ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-041X
    Keywords: Oocyte nuclear proteins ; Lampbrush chromosomes ; Monoclonal antibody ; Development ; Pleurodeles waltl
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The distribution of a nuclear antigen ofPleurodeles waltl oocytes, recognized by the monoclonal antibody B24/1, has been studied during oogenesis and early embryonic development. In stage I oocytes the antigen was localized in the nucleoplasm and on two atypical structures of lampbrush chromosomes, the spheres (S) and the mass (M). The immunostaining increased as the oocyte developed. In stage VI oocytes, the nucleoplasm and spheres showed intense staining. At this stage, the nucleoplasm often contained free spheres which were also labelled. The staining of M diminished during oogenesis, as did its size. Immunoblots of nuclear proteins of oocytes at different stages confirmed that there was an accumulation of this protein during oogenesis. During embryonic development, the nuclei of all the cells of blastula and gastrula were labelled by this antibody: there was no embryonic regionalization. Starting from the neurula stage, the staining progressively disappeared from the nuclei of ectodermal and mesodermal cells. In the tailbud stage, only the endodermal cell nuclei showed faint staining. Immunoblots of proteins from embryos of different stages showed that the quantity of this protein was constant until the young gastrula stage and then decreased progressively; in the young tailbud stage, this protein was practically absent. B24/1 is the first described protein of the sphere. This protein is accumulated in the oocyte nucleus and behaves like a maternal polypeptide, shifting early in the nuclei during embryonic development. Thus, B24/1 probably has a function required from the early developmental stages, perhaps in relation with small nuclear ribonucleoproteins.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-1211
    Keywords: Key words Axolotl ; Salamander ; Metamorphosis ; Development ; Class II
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Unlike most salamanders, the Mexican axolotl (Ambystoma mexicanum) fails to produce enough thyroxin to undergo anatomical metamorphosis, although a “cryptic metamorphosis” involving a change from fetal to adult hemoglobins has been described. To understand to what extent the development of the axolotl hemopoietic system is linked to anatomical metamorphosis, we examined the appearance and thyroxin dependence of class II molecules on thymus, blood, and spleen cells, using both flow cytometry and biosynthetic labeling followed by immunoprecipitation. Class II molecules are present on B cells as early as 7 weeks after hatching, the first time analyzed. At this time, most thymocytes, all T cells, and all erythrocytes lack class II molecules, but first thymocytes at 17 weeks, then T cells at 22 weeks, and finally erythrocytes at 26–27 weeks virtually all bear class II molecules. Class II molecules and adult hemoglobin appear at roughly the same time in erythrocytes. These data are most easily explained by populations of class II-negative cells being replaced by populations of class II-positive cells, and they show that the hemopoietic system matures at a variety of times unrelated to the increase of thyroxin that drives anatomical metamorphosis. We found that administration of thyroxin during axolotl ontogeny does not accelerate or otherwise affect the acquisition of class II molecules, nor does administration of drugs that inhibit thyroxin (sodium perchlorate, thiourea, methimazole, and 1-methyl imidazole) retard or abolish this acquisition, suggesting that the programs for anatomical metamorphosis and some aspects of hemopoietic development are entirely separate.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 51 (2000), S. 681-687 
    ISSN: 1432-1211
    Keywords: Lymphocytopoiesis Immunity RAG1 Development Urodele amphibian Axolotl
