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Biology subjects

Xu, J. C.

Publications and source records attributed to Xu, J. C..

2 recordsLinked to original sources

Injury risk functions for the four primary knee ligaments

The purpose of this study was to develop Injury Risk Functions (IRFs) for the Anterior- and Posterior Cruciate Ligament (ACL and PCL, respectively) and the Medial- and Lateral Collateral Ligament (MCL and LCL, respectively) in the knee joint. The IRFs were based on Post-Mortem Human Subject (PMHS) tensile failure strains of either Bone-Ligament-Bone (BLB) or dissected LIGament (LIG) preparations. Due to insufficient sample sizes of the experimental data points available in the current literature, statistically-generated failure strains (virtual values) based on the reported mean- and standard deviation were used to accommodate for the unprovided specimen-specific results. All virtual and specimen-specific values were then categorized into groups of static and dynamic rates, respectively, and tested for the best fitting theoretical distribution to derive a ligament IRF. Ten IRFs were derived (3 for ACL, 2 for PCL, 2 for MCL and 3 for LCL). These IRFs are, to the best of the authors knowledge, the first attempt of knee ligament injury prediction tools based on PMHS data. For future improvements of the knee ligament IRFs, upcoming experiments need comparable testing and strain measurements. More emphasis on a clear definition of failure and transparent reporting of each specimen-specific result is necessary.

bioengineering↗

Ca2+-dependent liquid-liquid phase separation underlies intracellular Ca2+ stores.

Endoplasmic/sarcoplasmic reticulum Ca2+ stores are essential to myriad cellular processes, however, the structure of these stores is largely unknown and existing models do not address all literature observations. We investigate CASQ1 - the major Ca2+ binding protein of skeletal muscle - and discover Ca2+-dependent liquid-liquid phase separation activity. The intrinsic disorder of CASQ1 underlies this activity and is regulated via phosphorylation by the secretory pathway kinase FAM20C. This divalent cation driven condensation demonstrates liquid-liquid phase separation occurs within the endoplasmic/sarcoplasmic reticulum, mechanistically explains efficient Ca2+ buffering and storage, and represents a largely unexplored mechanism of divalent-cation driven protein association.

biochemistry↗