Fish-odour syndrome: dealing with offensive body odour.

This article is aimed at nursing professionals who may have been, or may be confronted with, patients who complain of fish-smelling body odour. The individual may be suffering from intermittent symptoms of the fish-odour syndrome. Recent contact with sufferers of such symptoms has highlighted the need to raise awareness among nurses about this syndrome. Sufferers expressed disappointment with regard to the advice they received from primary health-care professionals with respect to their problem. In content, the advice was variable but commonly centred around methods of increasing personal hygiene. Thus, the purpose of this article is to provide factual information about the fish-odour syndrome to increase awareness among nurses who could potentially aid the management of the syndrome and relieve some of the distress of its sufferers.

Characterization and immunolocalization of rat liver annexin VI.

Annexin VI has been purified to homogeneity from rat liver and monospecific antibodies have been produced. The antibodies have been used for immunoblot analysis of rat tissues. Annexin VI is present in most tissues, with particularly high concentrations in liver, spleen, muscle, and intestine. In liver, annexin VI constitutes approximately 0.25% of total cellular protein. Immunohistochemical studies have located annexin VI on plasma membranes of hepatocytes with enhanced concentration on bile canaliculi. Annexin VI binds in a Ca(2+)-dependent manner to a sub-cellular fraction containing membranes. In the presence of physiological concentrations of ATP, the free Ca2+ concentration required for half-maximal binding of annexin VI to membranes is significantly reduced. While annexin VI binds in vitro to membranes in the presence of Ca2+, in rat liver about 31% of the annexin VI is associated with membranes in a Ca(2+)-independent manner and its solubilization requires the presence of Triton X-100. However, studies using Triton X-114 showed no increase in the hydrophobicity of this fraction of the protein compared to the purified EGTA-soluble annexin VI.

The sub-cellular localization of annexin V in cultured chick-embryo fibroblasts.

The Ca(2+)- and phospholipid-binding protein, annexin V, has been shown by an immune assay to represent 0.4% of total cell protein in cultured chick-embryo fibroblasts. Immunofluorescent localization studies indicate that in primary cultures the protein is abundant in the cytoplasm of the cells and also extends into the nucleus. Nuclear staining is no longer detectable, however, in approx. 25% of the cells following sub-culture. Sub-populations of annexin V are associated with cytoskeletal structures and with the inner face of the plasma membrane in a Ca(2+)-independent manner. In addition, we report results indicating the secretion of annexin V from this cell type.

Isolation, characterization and localization of annexin V from chicken liver.

Annexin V has been purified from chicken liver; 40 mg of annexin V was obtained per kg of tissue. In contrast with mammalian liver, very little annexin VI was obtained. Surprisingly, chicken liver annexin V resembles mammalian annexin IV in its M(r) (32,500) and its isoelectric point (5.6), but amino-acid-sequence analysis demonstrates identity with chicken annexin V (anchorin CII). It binds to phospholipids in a Ca(2+)-dependent manner with free-Ca2+ concentrations for half-maximal binding to phosphatidylserine and phosphatidic acid of 10 microM; phosphatidylethanolamine of 32 microM and phosphatidylinositol of 90 microM. No binding to phosphatidylcholine was observed at Ca2+ concentrations up to 300 microM. In isolated liver membranes a significant proportion of annexin V was not extractable with EGTA but could only be extracted with Triton X-100, suggesting the existence of a tightly membrane-associated form of annexin V. A specific antiserum to chicken annexin V was used to localize the protein in adult and embryonic chicken liver. In the adult, annexin V was highly concentrated in epithelial cells lining the bile ducts, and along the bile canaliculi. In embryonic liver, strong staining of the bile-duct epithelial cells was again evident, and in addition, endothelial cells were strongly immunoreactive.

Structure of chicken annexin V at 2.25-A resolution.

The crystal structure of chicken annexin V has been solved by molecular replacement and refined at 2.25 A. The final R factor is 19.7% with good geometry. The chicken annexin V structure is very similar to the human annexin V structure, with four similar domains each containing five helices. The structure includes three calcium ions in domains I, II, and IV, each bound by the characteristic K-G-X-G-T-(38 residues)-D/E motif. In view of the structural similarity between human and chicken annexin V, we suggest that they have a common vital function which developed early in evolutionary history.

The pharmacogenetics of chemical carcinogenesis.

The human body is endowed with a large number of xenobiotic chemical metabolizing enzymes, a significant proportion of which are polymorphic and thus render one individual at greater or lesser risk than another of chemically-induced disease. All examples of genetic polymorphism of chemical metabolizing enzymes have been reviewed in relation to their potential to activate and detoxicate procarcinogens and promutagens. Many examples are cited whereby phenotype can act as a carcinogenic risk factor. With the availability of a large amount of DNA sequence data for chemical metabolizing enzymes there has emerged a number of polymerase chain reaction (PCR) strategies aimed at discerning one metabolic phenotype or another. This is seen as a very positive and democratic scientific development, widening the franchise for studies of disease risk. Nevertheless, it is argued that, at these early stages with many laboratory-based scientists scarcely familiar with epidemiological study design, a cautious approach should obtain when interpreting single studies.

