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Biomedical subjects

H Ahmed

Publications and source records attributed to H Ahmed.

At least 37 records · Page 2Linked to original sources
PubMed1997

Gastric mucosal hydrophobicity in duodenal ulceration: role of Helicobacter pylori infection density and mucus lipids.

BACKGROUND & AIMS: Gastric mucosal hydrophobicity is reduced in Helicobacter pylori infection. Infection density is increased in duodenal ulcer (DU) compared with H. pylori gastritis alone, but it is unknown whether there is a corresponding difference in hydrophobicity or whether hydrophobicity is related to infection density or to mucus lipids. The aim of this study was to determine the relationship between H. pylori infection density and mucosal hydrophobicity, and between mucus lipids and hydrophobicity, and to compare results in patients with H. pylori-induced gastritis with and without DU. METHODS: Fifty-four patients, including 29 H. pylori-positive (15 with DU and 14 with gastritis alone) and 25 H. pylori-negative controls, were studied. Hydrophobicity was determined by goniometry and infection density by histology. Mucus lipids were determined by colorimetry and phospholipase A2 activity by radioenzymatic assay. RESULTS: Hydrophobicity was reduced in DU compared with gastritis alone (39 degrees vs. 48 degrees; P < 0.05) and with healthy controls (39 degrees vs. 60 degrees; P < 0.0001). Hydrophobicity correlated with infection density (Rs = -0.55; P < 0.01). Mucus triglyceride level was modestly increased with infection, but mucus phospholipids or lipolysis were unrelated to H. pylori and hydrophobicity. CONCLUSIONS: Mucosal hydrophobicity is reduced in H. pylori-positive patients with DU compared with those having gastritic only. Hydrophobicity correlates with infection density but not with mucus lipid levels.

Adult↗
PubMed1997

JSJ-1, an anti-spermidine monoclonal antibody with potential clinical applications.

Polyamines have been implicated in a wide variety of functions including nucleic acid synthesis and protein synthesis. Their levels have been shown to increase in response to cell growth and differentiation. Use of polyamines as prognostic indicators of proliferative disease conditions has been hindered by the lack of suitable rapid and sensitive assays. We report the characterization of an anti-spermidine antibody, JSJ-1, with novel putrescine cross reactivity. JSJ-1 cross-reacts more strongly with putrescine (11%) than with spermine (6%). This suggests that the aminobutyl group common to both putrescine and spermidine is an important element in the antibody-antigen interaction. We have demonstrated that antibody-spermidine binding is effected by increased ionic strength. This finding is consistent with the antibody-antigen interaction being ionic. The JSJ-1 antibody has been successfully used to detect increased polyamine levels in clinical serum samples and identify those with increased polyamine levels.

Animals↗
PubMed1996

The primary structure and carbohydrate specificity of a beta-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis.

The detailed characterization of a galectin from the toad (Bufo arenarum Hensel) ovary in its primary structure, carbohydrate specificity, and overall biochemical properties has provided novel information pertaining to structural and evolutionary aspects of the galectin family. The lectin consists of identical single-chain polypeptide subunits composed of 134 amino acids (calculated mass, 14,797 daltons), and its N-terminal residue, alanine, is N-acetylated. When compared to the sequences of known galectins, the B. arenarum galectin exhibited the highest identity (48% for the whole molecule and 77% for the carbohydrate recognition domain (CRD)) with the bovine spleen galectin-1, but surprisingly less identity (38% for the whole molecule and 47% for the CRD) with a galectin from Xenopus laevis skin (Marschal, P., Herrmann, J., Leffler, H., Barondes, S. H., and Cooper, D. N. W. (1992) J. Biol. Chem. 267, 12942-12949). Unlike the X. laevis galectin, the binding activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccharide and Galbeta1,3GalNAc relative to lactose, was in agreement with that observed for the galectin-1 subgroup and those galectins having "conserved" (type I) CRDs (Ahmed, H., and Vasta, G. R. (1994) Glycobiology 4, 545-549). Moreover, the toad galectin shares three of the six cysteine residues that are conserved in all mammalian galectins-1, but not in the galectins from X. laevis, fish, and invertebrates described so far. Based on the homologies of the B. arenarum galectin with the bovine spleen galectin-1 and X. laevis skin galectin, it should be concluded that within the galectin family the correlation between conservation of primary structure and phylogenetic distances among the source species may not be a direct one as proposed elsewhere (Hirabayashi, J., and Kasai, K. (1993) Glycobiology 3, 297-304). Furthermore, galectins with conserved (type I) CRDs, represented by the B. arenarum ovary galectin, and those with "variable" (type II) CRDs, represented by the X. laevis 16-kDa galectin, clearly constitute distinct subgroups in the extant amphibian taxa and may have diverged early in the evolution of chordate lineages.

Amino Acid Sequence↗
PubMed1996

Galectin-1 from bovine spleen: biochemical characterization, carbohydrate specificity and tissue-specific isoform profiles.