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The developmental expression of the RAG1 gene in the Mexican axolotl hematopoietic organs was studied. RAG1 mRNAs were first detected in trunk extracts from 6-week-old larvae, and in head and trunk extracts of 8- and 9-week-old larvae. RAG1 is expressed in the thymus at all stages of development, until its natural involution after 12 months of age. In contrast, although RAG1 transcripts were present in the spleen and liver of the young larvae, they were not detected in the liver after 4.5 months and in the spleen after 8 months. No RAG1 mRNA expression was observed in the spleens or livers of 24-month-old hyperimmunized axolotls. The developmental expression of the RAG2 protein was also analyzed in axolotl thymus, spleen, and liver extracts using specific anti-RAG2 antibodies. RAG2 was readily detected at 7 months, but not in hematopoietic organs of 12- and 24-month-old axolotls. The presence of RAG1 transcripts was limited to the sub-capsular area of the thymus lobes, as detected by in situ hybridization. Discrete clusters of labeled cells were observed in the spleen sections, and a relatively large number of labeled cells were located in the hepatic peripheral hematopoietic layer of 3-month-old axolotls. The first appearance of RAG1 gene products in the axolotl hematopoietic organs is thus well correlated with the first production of rearranged T-cell and B-cell receptor mRNAs, 40–60 days after fertilization.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1432-1211
    Keywords: Immunoglobulin Light chain Lambda Phylogeny Amphibian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We report here the structure of cDNA clones encoding axolotl light chains of the lambda type. A single IGLC gene and eight different potential IGLV genes belonging to four different families were detected. The axolotl Cλ domain has several residues or stretches of residues that are typically conserved in mammalian, avian, and Xenopus C λ, but the KATLVCL stretch, which is well conserved in the Cλ and T-cell receptor Cβ domains of many vertebrate species, is not well conserved. All axolotl Vλ sequences closely match several human and Xenopus Vλ-like sequences and, although the axolotl Cλ and Vλ sequences are very like their tetrapod homologues, they are not closely related to nontetrapod L chains. Southern blot experiments suggested the presence of a single IGLC gene and of a limited number of IGLV genes, and analysis of IGLV-J junctions clearly indicated that at least three of the IGLJ segments can associate with IGLV1, IGLV2, or IGLV3 subgroup genes. The overall diversity of the axolotl Vλ CDR3 junctions seems to be of the same order as that of mammalian Vλ chains. However, a single IGLV4 segment was found among the 45 cDNAs analyzed. This suggests that the axolotl IGL locus may have a canonical tandem structure, like the mammalian IGK or IGH loci. Immunofluorescence, immunoblotting, and microsequencing experiments strongly suggested that most, if not all L chains are of the λ type. This may explain in part the poor humoral response of the axolotl.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Atlantic salmon (Salmo salar) cDNAs encoding the T-cell antigen receptor beta chain (TCRB) were isolated from leukocyte RNA by reverse transcription – polymerase chain reaction (RT-PCR). Twenty-five distinct cDNA fragments covering the variable (V) – diversity (D) – joining (J) junction and part of the constant (C) region were characterized; the sequences of which indicate interchangeable V/D/J usage and expression in the context of one TCRBC gene. Full-length TCRBC sequence information was derived from a leukocyte cDNA library. Key residues of the salmon TCRBC region are in good agreement with those of other species. One distinct exception is the absence of the hinge region cysteine residue which is involved in covalent bonding between the alpha and beta chain in mammalian TCRs. As in amphibian and avian species, the salmon TCRBC membrane proximal region is considerably shorter than the mammalian. An octamer sequence (GGACAGGG) very similar to amphibian, avian, and mammalian D sequences could be recognized in the VDJ junctions from salmon. The pattern of VDJ variability also indicates that mechanisms like trimming and addition occur in fish as in higher vertebrates. Compared with mammals, a relatively high frequency (32%) of the VDJ junctions in salmon were out of frame.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract An Igh-V library was constructed from the head kidney cytoplasmic RNA of an 8.5-month-old non-immunized rainbow trout, Oncorhynchus mykiss, using the 5′ RACE polymerase chain reaction. Six new Igh-V segments were identified, bringing to nine the number of Igh-V families actually defined in that species. A phylogenetic analysis shows that these nine Igh-V families can be classified into three major groups. The first includes the Igh-V1, Igh-V3, Igh-V4, and Igh-V7 families, and is homologous to the human and mouse Group III Igh-V families. The second includes the Igh-V5, Igh-V8, and Igh-V9 families and is more closely related to the Group I and Group II human and mouse Igh-V families. The third group includes the Igh-V2 and Igh-V6 families, which are not closely related to any other vertebrate Igh-V gene. Six Igh-J segments were characterized. They can recombine with Igh-V segments belonging to different families and there is a high level of junctional diversity between the Igh-V and Igh-J segments.