TISSUE ENZYME ACTIVITIES IN KEMP'S RIDLEY TURTLES (LEPIDOCHELYS KEMPII).

This study determined the tissue distribution and activities of eight enzymes in 13 juvenile Kemp's ridley turtles (Lepidochelys kempii) that died after stranding. Samples from the liver, kidney, skeletal muscle, cardiac muscle, pancreas, lung, small intestine, and spleen were evaluated for activities of alanine aminotransferase (ALT), alkaline phosphatase (ALP), amylase, aspartate aminotransferase (AST), creatine kinase (CK), γ-glutamyl transferase (GGT), lactate dehydrogenase (LDH), and lipase. AST, CK, and LDH activities were highest in cardiac and skeletal muscle but were also found in all other tissues.

Atypical nodular astrocytosis in simian immunodeficiency virus-infected rhesus macaques (Macaca mulatta).

Background: Simian immunodeficiency virus (SIV), a model for HIV pathogenesis, is associated with neuropathology.

Methods: Five SIV-infected animals were selected following a database search of 1206 SIV-infected animals for nodular or astrocytic lesions. Two of five had neurologic dysfunction, and 3 of 5 were incidental findings.

Prolactin prevents hepatocellular carcinoma by restricting innate immune activation of c-Myc in mice.

Women are more resistant to hepatocellular carcinoma (HCC) than men despite equal exposure to major risk factors, such as hepatitis B or C virus infection. Female resistance is hormone-dependent, as evidenced by the sharp increase in HCC incidence in postmenopausal women who do not take hormone replacement therapy. In rodent models sex-dimorphic HCC phenotypes are pituitary-dependent, suggesting that sex hormones act via the gonadal-hypophyseal axis.

A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes.

LIN-2/7 (L27) domains are protein interaction modules that preferentially hetero-oligomerize, a property critical for their function in directing specific assembly of supramolecular signaling complexes at synapses and other polarized cell-cell junctions. We have solved the solution structure of the heterodimer composed of the L27 domains from LIN-2 and LIN-7. Comparison of this structure with other L27 domain structures has allowed us to formulate a general model for why most L27 domains form an obligate heterodimer complex.