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A Carlos

Publications and source records attributed to A Carlos.

9 recordsLinked to original sources
PubMed2002

Analysis of genetic heterogeneity of hepatitis C viruses in Central America reveals a novel genetic lineage. Brief report.

Hepatitis C virus (HCV) has high genomic variability and at least six different types have been reported. The genotypes distribution is currently unknown among HCV strains circulating in Central America. In order to study the degree of genetic variability of strains isolated in Costa Rica, sequence data obtained from the 5' non coding region from 7 patients from Costa Rica were compared with published sequences from 57 strains of all types. The phylogenetic analysis revealed the existence of type 1 strains of a novel genetic lineage, recently described for some South American countries, and indicates an increasing diversification of HCV.

5' Untranslated Regions↗
PubMed2002

Cytochemical study of the distribution of RNA and DNA in the synaptonemal complex of guinea-pig and rat spermatocytes.

The distribution of DNA and RNA in the synaptonemal complex and related structures, was studied using high resolution cytochemical methods and in situ hybridization, in guinea pig and rat testis. Serial sectioning demonstrates that frequently the formation of the synaptonemal complex (SC) occurs without a previous development of isolated chromosomal axes. The lateral elements of the forming SC are in continuity with pairs of DNA-containing thin filaments. These chromatin filaments fold in numerous short loops just before incorporating to the lateral elements. Some of these loops are included in the ribbon-like structure of the lateral elements of the mature SC. We propose that these short loops contain the DNA attachment sequences associated with the proteins of the LE. During the formation of the SC one of the two chromatin filaments incorporates at the central surface of the forming lateral element (LE) and the other is located at the external side of the LE. This unexpected distribution does not correspond to the pair of thick filaments previously discerned in structure of the LE. The presence of RNA associated with the DNA-containing thin filaments, as well as with the axial chromatin elements of the forming SC, may be related with the transcription occurring during meiotic prophase, specially during zygotene stage. We propose that RNA is involved in a still uncharacterized process essential for pairing.

Animals↗
PubMed2001

Caldesmon exhibits a clustered distribution along individual chicken gizzard native thin filaments.

Our earlier immuno-gold electron microscopic study indicated that the distribution of caldesmon (CaD) on actin filaments is not uniform and is restricted to the vicinity of the myosin filaments (Mabuchi K, Li Y, Tao T, Wang CLA (1996) J Muscle Res Cell Motil 17: 243). This suggested that CaD could effectively inhibit muscle contraction, if those actin filaments in the vicinity of myosin filaments were saturated with CaD. In the present study we further examined the distribution of CaD along isolated, crude and purified native thin filaments (NTF). Individual CaD molecules on purified NTF were visualized with the aid of a chemical crosslinker, 5,5'-dithiobis(2-nitrobenzoic acid), which efficiently crosslinks CaD to actin (Graceffa P, Adam LP, Lehman W (1993) Biochem J294: 63), and of a monoclonal anti-CaD antibody. The results indicated that individual NTF had alternating CaD-rich and CaD-deficient regions. Moreover, we found that the N-termini of all CaD molecules in a given cluster appeared on the same side of an actin filament. Electron microscopic images of crude NTF immunoprecipitated by a polyclonal antibody clearly indicated that the spacing between the CaD clusters is wide enough for myosin heads to interact with actin subunits. Similar clustering of CaD was also observed in plastic embedded tissue sections. These observations raise the possibility that CaD is not acting as a simple on/off switch, but more likely as a modulator, of smooth muscle contraction.

Actin Cytoskeleton↗
PubMed1984

Modulation of the actin-activated adenosinetriphosphatase activity of myosin by tropomyosin from vascular and gizzard smooth muscles.

Tropomyosins from bovine aorta and pulmonary artery exhibit identical electrophoretic patterns in sodium dodecyl sulfate but differ from tropomyosins of either chicken gizzard or rabbit skeletal muscle. Each of the four tropomyosins binds readily to skeletal muscle F-actin as indicated by their sedimentation with actin and by their ability to maximally stimulate or inhibit actin-activated ATPase activity at a molar ratio of one tropomyosin per seven actin monomers. Smooth and skeletal muscle tropomyosins differ in their effects on activity of skeletal myosin or heavy meromyosin (HMM); the former can enhance activity under conditions in which the latter inhibits. Gizzard and arterial tropomyosins are usually equally effective in stimulating ATPase activity of skeletal acto-HMM, but at high concentrations of Mg2+ gizzard tropomyosin is more effective, a result that cannot be attributed to differences in the binding of the two tropomyosins to F-actin. The effects of tropomyosin also depend on the type of myosin; tropomyosin enhances activity of gizzard myosin under conditions in which it inhibits that of skeletal myosin. Increasing the pH or the Mg2+ concentration can reverse the effect of tropomyosin on actin-stimulated ATPase activity of skeletal HMM from activation to inhibition, but this reversal is not found with gizzard myosin. Activity in the absence of tropomyosin is independent of pH, and the loss of activation with increasing pH is not accompanied by loss of binding of tropomyosin to actin.

Actins↗