			Home About us Contact

Terminal Segment (terminal + segment)

Distribution by Scientific Domains

Life Sciences	71%
Medical Sciences	28%

Selected Abstracts

Important region in the ,-spectrin C -terminus for spectrin tetramer formation

EUROPEAN JOURNAL OF HAEMATOLOGY, Issue 2 2002
Bing-Hao Luo
Abstract: Many hereditary hemolytic anemias are due to spectrin mutations at the C -terminal region of ,-spectrin (the ,C region) that destabilize spectrin tetramer formation. However, little is known about the ,C region of spectrin. We have prepared four recombinant ,-peptides of different lengths from human erythrocyte spectrin, all starting at position 1898 of the C -terminal region, but terminating at position 2070, 2071, 2072 or 2073. Native polyacrylamide gel electrophoresis showed that the two peptides terminating at positions 2070 and 2071 did not associate with an N -terminal region ,-peptide (Sp,1,156) in the micromolar range. However, the peptides that terminated at positions 2072 and 2073 associated with the ,-peptide. Circular dichroism results showed that the unassociated helices in both ,- and ,-peptides became associated, presumably to form a helical bundle, for those ,-peptides that formed an ,, complex, but not for those ,-peptides that did not form an ,, complex. In addition, upon association, an increase in the ,-helical content was observed. These results showed that the ,-peptides ending prior to residue 2072 (Thr) would not associate with ,-peptide, and that no helical bundling of the partial domains was observed. Thus, we suggest that the C -terminal segment of ,-spectrin, starting from residue 2073 (Thr), is not critical to spectrin tetramer formation. However, the C -terminal region ending with residue 2072 is important for its association with ,-spectrin in forming tetramers. [source]

Introgression of crown rust (Puccinia coronata) resistance from meadow fescue (Festuca pratensis) into Italian ryegrass (Lolium multiflorum): genetic mapping and identification of associated molecular markers

PLANT PATHOLOGY, Issue 1 2006
I. P. Armstead
Crown rust (Puccinia coronata) resistance (CRres), which had been introgressed from meadow fescue (Festuca pratensis) into the Italian ryegrass (Lolium multiflorum) background, was genetically mapped with amplified fragment length polymorphism (AFLP) and sequence tagged site (STS) markers to a terminal segment of chromosome 5. Comparative mapping had previously shown that this region of the Lolium/Festuca genome has a degree of conserved genetic synteny with chromosomes 11 and 12 of rice. Sequences from rice chromosome 12 were used as templates for identifying further STS markers that cosegregated with CRres. The relative genomic positions of molecular markers associated with CRres in L. multiflorum, L. perenne, F. pratensis and oats is discussed, along with their relationships to physical positions on rice chromosomes C11 and C12. [source]

Histochemical Detection of Glycoconjugates in the Canine Epididymis

ANATOMIA, HISTOLOGIA, EMBRYOLOGIA, Issue 2 2009
B. Schick
Summary A histochemical study using fluorescein isothiocyanate (FITC)-labelled lectins to identify glycoconjugates present in the efferent ductules and the three segments of the ductus epididymis (initial, middle and terminal segment) of dogs was carried out. The lectins used were: mannose-binding lectins (Con A, LCA and PSA), galactose-binding lectins (PNA, RCA), N -acetylgalactosamine-binding lectins (DBA, SBA, SJA and GSL I), N -acetylglucosamine-binding lectins (WGA and WGAs), fucose-binding lectins (UEA) and lectins which bind to complex carbohydrate configurations (PHA E and PHA L). The lectin-binding pattern in the canine epididymis presents similarities and differences to those observed in other mammalian species. The ductuli efferentes distinctly stained with most of the lectins used, whereas in the ductus epididymis a segment specific staining pattern was observed. Whereas principal cells of the ductus epididymis stained clearly with several FITC-labelled lectins (WGA, UEA and PHA-L), basal cells showed only a significant binding of Con A. [source]

Differential Localization of Immunoreactive ,- and ,-subunits of S-100 Protein in Feline Testis

ANATOMIA, HISTOLOGIA, EMBRYOLOGIA, Issue 2 2000
B. C. Cruzana
This study investigates the differential localization of the ,- subunit (S100-,) and the ,-subunit (S100-,) of the S-100 protein in the feline testis, using immunohistochemistry with polyclonal antibodies to bovine S-100 protein (S-100) and monoclonal antibodies to bovine S100-, and S100-,. Appreciable differences were observed in the cellular localization of the immunoreactivity of each subunit. S-100 was observed in the Sertoli cells, the epithelial cells of the transitional segment of the seminiferous tubules, Leydig cells and the peritubular cells of the seminiferous tubules, but was not observed in the epithelial cells of straight tubules and the rete testis or in the endothelial cells of blood and lymph vessels. S100-, immunoreactivity was localized in Sertoli cells, peritubular cells and the epithelial cells of the terminal segment of the tubules, whereas S100-, immunoreactivity was localized in Leydig cells. The differential localization of the ,- and ,-subunits of the S-100 protein in the feline testis suggests that this protein is multifunctional and be useful as an investigative tool in studying feline testis function. [source]

