The knockout of cytoglobin 1 in zebrafish (Danio rerio) alters lipid metabolism, iron homeostasis and oxidative stress response.

Cytoglobin (Cygb) is an evolutionary ancient heme protein with yet unclear physiological function(s). Mammalian Cygb is ubiquitously expressed in all tissues and is proposed to be involved in reactive oxygen species (ROS) detoxification, nitric oxide (NO) metabolism and lipid-based signaling processes. Loss-of-function studies in mouse associate Cygb with apoptosis, inflammation, fibrosis, cardiovascular dysfunction or oncogenesis.

The More, the Merrier? Multiple Myoglobin Genes in Fish Species, Especially in Gray Bichir (Polypterus senegalus) and Reedfish (Erpetoichthys calabaricus).

The members of the globin superfamily are a classical model system to investigate gene evolution and their fates as well as the diversity of protein function. One of the best-known globins is myoglobin (Mb), which is mainly expressed in heart muscle and transports oxygen from the sarcolemma to the mitochondria. Most vertebrates harbor a single copy of the myoglobin gene, but some fish species have multiple myoglobin genes.

Ecological specialization resulting in restricted gene flow promotes differentiation in door snails.

We tested the hypothesis that ecological specialization that affects dispersal promotes diversification by a comparison of the genetic structure of two sister species of door snails across their broadly overlapping ranges in the Crimean Mountains. The hypothesized effect of ecological specialization on diversification is supported by STRUCTURE analyses that showed that Mentissa gracilicosta that is restricted to limestone rocks, is subdivided into several distinct clusters, whereas all populations of the species adapted to more continuous habitat, the forests-dwelling Mentissa canalifera, were assigned to a single cluster. Furthermore, it is supported by AMOVAs that showed that a larger part of the genetic variation of M.