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1.
Sci Rep ; 13(1): 1849, 2023 02 01.
Artigo em Inglês | MEDLINE | ID: mdl-36725891

RESUMO

To evaluate the radiological differences between diffuse idiopathic skeletal hyperostosis (DISH) and ankylosing spondylitis (AS) using whole spine computed tomography (CT), including the spine and sacroiliac joint (SIJ). The ossification and bridging of spinal ligament and fusion of the facet joint and SIJ were evaluated in 111 patients who were diagnosed with DISH and 27 patients with AS on the whole spine CT. The number of anterior bridging and shape of bridging (candle-wax-type/ smooth-type) were also evaluated. We further evaluated patients with DISH and AS by matching their age and sex. Complete SIJ fusion was more common in AS, whereas anterior and posterior bony bridging around SIJ was more common in DISH. However, 63% of patients with DISH had a partial or complete fusion. In spinal anterior bony bridging, the majority of patients with AS had the smooth-type, whereas those with DISH had the candle-wax-type. However, some of the patients with DISH (11%) had smooth-type. Intervertebral facet joint fusion is more common in AS. The number of anterior spinal bony bridging was greater in AS than in DISH, especially in the lumbar spine. These results are useful in differentiating DISH from AS and should therefore be considered when making a diagnosis.


Assuntos
Hiperostose Esquelética Difusa Idiopática , Espondilite Anquilosante , Humanos , Hiperostose Esquelética Difusa Idiopática/diagnóstico por imagem , Espondilite Anquilosante/diagnóstico por imagem , Articulação Sacroilíaca/diagnóstico por imagem , Tomografia Computadorizada por Raios X/métodos , Vértebras Lombares/diagnóstico por imagem
2.
Spine J ; 22(6): 934-940, 2022 06.
Artigo em Inglês | MEDLINE | ID: mdl-35017056

RESUMO

BACKGROUND CONTEXT: Its rare prevalence and subtle radiological changes often lead to difficulties in diagnosing cervical ossification of the posterior longitudinal ligament (OPLL) on plain radiographs. However, OPLL progression may lead to trauma-induced spinal cord injury, resulting in severe paralysis. To address the difficulties in diagnosis, a deep learning approach using a convolutional neural network (CNN) was applied. PURPOSE: The aim of our research was to evaluate the performance of a CNN model for diagnosing cervical OPLL. STUDY DESIGN AND SETTING: Diagnostic image study. PATIENT SAMPLE: This study included 50 patients with cervical OPLL, and 50 control patients with plain radiographs. OUTCOME MEASURES: For the CNN model performance evaluation, we calculated the area under the receiver operating characteristic curve (AUC). We also compared the sensitivity, specificity, and accuracy of the diagnosis by the CNN with those of general orthopedic surgeons and spine specialists. METHODS: Computed tomography was used as the gold standard for diagnosis. Radiographs of the cervical spine in neutral, flexion, and extension positions were used for training and validation of the CNN model. We used the deep learning PyTorch framework to construct the CNN architecture. RESULTS: The accuracy of the CNN model was 90% (18/20), with a sensitivity and specificity of 80% and 100%, respectively. In contrast, the mean accuracy of orthopedic surgeons was 70%, with a sensitivity and specificity of 73% (SD: 0.12) and 67% (SD: 0.17), respectively. The mean accuracy of the spine surgeons was 75%, with a sensitivity and specificity of 80% (SD: 0.08) and 70% (SD: 0.08), respectively. The AUC of the CNN model based on the radiographs was 0.924. CONCLUSIONS: The CNN model had successful diagnostic accuracy and sufficient specificity in the diagnosis of OPLL.


Assuntos
Ligamentos Longitudinais , Ossificação do Ligamento Longitudinal Posterior , Vértebras Cervicais/diagnóstico por imagem , Humanos , Redes Neurais de Computação , Ossificação do Ligamento Longitudinal Posterior/diagnóstico por imagem , Osteogênese , Projetos Piloto
3.
Int J Biochem Cell Biol ; 34(10): 1221-9, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12127572

RESUMO

Arginine kinases (AKs) isolated from the adductor muscle of the clams Solen strictus and Corbicula japonica have relative molecular masses of 80 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in contrast to the 40 kDa AKs found in Mollusca and Arthropoda. The cDNAs encoding Solen and Corbicula AKs have open reading frames of 2175 nucleotides (724 amino acid protein) and 2172 nucleotides (723 amino acid protein), respectively. The amino acid sequence clearly indicates that Solen and Corbicula AKs have a two-domain structure: the first-domain includes residues 1-363 and the second-domain includes residue 364 to the end. There is approximately 60% inter-domain amino acid identity. It is clear that gene-duplication and subsequent fusion occurred in the immediate ancestor of the clams Solen, Corbicula, and Pseudocardium. During substrate binding, it is proposed that AK undergoes a substrate-induced conformational change and that the hydrogen bond between D(62) and R(193) stabilizes the substrate-bound structure. However, in Solen and Corbicula two-domain AKs, D(62) is replaced by a G, and R(193) by A, S, or D. Consequently, the two-domain AKs can not form the stabilizing hydrogen bond. Nevertheless, the enzyme activity of Corbicula AK is comparable to those of other molluscan 40 kDa AKs. We assumed that the substrate-bound structure of the two-domain AK is stabilized not by the hydrogen bond between D(62) and R(193) but by the bond between H(60) and D(197), characteristic of the unusual two-domain AKs. This explains why D(62) and R(193), which remain highly conserved in other AKs, have undergone amino acid replacements in Solen and Corbicula AKs.


Assuntos
Arginina Quinase/metabolismo , Bivalves/enzimologia , Sequência de Aminoácidos , Substituição de Aminoácidos , Animais , Arginina Quinase/química , Arginina Quinase/classificação , Arginina Quinase/genética , Sequência de Bases , Primers do DNA , DNA Complementar , Eletroforese em Gel de Poliacrilamida , Dados de Sequência Molecular , Filogenia , Homologia de Sequência de Aminoácidos
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