β-thymosins and hemocyte homeostasis in a crustacean.

Thymosin proteins are well known for their actin-binding activity. Thymosin beta 4 (Tβ4) has been associated with biological activities in tissue repair and cell migration via interaction with ATP-synthase in vertebrates, while the information of similar thymosin functions in invertebrates is limited. We have shown previously that ATP-synthase is present on the surface of crayfish hematopoietic tissue (HPT) cells, and that astakine 1 (Ast1, an invertebrate cytokine) was found to interact with this β-subunit of ATP synthase.

Astakine 2--the dark knight linking melatonin to circadian regulation in crustaceans.

Daily, circadian rhythms influence essentially all living organisms and affect many physiological processes from sleep and nutrition to immunity. This ability to respond to environmental daily rhythms has been conserved along evolution, and it is found among species from bacteria to mammals. The hematopoietic process of the crayfish Pacifastacus leniusculus is under circadian control and is tightly regulated by astakines, a new family of cytokines sharing a prokineticin (PROK) domain.

Receptor for Activated C Kinase-1 protein from Penaeus monodon (Pm-RACK1) participates in the shrimp antioxidant response.

Cellular oxidative stress responses are caused in many ways, but especially by disease and environmental stress. After the initial burst of reactive oxygen species (ROS), the effective elimination of ROS is crucial for the survival of organisms and is mediated by antioxidant defense mechanisms. In this paper, we investigate the possible antioxidant function of Penaeus monodon Receptor for Activated C Kinase-1 (Pm-RACK1).

Identification of a receptor for activated protein kinase C1 (Pm-RACK1), a cellular gene product from black tiger shrimp (Penaeus monodon) interacts with a protein, VP9 from the white spot syndrome virus.

A gene encoding a receptor for activated protein kinase C1 homolog has been isolated from the shrimp, Penaeus monodon (Pm-RACK1). The full length Pm-RACK1 cDNA has 957 bp, and an open reading frame encoding a protein of 318 amino acid residues. The protein contains seven WD40 repeats and shares approximately 78% identity with vertebrate RACK1.