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As part of the process of developing a Clinical Practice Guideline (CPG) on cervical spine manipulation (CSM), a working group sent out an 82-item postal survey to 150 randomly selected Ontario physiotherapists (PTs) who perform spinal manipulation, to collect information on the socio-demographics, practices, opinions of risk, and attitudes towards CPGs of these PTs (n=118; response rate=79%). Of the 118 respondents who performed spinal manipulation, 41 performed CSM. Respondents strongly agreed with three out of six indications listed in the survey for applying CSM: segmental fixation, stiff but stable joint, internal derangement (over 70%). Respondents also strongly agreed (over 88%) that all screening tests listed in the survey should be performed prior to applying CSM: tests for irritability, stability, vascular and neurological systems. Respondents rated patient education, other manual therapy, and exercise as the most common adjuncts to CSM (over 88%). Respondents reported seeing mild complications or side effects only rarely following the application of CSM. Fourteen percent of respondents reported having a written CSM policy or CPG on CSM in their work setting. Feedback from this survey will be used in developing a CSM CPG. A future survey will evaluate changes in clinical practice and in attitudes toward CPGs some time after the dissemination of the CSM CPG.

We recently observed that specific inhibitors of post-proline cleaving aminodipeptidases cause apoptosis in quiescent lymphocytes in a process independent of CD26/dipeptidyl peptidase IV. These results led to the isolation and cloning of a new protease that we have termed quiescent cell proline dipeptidase (QPP). QPP activity was purified from CD26(-) Jurkat T cells. The protein was identified by labeling with [(3)H]diisopropylfluorophosphate and subjected to tryptic digestion and partial amino acid sequencing. The peptide sequences were used to identify expressed sequence tag clones. The cDNA of QPP contains an open reading frame of 1476 base pairs, coding for a protein of 492 amino acids. The amino acid sequence of QPP reveals similarity with prolylcarboxypeptidase. The putative active site residues serine, aspartic acid, and histidine of QPP show an ordering of the catalytic triad similar to that seen in the post-proline cleaving exopeptidases prolylcarboxypeptidase and CD26/dipeptidyl peptidase IV. The post-proline cleaving activity of QPP has an unusually broad pH range in that it is able to cleave substrate molecules at acidic pH as well as at neutral pH. QPP has also been detected in nonlymphocytic cell lines, indicating that this enzyme activity may play an important role in other tissues as well.