Selected biochemical properties, including the charge heterodispersity profile and carbohydrate specificity, of bovine galectin-1 were determined in detail. The lectin was purified through an improved purification protocol that yielded 35-40 mg/kg of wet tissue with a specific activity of 1.7-2 x 10(4) mg-1.ml. The galectin is a homodimer of approximately 14.5 kDa subunits with E(280)mg/ml of 0.65 ml.mg-1.cm-1. When stored in the presence of its carbohydrate ligand, the lectin's binding activity remained stable in a non-reducing environment even at room temperature. The optimal pH for binding to the ligand was 6.5-8.0. The overall carbohydrate specificity of the bovine galectin-1 isolated from spleen is similar to that of the galectin isolated from heart and to other mammalian galectins that exhibit "conserved" (Type I) carbohydrate recognition domains (CRDs) [Ahmed, H. and Vasta, G.R. (1994) Glycobiology 4, 545-549], but differs from those from Xenopus laevis and rat intestine domain I. The fluorescence of 4-methylumbelliferyl alpha-D-galactopyranoside was quenched on binding to bovine spleen galectin-1. Scatchard plots of data obtained at 5, 15, and 30 degrees C showed that the galectin has two sugar exothermic binding sites with association constants of 3.4 x 10(5), 1.0 x 10(5), and 0.3 x 10(5), respectively. Chemical modification studies indicated that histidine, tryptophan, carboxylic acid, and arginine, but not lysine or tyrosine, are involved in the binding to the carbohydrate ligand. On isoelectric focusing, the spleen galectin-1 appeared as six isoforms ranging from pI4.56-4.88 with main components at pI 4.63 (34.0%), 4.73 (42.6%), and 4.88 (16.6%). The galectin-1 isolated from heart yielded a quali- and quantitatively different profile with four isoforms ranging from pI 4.53-4.73, those with pIs of 4.56, 4.63, and 4.73 being common to the spleen homolog. Edman degradation of selected peptides purified from the spleen galectin-1 digest revealed amino acid sequences identical to those obtained for the heart galectin-1. This suggests that although point mutations in the subunit primary structure may not be the likely source of isolectins, as observed for X. laevis, tissue-specific co- or post-translational modifications may be the possible cause of the differences in the galectin isoform profile between bovine spleen and heart.

Amino Acid Sequence↗
PubMed1995

Isolation of a melibiose-binding protein from human spleen.

A melibiose-binding protein was isolated from human spleen by serial affinity chromatography on lactose-, mannose-, and melibiose-Sepharose. The purified protein agglutinated rabbit erythrocytes and re-bound to melibiose, but did not bind to murine nor human laminin. The protein was composed of approximately 58 kDa and 26 kDa polypeptides. The polypeptides were detected in buffy coat cell extracts and they were synthesized in vitro by B lymphoblastoid cells. The polypeptides did not react with anti-galaptin, anti-C-reactive protein, anti-amyloid P, anti-keratin, and anti-rat lung lectin 29 sera. The 58 kDa polypeptide reacted very weakly with anti-core-specific lectin serum and reacted with anti-IgG serum. The data suggest that the major protein isolated is an anti-Ga1 alpha 1-->6 immunoglobulin.

Animals↗
PubMed1995

Neonatal jaundice with reference to aflatoxins: an aetiological study in Zaria, northern Nigeria.

Two prospective studies were undertaken to determine a possible relationship between perinatal aflatoxin exposure and neonatal jaundice. First, cord blood samples from 37 neonates who subsequently developed jaundice and from 40 non-jaundiced (control) babies were analysed for six major aflatoxins and aflatoxicol. Peripheral blood samples of both groups were also analysed postnatally for aflatoxins. In a second study, serum aflatoxin levels of 64 jaundiced neonates admitted from outside the hospital were compared with levels in 60 non-jaundiced control babies. Aflatoxins were detected in 14 (37.8%) cord blood samples of jaundiced neonates and in nine (22.5%) of the controls. The mean cord aflatoxin concentration was highest in jaundiced neonates with septicaemia, but the difference was not statistically significant. The frequency of detection of aflatoxins in peripheral blood was not significantly different in jaundiced and non-jaundiced babies. Aflatoxins were detected in the blood of over 50% of neonates with jaundice of 'unknown' aetiology. There was no correlation between severity of hyperbilirubinaemia and serum aflatoxin levels. Further studies are needed to determine the extent of pre- and postnatal exposure to aflatoxin in Nigerian infants and the effects of such exposure on fetal and neonatal health.

Aflatoxins↗
PubMed1994

Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution.

In recent years, the significant contributions from molecular research studies on animal lectins have elucidated structural aspects and provided clues not only to their evolution but also to their multiple biological functions. The experimental evidence has suggested that distinct, and probably unrelated, groups of molecules are included under the term "lectin." Within the invertebrate taxa, major groups of lectins can be identified: One group would include lectins that show significant homology to membrane-integrated or soluble vertebrate C-type lectins. The second would include those beta-galactosyl-specific lectins homologous to the S-type vertebrate lectins. The third group would be constituted by lectins that show homology to vertebrate pentraxins that exhibit lectin-like properties, such as C-reactive protein and serum amyloid P. Finally, there are examples that do not exhibit similarities to any of the aforementioned categories. Moreover, the vast majority of invertebrate lectins described so far cannot yet be placed in one or another group because of the lack of information regarding their primary structure. (See Table 1.) Animal lectins do not express a recombinatorial diversity like that of antibodies, but a limited diversity in recognition capabilities would be accomplished by the occurrence of multiple lectins with distinct specificities, the presence of more than one binding site, specific for different carbohydrates in a single molecule, and by certain "flexibility" of the binding sites that would allow the recognition of a range of structurally related carbohydrates. In order to identify the lectins' "natural" ligands, we have investigated the interactions between those proteins and the putative endogenous or exogenous glycosylated substances or cells that may be relevant to their biological function. Results from these studies, together with information on the biochemical properties of invertebrate and vertebrate lectins, including their structural relationships with other vertebrate recognition molecules, are discussed.

Animals↗
PubMed1994

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.

The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.

Amino Sugars↗