345 research outputs found

    Injury Rates During Water-Based Wilderness Recreation

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    This study came about after the author approached several people in the wilderness-recreation field about their risk-management practices, especially those related to training people who lead trips involving water exposure. The author was surprised that no widely accepted standards exist for training trip leaders or for the skills they need to deal with cases of water emergency. Some people even speculated that injury rates would increase if more water-safety training were conducted because injury rates during land-based activities were assumed to be greater. Although it was outside the scope of this effort to test all current opinions about wilderness water safety held by every practitioner in the field, the author hopes that this study will initiate more conversation about a topic that has not gotten much attention. The purpose of the study was to compare injury rates between water-based wilderness recreation and other backcountry activities and investigate whether more needs to be done to reduce the probability of injury during water-related backcountry activities

    The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells

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    cAMP-dependent protein kinase has a central role in the control of mammalian sperm capacitation and motility. Previous protein biochemical studies indicated that the only cAMP-dependent protein kinase catalytic subunit (C) in ovine sperm is an unusual isoform, termed C(s), whose amino terminus differs from those of published C isoforms of other species. Isolation and sequencing of cDNA clones encoding ovine C(s) and Calpha1 (the predominant somatic isoform) now reveal that C(s) is the product of an alternative transcript of the Calpha gene. C(s) cDNA clones from murine and human testes also were isolated and sequenced, indicating that C(s) is of ancient origin and widespread in mammals. In the mouse, C(s) transcripts were detected only in testis and not in any other tissue examined, including ciliated tissues and ovaries. Finally, immunohistochemistry of the testis shows that C(s) first appears in pachytene spermatocytes. This is the first demonstration of a cell type-specific expression for any C isoform. The conservation of C(s) throughout mammalian evolution suggests that the unique structure of C(s) is important in the subunit\u27s localization or function within the sperm

    A FAP46 Mutant Provides New Insights into the Function and Assembly of the C1d Complex of the Ciliary Central Apparatus

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    Virtually all motile eukaryotic cilia and flagella have a \u279+2\u27 axoneme in which nine doublet microtubules surround two singlet microtubules. Associated with the central pair of microtubules are protein complexes that form at least seven biochemically and structurally distinct central pair projections. Analysis of mutants lacking specific projections has indicated that each may play a unique role in the control of flagellar motility. One of these is the C1d projection previously shown to contain the proteins FAP54, FAP46, FAP74 and FAP221/Pcdp1, which exhibits Ca(2+)-sensitive calmodulin binding. Here we report the isolation and characterization of a Chlamydomonas reinhardtii null mutant for FAP46. This mutant, fap46-1, lacks the C1d projection and has impaired motility, confirming the importance of this projection for normal flagellar movement. Those cells that are motile have severe defects in phototaxis and the photoshock response, underscoring a role for the C1d projection in Ca(2+)-mediated flagellar behavior. The data also reveal for the first time that the C1d projection is involved in the control of interdoublet sliding velocity. Our studies further identify a novel C1d subunit that we term C1d-87, give new insight into relationships between the C1d subunits, and provide evidence for multiple sites of calmodulin interaction within the C1d projection. These results represent significant advances in our understanding of an important but little studied axonemal structure
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