It is well-recognized that human immunodeficiency virus type-1 (HIV-1) mainly targets CD4 T cells and macrophages. Nonetheless, during the past three decades, a huge number of studies have reported that HIV-1 can directly or indirectly target other cellular components of the immune system including CD8 T cells, B cells, dendritic cells, natural killer cells, and polymorphonuclear neutrophils (PMNs), among others. PMNs are the most abundant leukocytes in the human circulation, and are known to play principal roles in the elimination of invading pathogens, regulating different immune responses, healing of injured tissues, and maintaining mucosal homeostasis. Until recently, little was known about the impact of HIV-1 infection on PMNs as well as the impact of PMNs on HIV-1 disease progression. This is because early studies focused on neutropenia and recurrent microbial infections, particularly, during advanced disease. However, recent studies have extended the investigation area to cover new aspects of the interactions between HIV-1 and PMNs. This review aims to summarize these advances and address the impact of HIV-1 infection on PMNs as well as the impact of PMNs on HIV-1 disease progression to better understand the pathophysiology of HIV-1 infection.

The effect of different concentrations (0, 0.01, 0.1, and 0.5 mg/ml) of plant aqueous extracts on the anti-tumor activity of natural killer (NK) cells isolated from human blood was examined. Plant extracts induced significant enhancement of (26.6-67.7%) of NK cell activity against K562 tumor cells. This increase in NK cell cytotoxicity was found to be due to the enhancement of NK cell production of interferon-gamma (87-337%), and on tumor necrosis factor-alpha (60-200%). Furthermore, the release of both granzyme A and N-acetyl-beta-D-glucosaminidase was increased significantly when compared with controls. Activation of granzyme A and N-acetyl-beta-D-glucosaminidase was clearly observed ranging from 24.2-106.4% to 26.8-110.7%, respectively. Lastly, in the absence of IL-2, plant extracts caused a significant increase in NK-cell-induced cytotoxicity (256%) against K562 tumor cells, and in the presence of IL-2 stimulated cells plant extracts caused an increase in NK cell-cytotoxicity (112%).

The coupling of ellipticine and CI-921, two antineoplastic pharmaceuticals, to polyaldehyde dextran can be carried out under mild reaction conditions with novel acid hydrazides of the parent drugs. The resulting acyl hydrazones resist hydrolytic and enzymatic cleavage and offer a method for drug loading via dextran conjugates to monoclonal antibodies.

Albumin in vitro contains several molecular forms, while in vivo it exists mainly as a monomer with a small fraction of a dimer. The aim of the present work was to detect and estimate albumin forms in fresh blood samples. The available analytical methods at present are inadequate for this purpose. An improved immunoblotting method was used where plasma was subjected to electrophoretic separation on 4-25% gradient polyacrylamide gels followed by immunoblotting on agarose gel containing anti-human albumin. The interference from the huge amount of the monomer in plasma was overcome by cutting the monomer region from the polyacrylamide gel before immunoblotting. After staining of the agarose gel, it revealed the presence of seven stained bands of albumin in addition to the monomer. These bands represent albumin aggregates and complexes of varying molecular masses (112-428 kDa). These albumin forms accounted for 0.7% of the total plasma albumin and their estimated level was 30.7 mg/dL. This study shows that the native albumin in blood has several molecular forms. It is concluded that albumin in healthy human subjects may form association complexes of varying molecular masses with other macromolecules in blood and these complexes are expected to be of physiological relevance.

A simple method is described for electrophoretic desorption of proteins from antigen-antibody complexes, with more than 90 % recovery and without denaturation, after immunosorbent affinity chromatography. Radiolabeled or unlabeled human serum albumin (HSA) and c~-]-antitrypsin (AAT), conjugated to rabbit anti-HSA or anti-AAT polyclonal antisera, respectively, were electrophoretically desorbed from Sepharose 4B. In addition, purification and concentration of the major HSA protein band (monomer) of 68 kD from the other oligomeric protein bands were achieved by use of a two-membrane system in a simple electroelution apparatus. The system consisted of an uppe r cellulose acetate membrane, with pore size 20 nm and separation limit 70 kD, and a lower dialysis cellophane membrane with molecular weight cut-off from 1-50 kD that enables separation according to size. Furthermore, purification of the monomer HSA or AAT from normal human serum was performed with 92 % recovery. Homogeneity was implied by the presence of one band after sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, Western blot, and autoradiography.