Directional Rope Capture Device

The current market for rope capture devices shows a trend of using toothed devices as the method of creating a rope capture system. These systems are effective for a variety of applications but in any scenario in which a high load is encountered there is a large amount of damage done by the teeth to the rope. The objective of this project was to create a rope capture device that did not utilize teeth in order to create a safer loading condition on the rope. The method used for this project was application of equiangular spirals, this is the same method used for climbing cams. A profile was built using a section of a mathematical curve and was imported into a CAD/CAM program in order to be manufactured. Initial calculations showed that a small cam could replace the toothed plates used in commercial devices in order to remove the elements which could damage the sheath of the rope. The results of the project showed a successful application of the mathematical principles in creating a device that would slide up the rope cleanly in one direction but immediately catch in the opposite direction. This proof of concept device demonstrates the working concepts of a camming unit as a replacement of a toothed device

A Novel Mutation in the HSD17B10 Gene of a 10-Year-Old Boy with Refractory Epilepsy, Choreoathetosis and Learning Disability

Hydroxysteroid (17beta) dehydrogenase 10 (HSD10) is a mitochondrial multifunctional enzyme encoded by the HSD17B10 gene. Missense mutations in this gene result in HSD10 deficiency, whereas a silent mutation results in mental retardation, X-linked, syndromic 10 (MRXS10). Here we report a novel missense mutation found in the HSD17B10 gene, namely c.194T\u3eC transition (rs104886492), brought about by the loss of two forked methyl groups of valine 65 in the HSD10 active site. The affected boy, who possesses mutant HSD10 (p.V65A), has a neurological syndrome with metabolic derangements, choreoathetosis, refractory epilepsy and learning disability. He has no history of acute decompensation or metabolic acidosis whereas his urine organic acid profile, showing elevated levels of 2-methyl-3-hydroxybutyrate and tiglylglycine, is characteristic of HSD10 deficiency. His HSD10 activity was much lower than the normal control level, with normal β-ketothiolase activity. The c.194T\u3eC mutation in HSD17B10 can be identified by the restriction fragment polymorphism analysis, thereby facilitating the screening of this novel mutation in individuals with intellectual disability of unknown etiology and their family members much easier. The patient\u27s mother is an asymptomatic carrier, and has a mixed ancestry (Hawaiian, Japanese and Chinese). This demonstrates that HSD10 deficiency patients are not confined to a particular ethnicity although previously reported cases were either Spanish or German descendants

A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory epilepsy, choreoathetosis and learning disability.

Hydroxysteroid (17beta) dehydrogenase 10 (HSD10) is a mitochondrial multifunctional enzyme encoded by the HSD17B10 gene. Missense mutations in this gene result in HSD10 deficiency, whereas a silent mutation results in mental retardation, X-linked, syndromic 10 (MRXS10). Here we report a novel missense mutation found in the HSD17B10 gene, namely c.194T>C transition (rs104886492), brought about by the loss of two forked methyl groups of valine 65 in the HSD10 active site. The affected boy, who possesses mutant HSD10 (p.V65A), has a neurological syndrome with metabolic derangements, choreoathetosis, refractory epilepsy and learning disability. He has no history of acute decompensation or metabolic acidosis whereas his urine organic acid profile, showing elevated levels of 2-methyl-3-hydroxybutyrate and tiglylglycine, is characteristic of HSD10 deficiency. His HSD10 activity was much lower than the normal control level, with normal β-ketothiolase activity. The c.194T>C mutation in HSD17B10 can be identified by the restriction fragment polymorphism analysis, thereby facilitating the screening of this novel mutation in individuals with intellectual disability of unknown etiology and their family members much easier. The patient's mother is an asymptomatic carrier, and has a mixed ancestry (Hawaiian, Japanese and Chinese). This demonstrates that HSD10 deficiency patients are not confined to a particular ethnicity although previously reported cases were either Spanish or German descendants

A Novel Mutation in the HSD17B10 Gene of a 10-Year-Old Boy with Refractory Epilepsy, Choreoathetosis and Learning Disability

Hydroxysteroid (17beta) dehydrogenase 10 (HSD10) is a mitochondrial multifunctional enzyme encoded by the HSD17B10 gene. Missense mutations in this gene result in HSD10 deficiency, whereas a silent mutation results in mental retardation, X-linked, syndromic 10 (MRXS10). Here we report a novel missense mutation found in the HSD17B10 gene, namely c.194T>C transition (rs104886492), brought about by the loss of two forked methyl groups of valine 65 in the HSD10 active site. The affected boy, who possesses mutant HSD10 (p.V65A), has a neurological syndrome with metabolic derangements, choreoathetosis, refractory epilepsy and learning disability. He has no history of acute decompensation or metabolic acidosis whereas his urine organic acid profile, showing elevated levels of 2-methyl-3-hydroxybutyrate and tiglylglycine, is characteristic of HSD10 deficiency. His HSD10 activity was much lower than the normal control level, with normal β-ketothiolase activity. The c.194T>C mutation in HSD17B10 can be identified by the restriction fragment polymorphism analysis, thereby facilitating the screening of this novel mutation in individuals with intellectual disability of unknown etiology and their family members much easier. The patient's mother is an asymptomatic carrier, and has a mixed ancestry (Hawaiian, Japanese and Chinese). This demonstrates that HSD10 deficiency patients are not confined to a particular ethnicity although previously reported cases were either Spanish or German descendants

Activities of mitochondrial respiratory chain enzymes in fibroblasts.

<p>Activities of mitochondrial respiratory chain enzymes in fibroblasts.</p

Comparison of amino acid sequence around valine 65 of HSD10 with those of its othologs in different species.

<p>Residues conserved in all species were bolded. The asterisk * indicates an extremely conserved residue of this NAD⁺-dependent dehydrogenase.</p

Mutation on the <i>HSD17B10</i> gene of patient with a clinical diagnosis of HSD10 deficiency.

<p>Chromatogram of the forward sequence of the <i>HSD17B10</i> gene from the patient showing c.194T>C transition. The nucleotide sequence of intron 2 is indicated by lower case. This mutation resulted in mutant HSD10(p.V65A).</p

Electroencephalography of the affected boy at 10 years of age.

<p>Electroencephalography of the affected boy at 10 years of age.</p

Concentrations of urine organic acids (mmole/mole creatine) at different age.

<p>Concentrations of urine organic acids (mmole/mole creatine) at different age.</p

Detection of the c.194T>C variant in the <i>HSD17B10</i> gene by RFLP analysis.

<p>The pGEM-T Easy vectors harboring the <i>HSD17B10</i> gene cloned from genomic DNA of a normal control [<b>C1–3</b>] (lanes 1–3), the patient's sister [<b>S1–6</b>] (lanes 4–9), the patient [<b>P1–3</b>] (lanes10–12), and the patient's mother [<b>M1–6</b>] (lanes 13–18) were digested by <i>BstE</i>II and then separated on a 1% agarose gel. Amounts of DNA loaded were 1 mg on lanes 1 and 2, 0.75 mg on lanes 3 and 6, and 0.5 mg on all the other lanes. A 2.2 kb fragment (indicated by an arrowhead) results from an allele carrying this variant. For a wild-type allele, this fragment is chopped into two shorter fragments (1.3 kb and 0.9 kb) as indicated by arrows. The vector is in the largest band indicated by an empty arrowhead.</p