Diversity and distribution of air-breathing sea slug genus Fleming, 1822 (Gastropoda: Onchidiidae) in southern Japanese waters.

Species of the genus Fleming, 1822, are air-breathing onchidiid sea slugs that inhabit intertidal reef flats of temperate to tropical zones. In the Ryukyu Islands of southern subtropical Japan, species are a traditional food source for local people. To date, there have been three species recorded around Okinawajima Island; and , along with recently described , which was described as possibly endemic to Okinawajima Island.

Serum antibodies to huntingtin interacting protein-1: a new blood test for prostate cancer.

Huntingtin-interacting protein 1 (HIP1) is frequently overexpressed in prostate cancer. HIP1 is a clathrin-binding protein involved in growth factor receptor trafficking that transforms fibroblasts by prolonging the half-life of growth factor receptors. In addition to human cancers, HIP1 is also overexpressed in prostate tumors from the transgenic adenocarcinoma of the mouse prostate (TRAMP) mouse model.

Effect of sodium nitroprusside on ischemia-reperfusion injuries of the rat liver.

Background/aims: The role of NO (nitric oxide) in liver ischemia-reperfusion injury remains controversial, therefore the effect of sodium nitroprusside (SNP), as NO donor on ischemia-reperfusion injuries of the rat liver was studied.

Methodology: Warm ischemia (68% of total liver) of the rat liver was induced for 30 min, followed by reperfusion for 60 min. A dose of 1 or 10 microg/kg/min SNP were continuously administered during the reperfusion period.

Hip1-related mutant mice grow and develop normally but have accelerated spinal abnormalities and dwarfism in the absence of HIP1.

In mice and humans, there are two known members of the Huntingtin interacting protein 1 (HIP1) family, HIP1 and HIP1-related (HIP1r). Based on structural and functional data, these proteins participate in the clathrin trafficking network. The inactivation of Hip1 in mice leads to spinal, hematopoietic, and testicular defects.

HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains.

Huntingtin-interacting protein 1-related (HIP1r) is the only known mammalian relative of huntingtin-interacting protein 1 (HIP1), a protein that transforms fibroblasts via undefined mechanisms. Here we demonstrate that both HIP1r and HIP1 bind inositol lipids via their epsin N-terminal homology (ENTH) domains. In contrast to other ENTH domain-containing proteins, lipid binding is preferential to the 3-phosphate-containing inositol lipids, phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 3,5-bisphosphate.