Menkes' disease is an X-linked recessive disorder charaaerized by accumulation of copper in various organs and cells, such as the intestine, kidney, and cultured fibroblasts. Light and electron microscopic localization of Cu was investigated in the intestine and kidney ofmacular mice, an animal model of Menkes' disease, by a modified dide-silver method. Cu was accumulated in the cytoplasm of the absorptive epithelial cells, the vascular endothelium, and secretory granules of the Paneth cells. In kidney the distal tubule cells and glomeruli of both macular and control mice stained faintly, whereas the organelle-free cytoplasm in the proximal tubule

Vascular endothelial growth factor (VEGF) is a glycoprotein that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. We report that infiltrating polymorphonuclear leukocytes in an incision wound in rat skin express VEGF from 1 day after the injury, as shown by immunohistochemistry. VEGF is also present in macrophages, fibroblast-like cells, and endothelial cells 3 and 7 days after the injury. mRNA for VEGF is statistically significantly increased in the wound area in the tissue 1 day after the skin incision compared with 3 and 7 days after the incision. The VEGF protein content in the wound tissue is statistically significantly higher in the wound than in control skin at 1 and 3 days after skin incision. Our results indicate that VEGF is produced by inflammatory cells to induce vascularization in the early stage of the wound healing process.

Human immunodeficiency virus type 1 (HIV-1) strain LAV-1 (HIV-1 LAV-1 ) particles were collected by ultracentrifugation, treated with subtilisin, and then purified by Sepharose CL-4B column chromatography to remove microvesicles. The lysate of the purified HIV-1 LAV-1 particles was subjected to two-dimensional (2D) gel electrophoresis and stained. The 2D gel electrophoresis image suggested that 24 proteins can be identified inside the virion. Furthermore, the stained protein spots were excised and digested with trypsin. The resulting peptide fragments were characterized by matrix-assisted laser desorption ionization-time of flight mass spectrometry. Peptide mass fingerprinting data suggested that two isoforms of cyclophilin A (CyPA), one with an isoelectric point (pI) of 6.40 and one with a pI of 6.53, are inside the viral membrane; that another isoform, with a pI of 6.88, is outside the viral membrane; and that the CyPA isoform with a pI of 6.53 is N acetylated. The mechanisms that permit the redistribution of CyPA on the viral surface have not yet been clarified, but it is surmised that the CyPA isoform with a pI of 6.88 may play a critical role in the attachment of virions to the surface of target cells and that both CyPA isoforms with pIs of 6.40 and 6.53 may regulate the conformation of the HIV-1 capsid protein.

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