic Essex-Lopresti injuries. As plastic surgeons become more involved in the treatment of wrist injuries, the conscientious practitioner should be aware of more complicated pathology that may present as a seemingly straightforward wrist problem.

The human kallikrein protein 5 (hK5) is enzymatically active, glycosylated and forms complexes with two protease inhibitors in ovarian cancer fluids.

The kallikrein family is a group of 15 serine protease genes clustered on chromosome 19q13.4. Binding of kallikreins to protease inhibitors is an important mechanism for regulating their enzymatic activity and may have potential clinical applications. Human kallikrein gene 5 (KLK5) is a member of this family and encodes for a secreted serine protease (hK5). This kallikrein was shown to be differentially expressed at the mRNA and protein levels in diverse malignancies. Our objective was to study the enzymatic activity and the interaction of recombinant hK5 protein with protease inhibitors. Recombinant hK5 protein was produced in yeast and mammalian expression systems and purified by chromatography. HPLC fractionation, followed by ELISA-type assays, immunoblotting and radiolabeling experiments were performed to detect the possible interactions between hK5 and proteinase inhibitors in serum. Enzymatic deglycosylation was performed to examine the glycosylation pattern of the protein. The enzymatic activity of hK5 was tested using trypsin and chymotrypsin-specific synthetic fluorogenic substrates. In serum and ascites fluid, in addition to the free ( approximately 40 kDa) form, hK5 forms complexes with alpha(1)-antitrypsin and alpha(2)-macroglobulin. These complexes were detected by hybrid ELISA-type assays using hK5-specific coating antibodies and inhibitor detection antibodies. The ability of hK5 to bind to these inhibitors was further verified in vitro. Spiking of serum samples with 125I-labeled hK5 results in the distribution of the protein in two higher molecular mass (bound) forms, in addition to the unbound form. The hK5 mature enzyme is active and shows trypsin, but not chymotrypsin-like, activity. The pro-form of hK5 is not active. Recombinant hK5 shows a higher than predicted molecular mass due to glycosylation. hK5 is partially complexed with alpha(1)-antitrypsin and alpha(2)-macroglobulin in serum and ascites fluid of ovarian cancer patients. The recombinant protein is glycosylated and its mature form shows trypsin-like activity.

Purification of human kallikrein 6 from biological fluids and identification of its complex with alpha(1)-antichymotrypsin.

BACKGROUND: Human kallikrein 6 (hK6) is significantly increased in serum in many patients with ovarian cancer and may have a role in amyloid precursor processing and Alzheimer disease. The forms of hK6 in biological fluids are poorly characterized. METHODS: hK6 protein was immunoaffinity-purified and positively identified by Western blotting, N-terminal sequencing, and mass spectrometry. hK6 in cerebrospinal fluid (CSF), milk, ascites, and serum was size-fractionated by chromatography and then measured by a highly sensitive and specific immunoassay. Hybrid assays were performed to detect the possible interactions between hK6 and proteinase inhibitors in CSF, milk, ascites fluid, and serum. RESULTS: N-Terminal sequencing identified hK6 in the proform in both CSF and milk. hK6 exists in two forms in milk and ascites fluid: a free form with a molecular mass of approximately 25 kDa and a higher molecular mass form. Hybrid sandwich assays (capture antibody for hK6 and detection antibody for inhibitors), utilizing a panel of known serine protease inhibitors, indicated that alpha(1)-antichymotrypsin forms a complex with hK6 in milk and ascites fluid. Only the free form of hK6 was detected in CSF and serum. CONCLUSIONS: hK6 exists mainly as a proenzyme in milk and CSF. A fraction of this enzyme is partially complexed with alpha(1)-antichymotrypsin in milk and ascites fluid of ovarian cancer patients.