News - Page 58 of 72 - Yokohama City University

2020-06-17

In vitro production of functional sperm in cultured neonatal mouse testes

Spermatogenesis is one of the most complex and longest processes of sequential cell proliferation and differentiation in the body, taking more than a month from spermatogonial stem cells, through meiosis, to sperm formation1,2. The whole process, therefore, has never been reproduced in vitro in mammals3,4,5, nor in any other species with a very few exceptions in some particular types of fish6,7. Here we show that neonatal mouse testes which contain only gonocytes or primitive spermatogonia as germ cells can produce spermatids and sperm in vitro with serum-free culture media.

2020-06-14

Multisystem Inflammatory Syndrome in Children (MIS-C) with COVID-19: Insights from simultaneous familial Kawasaki Disease cases

Recently, an increasing number of SARS-CoV-2 patients with COVID-19 syndrome, which overlaps with Kawasaki Disease (KD), have been reported, supporting the suggestion that infection is one of the triggers of KD.

2020-06-11

A YCU alumnus, Prof. Dr. S. M. Abe Kawsar, University of Chittagong, published two academic books from a German publisher.

Prof. Dr. Kawsar is an honorable alumnus at Yokohama City University (YCU) who was promoted to a professor position after the completion of the Ph.D. program (2005-2009). In 2014, he was promoted to professor at the University of Chittagong, Bangladesh. Prof. Dr. Kawsar returned to YCU the next year as a visiting professor at the Japan Society for the Promotion of Science. He researched on clinical and diagnostical applications of marine invertebrate lectins and provided special lectures at YCU as visiting professor.

2020-06-09

Adaptive reduction of male gamete number in the selfing plant Arabidopsis thaliana

Ubiquitin-like with PHD and RING finger domains 1 (UHRF1) is an essential factor for the maintenance of mammalian DNA methylation and harbors several reader modules for recognizing epigenetic marks. The tandem Tudor domain (TTD) of UHRF1 has a peptide-binding groove that functions as a binding platform for intra- or intermolecular interactions. Besides the groove interacting with unphosphorylated linker 2 and spacer of UHRF1, it also interacts with di/tri-methylated histone H3 at Lys9 and DNA ligase 1 (LIG1) at Lys126. Here we focus on the phosphorylation of Ser298 in linker 2, which was implied to regulate the ligand-binding property of the TTD.