ABSTRACT
The Fc receptor for immunoglobulin A (IgA), FcalphaRI, is expressed on several types of myeloid cells, and activates them upon ligand binding. However, binding of IgA to the extracellular domain of the receptor requires previous stimulation of the cell by cytokines, and the cytoplasmic tail of FcalphaRI has been shown to play a role in this. Therefore, polymorphism in this region might affect this process. However, no changes in the amino acid sequence in this region of the FcalphaRI have so far been reported. Here, we describe for the first time a single nucleotide polymorphism in exon 5 of the immunoglobulin A Fc receptor (FCAR) gene leading to a Ser-->Gly substitution at position 248 of the mature FcalphaRI protein. Prediction of structural features suggests some changes that may affect the function of the protein to some extent. However, the Gly248 variant is quite common (4% homozygotes and 38% heterozygotes) in healthy population, suggesting a weak effect, if any, on function, at least in heterozygotes.
Subject(s)
Antigens, CD/genetics , Cytoplasm/genetics , Polymorphism, Single Nucleotide , Receptors, Fc/genetics , Amino Acid Sequence , Amino Acid Substitution , Exons , Humans , Molecular Sequence DataABSTRACT
Collagen II was isolated and characterized from hyaline cartilage (articular cartilage) and fibro-cartilage (annulus fibrosus). Collagen II from the latter tissue has a substantially higher degree of hydroxylation and glycosylation than that isolated from articular cartilage. The higher degree of posttranslational modification was associated with a slower electrophoretic mobility, a greater resistance to mammalian collagenase digestion and a higher thermal stability. An increase of glycosylation accelerates the initial steps in fibril formation of collagen molecules but slows down the following lateral growth. The newly formed aggregates of collagen II from annulus fibrosus consisted of fibrils with a smaller diameter.
Subject(s)
Cartilage, Articular/chemistry , Cartilage/chemistry , Collagen/biosynthesis , Protein Processing, Post-Translational , Amino Acid Sequence , Child , Collagen/chemistry , Electrophoresis, Polyacrylamide Gel , Glycosylation , Hot Temperature , Humans , Molecular Sequence Data , Organ SpecificityABSTRACT
A reevaluation of the secondary structure of Na, Ca and K channel proteins led to the following results. Only three segments (S1, S5 and S6) of each repeat are sufficiently hydrophobic to be predicted as transmembrane helices, if a window of 19 amino acids is used. Some of the S2 and S3 segments show higher hydrophobic values when calculated with the window of 9 amino acids and can be predicted as short helices. S4 segments are strongly hydrophilic and cannot be predicted as transmembrane helices. Some of the S2, S3 and S4 segments have an amphipathic character; however, these helices do not span a membrane. A model is proposed where 12 hydrophobic transmembrane helices surround 12 shorter helices, forming a hydrophilic pore. In addition, a unique pattern for S4 segments of voltage-gated channel proteins is defined.
Subject(s)
Ion Channel Gating , Membrane Proteins/chemistry , Protein Conformation , Amino Acid Sequence , Molecular Sequence Data , SolubilityABSTRACT
Human haptoglobin (Hp) of the 1-1 type incorporated one spin or fluorescence marker per molecule; the markers were found in the beta chain. Formation of the complex between spin-labelled Hp and haemoglobin or antibody caused conformational changes in the Hp molecular, evidenced by increased participation in the electron paramagnetic resonance spectrum of the component bound with the slowly rotating marker. From fluorescence-labelled Hp, the beta chain was isolated and cleaved by CNBr; only in one of the obtained peptides, one out of 4 histidine residues was modified with the marker.
