Publications by authors named "Kayano Moriyama"
Article Synopsis
- * A study analyzed serum samples from patients with osteoporosis without fractures and those with osteopenia and fragility fractures, identifying six serum proteins that changed similarly between the two groups.
- * One significant protein, ECM1, showed elevated levels in both groups and could potentially indicate the need for treatment; however, further larger studies are required to validate its effectiveness for early intervention.
Physical inactivity associated with gravity unloading, such as microgravity during spaceflight and hindlimb unloading (HU), can cause various physiological changes. In this study, we attempted to identify serum proteins whose levels fluctuated in response to gravity unloading. First, we quantitatively assessed changes in the serum proteome profiles of spaceflight mice using mass spectrometry with data-independent acquisition.
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- The study investigates how spaceflight impacts healthy tissue functions through changes in the serum proteome of six astronauts during a 6-month mission.
- Researchers used data-independent acquisition mass spectrometry (DIA-MS) to identify 624 proteins related to bone metabolism, revealing a decrease in T-scores in dual-energy X-ray scans over time.
- Findings suggest that specific proteins like ALPL, COL1A1, SPP1, and POSTN could serve as indicators of bone metabolism changes in space, advancing our understanding of biological adaptations to long-duration spaceflight.
Article Synopsis
- Gravity impacts the musculoskeletal health of elderly individuals by preventing muscle loss and improving bone density, which enhances quality of life.
- Researchers analyzed the soleus muscle in mice under various gravity conditions, identifying specific proteins (Myl6b, Gpd1, Fbp2, Pvalb, Actn3) that respond to these gravity changes, indicating a shift towards slow-twitch muscle fibers.
- Higher levels of Pvalb were found in the blood of mice and osteoporosis patients with muscle atrophy, suggesting it could be a key marker for evaluating muscle and bone health in seniors.
Article Synopsis
- Astronauts experience significant bone loss in microgravity, but the exact molecular mechanisms behind this are still not fully understood.
- Researchers developed a sensitive mass spectrometry analysis system to study proteomic changes in mouse bones, successfully identifying 40 proteins with varying abundance due to the absence of gravity and 22 proteins unaltered by mechanical stimuli.
- Notably, one protein, SPARCL1, may stimulate bone degradation processes, potentially revealing new insights into bone metabolism and the impact of mechanical forces on bones in space.
Article Synopsis
- * Researchers used a proteomic method called data-independent acquisition mass spectrometry (DIA-MS) to identify 27 serum proteins related to the prognosis of severe COVID-19 cases.
- * Analysis showed that specific proteins might be influenced by cytokine signaling and could help predict patient outcomes, with CHI3L1 and IGFALS identified as potential reliable prognostic markers.
New horny layer marker proteins for evaluating skin condition in atopic dermatitis.
Int Arch Allergy Immunol
September 2009
Background: Atopic dermatitis (AD) has a complicated pathogenesis and its clinical features vary greatly among patients. Although many clinical parameters have been reported, it remains difficult to evaluate AD skin conditions adequately.
Objective: To support better evaluation of AD patients, we attempted to develop a new, objective and noninvasive method that assesses skin condition in AD using biochemical markers in the skin's horny layer (HL).
Herlitz junctional epidermolysis bullosa (H-JEB) is a hereditary bullous disease caused by absent expression of laminin-5, a component of anchoring filaments within the dermal-epidermal basement membrane zone. Affected individuals usually die during the first 1 year of life. We studied an infant with H-JEB who presented with nephrotic syndrome, a previously unreported complication that may contribute to early death in this disease.
View Article and Find Full Text PDFLaminin-6 (LN6) and laminin-5 (LN5), which share the common integrin-binding domain in the laminin alpha3 chain, are thought to cooperatively regulate cellular functions, but the former has poorly been characterized. Human fibrosarcoma HT1080 cells expressing an exogenous alpha3 chain were found to secrete LN6 with the full-length alpha3 chain and a smaller amount of its processed form lacking the carboxyl-terminal G4-5 domain, besides mature LN5 without G4-5 (mat-LN5). We prepared the unprocessed LN6 and mat-LN5, as well as LN6 mutants without G4-5 (LN6DeltaG4-5) or G5 (LN6DeltaG5).
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