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract An RNA polymerase chain reaction strategy was used to amplify and clone a cDNA segment encoding for the complete constant part of the axolotl IgY heavy (Cυ) chain. Cυ is 433 amino acids long and organized into four domains (Cυ1–Cυ4); each has the typical internal disulfide bond and invariant tryptophane residues. Axolotl Cυ is most closely related to Xenopus Cυ (40% identical amino acid residues) and Cυ1 shares 46.4% amino acid residues among these species. The presence of additional cysteines in Cυ1 and Cυ2 domains is consistent with an additional intra-domain S-S bond similar to that suggested for Xenopus Cυ and Cχ, and for the avian Cυ and the human Cε. Cυ4 ends with the Gly-Lys dipeptide characteristic of secreted mammalian Cγ3, human Cε4, and avian and anuran Cυ4, and contains the consensus [G/GT(AA)] nucleotide splice signal sequence for joining Cυ4 to the transmembrane region. These results are consistent with the hypothesis of an ancestral structural relationship between amphibian, avian υ chains, and mammalian ε chains. However, these molecules have different biological properties: axolotl IgY is secretory Ig, anuran and avian IgY behave like mammalian IgG, and mammalian IgE is implicated in anaphylactic reactions.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Polymerase chain reaction was used to isolate cDNA clones encoding putative T-cell receptor (TCR) α chains in an amphibian, the Mexican axolotl (Ambystoma mexicanum). Five TCRα-V chain-encoding segments were identified, each belonging to a separate family. The best identity scores for these axolotl TCRα-V segments were all provided by sequences belonging to the human TCRα-V1 family and the mouse TCRα-V3 and TCRα-V8 families. A total of 14 different TCRA-J segments were identified from 44 TCRA-V/TCRA-J regions sequenced, suggesting that a large repertoire of TCRA-J segments is a characteristic of most vertebrates. The structure of the axolotl CDR3 α chain loop is in good agreement with that of mammals, including a majority of small hydrophobic residues at position 92 and of charged, hydrophilic, or polar residues at positions 93 and 94, which are highly variable and correspond to the TCRA-V/J junction. This suggests that some positions of the axolotl CDR3 α chain loop are positively selected during T-cell differentiation, particularly around residue 93 that could be selected for its ability to makes contacts with major histocompatibility complex-associated antigenic peptides, as in mammals. The axolotl Cα domain had the typical structure of mammalian and avian Cα domains, including the charged residues in the TM segment that are thought to interact with other proteins in the membrane, as well as most of the residues forming the conserved antigen receptor transmembrane motif.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Two subsets of lateral loops scattered on lampbrush chromosomes of the newtPleurodeles waltl were characterized. One group was identified by labelling with a monoclonal antibody (A1). The second group was identified by the ability of the loops to be induced by heat treatment. Three loops of each subset were mapped on a short region of the two homologues of lampbrush bivalent IV. These regions appear to be heteromorphic because the six loops are always heterozygous. Five loops are found on one homologue and the sixth on the partner. The distribution of these markers in phenotypic females corresponding to the three sexual genotypes ZW, WW and ZZ shows an absolute correlation of the five loop group with the W chromosome and of the other loop with the Z chromosome. Therefore the heteromorphic regions of the homologues correspond to the differential segments of the heterochromosomes. The identification of a trisomic ZZW female suggests that the W chromosome bears female sex determinants. Furthermore the results show that heat induces loop development and that under normal conditions giant loop development is influenced by the sexual genotype.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...