PubMed · 13867244
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L E BENITEZ, G A LISTA, M S BRAILE, R BRAILE. 1961-08-11. [Macroglobulinemic hyperproteinemia].. https://pubmed.ncbi.nlm.nih.gov/13867244/
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Protein Z, a vitamin K-dependent plasma protein, has been detected for the first time in a renal calculus along with osteopontin and prothrombin. The renal calculus was obtained from a hyperuricemic patient. Following two-dimensional polyacrylamide gel electrophoresis, the calculus was analyzed with the use of liquid chromatography mass spectrometry (LC-MS). The spectrometer was equipped with a nanoelectrospray interface and an ion trap. Four peptides were determined from a protein in the calculus through LC-MS/MS analysis. Tandem mass spectrum database matching tools were used to identify the protein as protein Z. Authentic protein Z was also analyzed using the same method, and all four peptides determined in the calculus were similarly identified. Whereas protein Z has been reported to be one of the vitamin K-dependent calcium-binding proteins, its role has not been well established. The fact that protein Z exists in a renal calculus composed of calcium oxalate will be beneficial in any future investigations into its role in the body.
Targeted photodynamic therapy (PDT) offers the opportunity of enhancing photodynamic efficiency by directly targeting diseased cells and tissues. While antibody-conjugates have received the most attention, cellular transformations offer numerous other potent targets to exploit during the delivery of photosensitizers (PSs) for PDT. Alterations in receptor expression, increased levels of specific cell surface membrane lipids and proteins as well as changes in the cellular microenvironment all occur in diseased cells. Along with other biochemical and physiological changes that occur during diseased and malignant cell transformation, these factors have been utilized in order to improve the efficacy of PDT. Attempts have been made to either increase the uptake of the dye by the target cells and tissues or to improve subcellular localization so as to deliver the dye to photosensitive sites within the cells. This review discusses various PS bioconjugates that utilize these factors and summarizes the results obtained to date.
The human endothelial cell plasma membrane harbors two subdomains of similar lipid composition, caveolae and rafts, both crucially involved in various essential cellular processes like transcytosis, signal transduction and cholesterol homeostasis. Caveolin-enriched membranes, isolated by either cationic silica or buoyant density methods, were explored by comparing large series of two-dimensional (2-D) maps and subsequent identification of over 100 protein spots by matrix-assisted laser desorption/ionization (MALDI) peptide mass fingerprinting. Improved representation and identification of membrane proteins and valuable information on various post-translational modifications was achieved by the presented optimized procedures for solubilization, destaining and database searching/computing. Whereas the cationic silica purification yielded predominantly known endoplasmic reticulum residents, the cold-detergent method yielded a large number of known caveolae residents, including caveolin-1. Thus, a large part of this subproteome was established, including known (trans-)membrane, signal transduction and glycosyl phosphatidylinositol (GPI)-anchored proteins. Several predicted proteins from the human genome were isolated for the first time from biological samples, including SGRP58, SLP-2, C8ORF2, and XRP-2. These findings and various optimized procedures can serve as a reference to study the differential composition of endothelial cell caveolae and rafts, known to be involved in pathologies like cancer and cardiovascular disease.