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OBJECTIVES: The advancement of laparoscopic surgery has allowed surgeons to see finer anatomical structures during surgery. As a result, several issues have arisen regarding Gerota fascia that cannot be explained by previous interpretations, such as its various forms observed during surgery. To address these issues, we histologically examined the structure of Gerota fascia. METHODS: Specimens for study were prepared from kidneys with Gerota fascia from four cadavers, and the structure was studied histologically. Its thickness and collagen fiber area ratios were measured using ImageJ and compared to those of the epimysium of the rectus abdominis muscle. RESULTS: Connective tissue that appeared to be Gerota fascia was observed in 26 specimens. Histologically, the basic structure of Gerota fascia was a sandwich-like structure with a thin layer of thick, long collagen fibers in the central layer, and small granular collagen fibers scattered at the edges. However, not all areas observed had a similar structure; eight specimens were composed only of small granular collagen fibers. The average thickness of the Gerota fascia was 466 μm, and the area ratio of collagen was 27.1%. In contrast, the epimysium was much thicker than Gerota fascia, and its collagen fibers were much thicker and denser. CONCLUSIONS: Gerota fascia, unlike the epimysium, was a very thin and fragile layer of collagen fibers, and its structure was diverse. This explains why Gerota fascia was observed in various states during surgery. It is important for surgeons to understand the properties of Gerota fascia and to treat it appropriately.

DOI： 10.1111/iju.15596

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The extraperitoneal laparoscopic approach (ELPAN) for para-aortic lymphadenectomy provides excellent visibility of the left side of the aorta, thus facilitating surgery in the retroperitoneal space. This technique is highly complex compared with the transperitoneal approach. In particular, advanced techniques are required to develop an appropriate surgical field in the narrow retroperitoneal space; therefore, surgeons need to undergo a significant amount of training to become competent. A variety of tools are available for surgical training but are limited by their ability to reproduce complex anatomy. Thus, cadavers may represent the most suitable tool for learning this unique technique. The present study describes a surgical training protocol for the ELPAN technique using a Thiel-embalmed human cadaver and provides a step-by-step description of the ELPAN technique performed at Okayama University (Okayama, Japan). A 72-year-old Thiel-embalmed female cadaver was used to develop a protocol for surgical training in the ELPAN technique that effectively reproduced the methodology required in clinical practice. A training method for ELPAN surgery was developed and successfully completed using the Thiel-embalmed cadaver that secured the surgical field in the retroperitoneal space and permitted resection of the lymph nodes. The Thiel-embalmed cadaver tissue possessed excellent properties for surgical training, including color tone, flexibility, and the membrane structure of connective and fat tissues. In addition, this method of fixation preserved stiffness and elasticity of the peritoneum, although large vessels were slightly fragile and poorly extensible. Surgical training using a Thiel-embalmed human cadaver represents a valuable option for learning the ELPAN surgical technique. However, this technique may be unsuitable for training in perivenous manipulation. To the best of our knowledge, this is the first report to describe the use of Thiel-embalmed cadavers as a tool for surgeons to undergo training in the ELPAN technique.

DOI： 10.3892/ol.2024.14422

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BACKGROUND: Increased expression of collagen XV has been reported in hepatocellular carcinogenesis in mice. The aim of this study was to confirm the previous murine findings in human hepatocellular carcinoma (HCC) specimens, along with the histopathological distribution of collagen XV in tumoral tissues. METHODS: Sixty-three primary HCC specimens were examined. Immunostaining of collagen XV and quantitative reverse transcriptional PCR of COL15A1, which encodes collagen XV, were performed. RESULTS: Positive staining of collagen XV was observed in all tumoral regions, regardless of differentiation level or pathological type of HCC, along the sinusoid-like endothelium, whereas collagen XV was not expressed in any non-tumoral region. The intensity score of collagen XV immunostaining and the mRNA value of COL15A1 were significantly correlated. COL15A1 expression in tumors was 3.24-fold higher than in non-tumoral regions. Multivariate analysis showed that COL15A1 expression was significantly higher in the absence of hepatitis virus and moderately differentiated HCC. CONCLUSIONS: COL15A1 mRNA was up-regulated in HCC and collagen XV was expressed along the sinusoid-like endothelium of HCC but not in non-tumoral regions, which implies that collagen XV contributes to the capillarization of HCC.

DOI： 10.1007/s10147-015-0888-2

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Vertebrate collagen types XV and XVIII are broadly distributed basement membrane components, classified into a structurally distinct subgroup called "multiplexin collagens". Mutations in mammalian multiplexins are identified in some degenerative diseases such as Knobloch syndrome 1 (KNO1) or skeletal/cardiac myopathies, however, these progressive properties have not been elucidated. Here we investigated Drosophila mutants of Multiplexin (Mp), the only orthologue of vertebrate collagen types XV and XVIII, to understand the pathogenesis of multiplexin-related diseases. The mp mutants exhibited morphological changes in cardiomyocytes and progressive dysfunction of the skeletal muscles, reminiscent phenotypes observed in Col15a1-null mice. Ultrastructural analysis revealed morphologically altered mitochondria in mutants' indirect flight muscles (IFMs), resulting in severely attenuated ATP production and enhanced reactive oxygen species (ROS) production. In addition, mutants' IFMs exhibited diminished βPS integrin clustering and abolished focal adhesion kinase (FAK) phosphorylation. Furthermore, mutants' defective IFMs are improved by the administrations of cyclosporin A, an inhibitor against mitochondrial permeability transition pore (mPTP) opening or losartan, an angiotensin II type 1 receptor (AT1R) blocker. Thus, our results suggest that Mp modulates mPTP opening and AT1R activity through its binding to integrin and that lack of Mp causes unregulated mPTP opening and AT1R activity, leading to mitochondrial dysfunctions. Hence, our results provide new insights towards the roles of multiplexin collagens in mitochondrial homeostasis and may serve as pharmacological evidences for the potential use of cyclosporin A or losartan for the therapeutic strategies.

DOI： 10.1016/j.biocel.2013.02.001

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J-GLOBAL

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J-GLOBAL

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J-GLOBAL

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J-GLOBAL

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J-GLOBAL

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