In modern optics, particular interest is devoted to the phase singularities that yield complicated and twisted phase structures by photons carrying optical angular momentum.In this paper, the traditional M-line method...In modern optics, particular interest is devoted to the phase singularities that yield complicated and twisted phase structures by photons carrying optical angular momentum.In this paper, the traditional M-line method is applied to a vortex beam(VB) by a symmetric metal cladding waveguide chip, which can host numerous oscillating guided modes via free space coupling.These ultrahigh-order modes(UOMs) result in high angular resolution due to the high finesse of the resonant chip.Experiments show that the reflected pattern of a VB can be divided into a series of inner and outer rings, whilst both of them are highly distorted by the M-lines due to the UOMs’ leakage.Taking the distribution of the energy flux into account, a simple ray-optics-based model is proposed to simulate the reflected pattern by calculating the local incident angle over the cross section of the beam.The theoretical simulations fit well with the experimental results, and the proposed scheme may enable new applications in imaging and sensing of complicated phase structures.展开更多
Myofibrillogenesis, the process of sarcomere formation, requires close interactions of sarcomeric proteins and various components of sarcomere structures. The myosin thick filaments and M-lines are two key components ...Myofibrillogenesis, the process of sarcomere formation, requires close interactions of sarcomeric proteins and various components of sarcomere structures. The myosin thick filaments and M-lines are two key components of the sarcomere. It has been suggested that myomesin proteins of M-lines interact with myosin and titin proteins and keep the thick and titin filaments in order. However, the function of myomesin in myofibrillogenesis and sarcomere organization remained largely enigmatic. No knockout or knockdown animal models have been reported to elucidate the role of myomesin in sarcomere organization in vivo. In this study, by using the gene-specific knockdown approach in zebrafish embryos, we carded out a loss-of-function analysis of myomesin-3 and slow myosin heavy chain 1 （smyhcl） expressed specifically in slow muscles. We demonstrated that knockdown of smyhcl abolished the sarcomeric localization of myomesin-3 in slow muscles. In contrast, loss of myomesin-3 had no effect on the sarcomeric organization of thick and thin filaments as well as M- and Z-line structures. Together, these studies indicate that myosin thick filaments are required for M-line organization and M-line localization of myomesin-3. In contrast, myomesin-3 is dispensable for sarcomere organization in slow muscles.展开更多
基金supported by the Fundamental Research Funds for the Central Universities of China (No.2017B14914)Postgraduate Research&Practice Innovation Program of Jiangsu Province (Nos.B200203143 and KYCX200433)+1 种基金Opening Funding of Hunan Provincial Key Laboratory of High Energy Laser Technology (No.GNJGJS07)National Natural Science Foundation of China (No.11874140)。
文摘In modern optics, particular interest is devoted to the phase singularities that yield complicated and twisted phase structures by photons carrying optical angular momentum.In this paper, the traditional M-line method is applied to a vortex beam(VB) by a symmetric metal cladding waveguide chip, which can host numerous oscillating guided modes via free space coupling.These ultrahigh-order modes(UOMs) result in high angular resolution due to the high finesse of the resonant chip.Experiments show that the reflected pattern of a VB can be divided into a series of inner and outer rings, whilst both of them are highly distorted by the M-lines due to the UOMs’ leakage.Taking the distribution of the energy flux into account, a simple ray-optics-based model is proposed to simulate the reflected pattern by calculating the local incident angle over the cross section of the beam.The theoretical simulations fit well with the experimental results, and the proposed scheme may enable new applications in imaging and sensing of complicated phase structures.
基金supported by a research grant(MB-8716-08) from United States-Israel Binational Agriculture Research and Development Fund to SJD and a NIH grant(DA14546) to SCELiangyi Xue was supported by a Pao Yu-Kong and Pao Zhao-Long Scholarship for Chinese Scholars Studying Abroad from Ningbo University,China
文摘Myofibrillogenesis, the process of sarcomere formation, requires close interactions of sarcomeric proteins and various components of sarcomere structures. The myosin thick filaments and M-lines are two key components of the sarcomere. It has been suggested that myomesin proteins of M-lines interact with myosin and titin proteins and keep the thick and titin filaments in order. However, the function of myomesin in myofibrillogenesis and sarcomere organization remained largely enigmatic. No knockout or knockdown animal models have been reported to elucidate the role of myomesin in sarcomere organization in vivo. In this study, by using the gene-specific knockdown approach in zebrafish embryos, we carded out a loss-of-function analysis of myomesin-3 and slow myosin heavy chain 1 （smyhcl） expressed specifically in slow muscles. We demonstrated that knockdown of smyhcl abolished the sarcomeric localization of myomesin-3 in slow muscles. In contrast, loss of myomesin-3 had no effect on the sarcomeric organization of thick and thin filaments as well as M- and Z-line structures. Together, these studies indicate that myosin thick filaments are required for M-line organization and M-line localization of myomesin-3. In contrast, myomesin-3 is dispensable for sarcomere organization in slow muscles.
