There was a significant increase in the number of BAL lymphocytes in the NK cell recipients vs. saline control, which likely reflects the added bulk of NK cells to the recruited population in the airways. Adoptively transferred NK cells did not protect against lung fibrosis in the bleomycin model; if anything, there was a trend for increased collagen deposition in the lungs in the NK cell recipient mice. Thus our data suggest that NK cells are dispensable for the development of BIPF and are unlikely to play a protective role in regulating lung fibrosis. Finally, NK cell depletion strategies have been proposed to inhibit persistent viral infection as well as to promote graft vs. tumor responses following allogeneic bone marrow cell transplantation. Our data indicate that such strategies would not contribute to the development or exacerbation of pulmonary fibrosis. Mutations in the genes PDE6A, PDE6B, and PDE6G, encoding for the a-, b- and c-subunits of PDE6 respectively, cause autosomal recessive retinitis pigmentosa, a degenerative retinopathy. However, one single mutation in PDE6B, the substitution p.His258Asn, has been observed in the adCSNB condition. Night blindness is an early symptom common to RP and CSNB resulting from functional dysfunction of rod photoreceptors. The loss of rod photoreceptor sensitivity is non-progressive in the CSNB condition whereas the rod photoreceptors death is observed simultaneously with the progressive impairment of the peripheral day vision in the RP condition. Galectins are low molecular weight, calcium-independent, bgalactoside- binding lectins. Galectin-3 is a multi-domain molecule which includes an N-terminal proline-rich domain and a C-terminal carbohydrate recognition domain essential for binding simple b-galactosides such as lactosamine and Galb1- 4GlcNAc; and for higher affinity binding to polylactosamine RS 25344 hydrochloride chains. Galectin-3 plays a key role in several intracellular physiological and pathological TC 1 processes including proliferation and apoptosis, via carbohydrate-independent mechanisms. In addition, galectin-3 is involved in modulation of cell-cell interactions and inflammation, predominately through extracellular carbohydrate binding functions. In the kidney, galectin-3 is strongly expressed in the ureteric bud and its derivatives, the collecting ducts, in normal development and the mature organ. Lower levels are also sometimes observed in mature tubules but the lectin is expressed in a more widespread distribution in models of acute kidney damage such as ischemia-reperfusion injury or high-dose folic acid treatment.