Immunohistochemical distribution of S-100 protein and subunits (S100-, and S100-,) in the swamp-type water buffalo (Bubalus bubalis) testis

ANDROLOGIA, Issue 3 2003
M. B. C. Cruzana
Summary. The distribution and localization of S-100 protein (S-100) and its subunits (S100-, and S100-,) in the testis of swamp-type water buffalo were investigated using immunohistochemistry. S-100 was detected in the Sertoli cells in the convoluted seminiferous tubules, modified Sertoli cells lining the terminal segment of the seminiferous tubules and in the intratesticular excurrent ducts (straight tubules and rete testis). S100-, showed the same distribution and localization with that of S-100. However, the cytoplasmic extension of the Sertoli cells in S100-, staining showed less staining intensity compared with that of S-100. S100-, showed a positive staining only in the modified Sertoli cells of the terminal segment of the seminiferous tubule. Endothelial cells of blood vessels were also positive with the proteins while the Leydig and spermatogenic cells showed a negative reaction. The localization of S-100 in the testis of the water buffalo was in parallel with that of other artiodactyls which supports the hypothesis that this protein is a multifunctional protein. S100-, in the Sertoli cells suggests that this protein is involved in establishing blood,testis barrier. Its presence in the modified Sertoli cells and in the epithelium of the excurrent ducts suggest secretory and absorptive function, respectively. Meanwhile, S100-,, which was detected only in the modified Sertoli cells, is involved in the secretory activity of these cells that are related to exocrine function. [source]

Identifying patterns of diversity of the actinopterygian fulcra

ACTA ZOOLOGICA, Issue 2009
Gloria Arratia
Abstract Fin rays, scutes or ridge scales, and fulcra have been traditionally interpreted as modified scales, but their diversity has been almost ignored. Based on results presented here, revised definitions of these elements are provided. At least two patterns of basal fulcra are found in actinopterygians: in Pattern I all or most basal fulcra are paired elements, whereas in Pattern II, a series of unpaired basal fulcra that are bifurcated proximally, and whose forking gradually becomes larger caudad, are followed by a series of paired elements. Basal fulcra are commonly present on unpaired fins of lower actinopterygians, including basal neopterygians. Among living fish they are absent in polypteriforms, Amia and teleosts. Fringing fulcra are always paired. Three patterns of fringing fulcra series are described: the series of fringing fulcra in basal actinopterygians is formed by expanded terminal segments of marginal lepidotrichia (Pattern A). Another series is formed by a combination of slightly expanded or modified terminal segments of rays and independent spiny, small elements (Pattern B). The third series is formed of small, spiny ossified elements positioned along the leading marginal fin ray(s) (Pattern C). Other patterns of basal and fringing fulcra remain to be investigated, along with their phylogenetic implications. [source]

Phylogenetic Relationships of the Suborders of Coleoptera (Insecta)

CLADISTICS, Issue 1 2000
Rolf G. Beutel
One hundred seven external and internal characters of larval and adult representatives of 28 genera of the coleopteran suborders were analyzed cladistically. Four groups of Neuropterida were introduced as outgroup. The analysis yielded 18 trees with a minimum of 194 steps (CI 0.691). All trees support the monophyly of all four suborders and a branching pattern (Archostemata + (Adephaga + (Myxophaga + Polyphaga))). The presence of elytra with meso- and metathoracic locking devices, the specific hind-wing folding, the close connection of exposed sclerites, the absence of the mera, the absence of eight thoracic muscles, the reduced abdominal sternite I, and the invagination of terminal segments are autapomorphies of Coleoptera. The monophyly of Coleoptera excl. Archostemata is supported by further transformations of the thoracic sclerites such as absence of the mesothoracic discriminal line and katepisternal joint, by an internalized or absent metathoracic trochantin, by the presence of a bending zone in the hind-wing, and by eight further muscle losses. Fusion of tibia and tarsus and presence of a single claw are larval synapomorphies of Myxophaga and Polyphaga. Adults are characterized by fusion of protrochantin and propleura and by the rigid connection of the meso- and metathoracic ventrites. The eucinetoid lineage of Polyphaga is characterized by the secondary absence of the bending zone of the alae. This results in a distinctly simplified wing folding mechanism. The monophyly of Cucujiformia (+ Bostrichoidea) is supported by the presence of cryptonephric Malpighian tubules. Transformations of fore-and hind-wings, reinforcement and simplification of the thoracic exoskeleton, and an efficient use of a distinctly reduced set of thoracic muscles play an important role in the early evolution of Coleoptera. Many different larval character transformations take place in the earlier Mesozoic within the suborders. [source]