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Biomedical subjects

J B Wilson

Publications and source records attributed to J B Wilson.

At least 109 records · Page 6Linked to original sources
PubMed1990

Expression of the BNLF-1 oncogene of Epstein-Barr virus in the skin of transgenic mice induces hyperplasia and aberrant expression of keratin 6.

The BNLF-1 gene of Epstein-Barr virus (EBV) encodes the latent membrane protein (LMP), one of the putative oncogene products of the virus. This gene has been expressed from two different enhancer-promoter constructs in transgenic mice, to determine its biological activity and possible contribution to oncogenesis. While transgenic mice expressing LMP in many tissues demonstrated poor viability, expression of LMP specifically in the epidermis induces a phenotype of hyperplastic dermatosis. Concomitant with the expression of LMP in this tissue (and in the esophagus) is an induction of the expression of a hyperproliferative keratin, K6, at aberrant locations within the epidermis. The epithelial hyperplastic phenotype caused by the LMP-encoding transgenes implies that the LMP plays a role in the acanthotic condition of the tongue epithelium in the human EBV- and HIV-associated syndrome oral hairy leukoplakia, as well as possibly predisposing the nasopharyngeal epithelium to carcinogenesis.

Animals↗
PubMed1990

Hemoglobin Birmingham and hemoglobin Galicia: two unstable beta chain variants characterized by small deletions and insertions.

Two unstable hemoglobins (Hbs) causing rather severe hemolytic anemia have been characterized. The beta chain of Hb Birmingham, found in an adult black man, is characterized by the loss of -Leu-Ala-His-Lys- at positions 141, 142, 143, and 144 and their replacement by one Gln residue. These changes are the result of a deletion of nine nucleotides, namely two base pairs (bp) of codon 141, all of codons 142 and 143, and one bp of codon 144; the remaining CAG triplet (C from codon 141 and AG from codon 144) codes for the inserted glutamine. In the beta chain of Hb Galicia from a Spanish patient, His and Val at positions 97 and 98 are replaced by one Leu residue. This is due to an ACG deletion in codons 97 and 98, which causes the removal of one His and one Val residue, while the remaining CTG triplet (C from codon 97 and TG from codon 98) codes for the inserted leucine residue. Two mechanisms, namely slipped mispairing in the presence of short repeats, and misreading by DNA polymerase due to a local distortion of the DNA helix, are considered in explaining the origin of the small deletions.

Adult↗
PubMed1990

Hb Sun Prairie or alpha(2)130(H13)Ala----Pro beta 2, a new unstable variant occurring in low quantities.

A severe hemolytic anemia with microcytosis and hypochromia was present in a young adopted Indian patient. Reversed phase high performance liquid chromatographic methodology and heat stability tests detected an unstable alpha chain which was present in 3 to 5% of the total hemoglobin. A larger quantity of the alpha X chain was obtained by preparative reversed phase high performance liquid chromatography. Structural analyses identified an Ala----Pro replacement at position 130 of the alpha chain. The instability of the variant, named Hb Sun Prairie, is comparable to that of Hb Bibba [alpha 136 (H19)Leu----Pro]. Gene mapping failed to detect an alpha-thalassemia deletion (alpha alpha/alpha alpha), while dot-blot analysis of amplified DNA with synthetic probes localized a G----C mutation in codon 130 (resulting in the Ala----Pro mutation) of the alpha 2-globin genes of both chromosomes. These results suggest a homozygosity for the G----C mutation and the condition alpha 2(G----C)alpha 1/alpha 2(G----C)alpha 1 adequately explains the rather severe clinical status of this child, including the marked microcytosis and hypochromia. Unfortunately, family studies to exclude the presence of a large deletion involving all zeta- and alpha-globin genes were not possible.

Amino Acid Sequence↗
PubMed1990

Hb F-Catalonia or alpha 2G gamma(2)15(A12)Trp----Arg.

Hb F-Catalonia, a G gamma chain variant with a Trp----Arg substitution at position gamma 15(A12), was observed in two Spanish newborn babies from Northeastern Spain. Analyses were performed with different reversed phase high performance liquid chromatographic procedures that allowed the identification of the amino acid replacement in only a minute quantity of the isolated G gamma X chain.

Amino Acids↗
PubMed1990

Hb Iowa or alpha 2 beta 2(119)(GH2)Gly----Ala.

Hb Iowa with a Gly----Ala mutation at position beta 119(GH2) was observed in a Black infant and her mother. The baby was also heterozygous for Hb S; Hb Iowa was confused with Hb F at birth because its electrophoretic mobility was similar to that of Hb F1. The beta chain of Hb Iowa could be readily separated from the beta A, alpha, and gamma chains by polyacrylamide gel electrophoresis and by reversed phase high performance liquid chromatography. Structural characterization was through amino acid analyses of peptides isolated from a tryptic digest of the aminoethylated beta-Iowa chain. The Gly----Ala replacement in Hb Iowa does not affect its stability and oxygen carrying properties; hematological data for mother and child were within normal ranges.

Adult↗
PubMed1990

Hb F-Jiangsu, the first gamma chain variant with a valine----methionine substitution: alpha 2A gamma 2 134(H12)Val----Met.

During a survey of cord blood samples of healthy Chinese babies an A gamma variant was detected by its partial separation from normal A gamma in a high performance liquid chromatographic experiment. Structural analysis of the isolated A gamma X chain identified a Val----Met substitution at position A gamma 134; this substitution created a rather unique Met-Met sequence. The ratio of A gamma X to A gamma was about 2 to 3; thus, Hb F with this variant A gamma chain appears to have approximately normal stability.

Amino Acid Sequence↗
PubMed1990

Hb Davenport or alpha 2(78)(EF7)Asn----His beta 2.

Hb Davenport is a new, stable alpha chain variant, that was detected in two members of a Caucasian family living in Iowa. Hematological data were within normal limits. It is characterized by an Asn----His replacement at position alpha 78. Mild acidic hydrolysis of the large alpha T-9 peptide, separation of the resulting fragments by reversed phase high performance liquid chromatography, and sequence analysis of a few of these peptides greatly facilitated the identification of this substitution.

Amino Acid Sequence↗
PubMed1990

Hb F-Charlotte, an A gamma variant with a threonine residue in position gamma 75 and a glycine residue in position gamma 136.

Structural analyses of an abnormal gamma chain, present in a relative amount of approximately 10% in a cord blood sample of a Black newborn baby, identified two substitutions (gamma 75 Ile----Thr and gamma 136 Ala----Gly) in an apparent variant of the A gamma chain. Gene mapping analysis of genomic DNA and hybridization with specific probes confirmed the presence of these two mutations and provided the evidence to indicate that the abnormal gamma chain was indeed a variant of A gamma with the two listed mutations.

Base Sequence↗