Crystallization and preliminary X-ray studies of annexin IV (endonexin), a calcium-dependent phospholipid-binding protein.

Annexin IV (endonexin) has been purified from chicken liver and crystallized by the vapour diffusion method. Crystals which diffract to at least 2.2 A have been obtained. They belong to space group R3 and have unit cell dimensions of a = b = 99.4 A, c = 96.2 A, alpha = 90 degrees, beta = 90 degrees, gamma = 120 degrees. There is one molecule of 32,500 Da per asymmetric unit.

Characterization of annexins in mammalian brain.

Three annexins--p68, endonexin, and p32--have been isolated from porcine brain using their calcium-dependent affinity for membranes. Large amounts (20-50 mg/kg of tissue) of p68 and p32 can be isolated from cerebrum and cerebellum. The p68 is present as up to 0.3% of total porcine brain protein. The p68 and p32 from porcine brain bind to phosphatidic acid (half-maximal binding at 6 and 34 microM free calcium, respectively) and to phosphatidylserine (8 and 34 microM, respectively). They do not bind to phosphatidylcholine at calcium concentrations up to 1 mM. Two other major proteins (Mr 180,000 and Mr 76,000) were isolated with the annexins in a calcium-dependent manner but do not bind to phospholipids. The 180-kilodalton protein is the heavy chain of clathrin. From immunohistochemical studies, p68 is strongly associated with the plasma membranes of Purkinje cell bodies and dendrites in porcine cerebellum. It is also an intracellular component of Purkinje cells localized to perinuclear structures. Staining of axons in the white matter and granule cell layer was also seen. In contrast, p32 is completely absent from Purkinje cells and their dendrites; it is predominantly located in the molecular layer and in white matter of the cerebellar folds. The distribution of p32 may be consistent with a predominantly glial localization.

Isolation and characterization of two novel calcium-dependent phospholipid-binding proteins from bovine lung.

Two calcium-dependent proteins of apparent Mr 32,000 and 34,000 were isolated from bovine lung. Approx. 70 mg/kg of each was obtained. Two-dimensional gel electrophoresis in the presence of 8 M urea showed their apparent p/values to be 5.1 and 5.0, respectively. Both proteins are related immunologically to calelectrin from Torpedo marmorata. They also have very similar amino acid compositions to calelectrin. Partial sequence information shows that both proteins contain the highly conserved sequence described for the annexins, a new family of calcium-dependent membrane-binding proteins. In common with other members of this family, the new proteins bind to acidic phospholipids in a calcium-dependent manner.

Annexins--new family of Ca2+-regulated-phospholipid binding protein.

Calcium and phospholipid binding proteins have been identified and localized by immunocytochemistry in a wide range of cells and tissues. Two of these proteins (calpactins) also bind F-actin and are substrates for tyrosine kinases. The similar membrane-binding properties of these molecules arise from conserved amino acid sequences and a model is proposed for the tertiary structure of a common calcium and phospholipid binding domain.

Cytoskeletal proteins at the cholinergic synapse: distribution of desmin, actin, fodrin, neurofilaments, and tubulin in Torpedo electric organ.

Treatment of the electric organ of Torpedo marmorata with Triton X-100 in the presence of 2 mM MgCl2 generated a cytoskeletal fraction in which a 54 kDa polypeptide is a major constituent. This 54 kDa polypeptide accounted for about 8% of the cellular protein when total electric organ tissue was analyzed by two-dimensional gel electrophoresis. Immunoblotting experiments showed that this protein reacts with monoclonal antibodies to desmin, the major intermediate filament protein of avian and mammalian muscle tissue. Negative stain analysis revealed that filaments of about 10 nm diameter are the major structural elements of the electric organ cytoskeleton. In the presence of Ca2+ there was a rapid degradation of the desmin-like protein and intermediate filaments due to a Ca2+-activated protease. Some of the resulting fragments retained antigenic activity against the desmin antibodies. Immunoblotting of membrane fractions enriched in acetylcholine receptor revealed desmin in addition to some actin. A further cytoskeletal component was identified from biochemical and immunological properties as a homologue of the mammalian neurofilament L-polypeptide. Thus Torpedo expresses proteins homologous to the mammalian desmin and neurofilament L-protein which can be detected using immunological approaches. Immunofluorescence microscopy was used to map the location of various cytoskeletal proteins of the cholinergic synapse on paraffin sections and on en face preparations of membranes. Desmin staining was restricted to electrocytes and in en face preparations was seen associated with both the ventral receptor-containing membrane and with the non-innervated dorsal membrane. Antibodies to neurofilament L-protein stained only the axons and not the electrocytes. Staining for fodrin, a non-erythrocyte spectrin, resulted in submembraneous decoration of both the axons and the electrocytes. Axonal staining for neurofilaments and microtubules did not extend into the ends of the nerve terminal arborizations.