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  • 1
    Electronic Resource
    Electronic Resource
    Structural and functional analysis of the porcine secretory carrier membrane protein 1 gene (SCAMP1) (1998)
    Springer
    Mammalian genome 9 (1998), S. 536-539 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The secretory carrier membrane proteins (SCAMPs) are highly conserved integral vesicle membrane components of the post-Golgi secretory and endocytic pathways. We have isolated and characterized the porcine SCAMP1 cDNA and gene coding for a variant of the SCAMP family. The SCAMP1 cDNA has a length of 3827 bp including a 133-bp 5′ and 2701-bp 3′ untranslated region. The mRNA has an open reading frame of 1014 nt coding for a protein of 338 amino acids with a calculated molecular mass of 37.9 kDa and a pI of 7.9. The porcine SCAMP1 is 97.04% identical with the human and rat paralogs, respectively. The SCAMP1 gene consists of nine exons with sizes ranging from 78 to 2842 bp and spans at least 70 kb of genomic DNA on porcine Chromosome (Chr) 2q21–q22. The promoter of the SCAMP1 gene is TATA-box-less, and transcription starts at a G-nucleotide 133 nt upstream the start codon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359900814
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular analysis and chromosomal assignment of the canine CALC-I/α-CGRP gene (2000)
    Springer
    Mammalian genome 11 (2000), S. 736-740 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We have isolated a recombinant phage harboring the canine CALC-I/α-CGRP gene. The gene spans a region of approx. 5.3 kb and consists of six exons with sizes ranging from 95 bp (exon 2) and 494 bp (exon 4). By alternative splicing, two transcripts with ORFs of 390 and 384 nt are generated. These encode either the 32-amino acid-long hormone calcitonin (CALC) or the neurotransmitter calcitonin gene-related peptide (α-CGRP) with a length of 37 amino acids after proteolytic processing of precursor molecules. The canine calcitonin precursor consists of 130 amino acids with a molecular mass of 14.05 kDa and a statistical pI of 8.0, whereas the deduced α-CGRP precursor harbors 128 amino acids with a molecular mass of 13.87 kDa and a statistical pI of 8.6. Both polypeptides have a common N-terminal region of 76 amino acids that is encoded by exons 2 and 3 and separated by different eight (CALC) or six (α-CGRP) amino acid spacers from the biologically active polypeptide. The CALC-I/α-CGRP gene is a member of the calcitonin gene family and was assigned to chromosome CFA 16q25.1. A comparative analysis of different dog breeds revealed a breed-specific allelic d(CAGGAG)-hexanucleotide expansion in exon 3. This expansion results in an elongation of the common N-terminal region by two amino acids (glutamine-glutamic acid) and alters the molecular mass to 14.31 kDa (pI 7.9) and 14.13 kDa (pI 8.5) of the calcitonin and α-CGRP precursor, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003350010157
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning and chromosomal assignment of the porcine 54 and 56 kDa vacuolar H(+)-ATPase subunit gene (V-ATPase) (1999)
    Springer
    Mammalian genome 10 (1999), S. 266-270 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Vacuolar proton-translocating ATPases (V-ATPase) are multisubunit enzyme complexes located in the membranes of eukaryotic cells regulating cytoplasmic pH. So far, nothing is known about the genomic organization and chromosomal location of the various subunit genes in higher eukaryotes. Here we describe the isolation and analysis of a cDNA coding for the 54- and 56-kDa porcine V-ATPase subunit alpha and beta isoforms. We have determined the genomic structure of the V-ATPase subunit gene spanning at least 62 kb on Chromosome (Chr) 4q14-q16. It consists of 14 exons with sizes ranging from 54 bp to 346 bp, with a non-coding first exon and an alternatively spliced seventh exon leading to two isoforms. The 5′ end of the V-ATPase cDNA was isolated by RACE-PCR. The V-ATPase alpha isoform mRNA, lacking the seventh exon, has an open reading frame of 1395 nucleotides encoding a hydrophilic protein of 465 amino acids with a calculated molecular mass of 54.2 kDa and a pI of 7.8, whereas the beta isoform has a length of 1449 nucleotides encoding a protein of 483 amino acids with a calculated molecular mass of 55.8 kDa. Amino acid and DNA sequence comparison revealed that the porcine V-ATPase subunit exhibits a significant homology to the VMA13 subunit of Saccharomyces cerevisiae V-ATPase complex and V-ATPase subunit of Caenorhabditis elegans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359900984
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular analysis of the porcine proteolipid protein (PLP) gene (1999)
    Springer
    Mammalian genome 10 (1999), S. 895-899 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The proteolipid protein (PLP) gene codes for the most abundant protein in the central nervous system (CNS) myelin of higher vertebrates. Its function in the myelin sheath is not clear however, a series of point mutations have been shown to have devastating effects on the myelin. The structure of the PLP genes is highly conserved, comprising seven exons that code for an open reading frame of 277 amino acids. We determined a total of 20,957 bp of the porcine PLP gene and compared this sequence with the human PLP sequence. A very high similarity was detected between the non-coding regions of the PLP genes of human and pig, interrupted primarily by several transposable elements. The porcine PLP gene was assigned to the long arm of Chromosome (Chr) X (SSXq2.2-2.4). The analysis of the PLP transcripts revealed three transcription start sites within 160 bp upstream of the translation start codon. Functional studies of the 3′ region showed the use of several polyadenylation signals. Three main transcripts were detected in adult pigs in the range of 3200, 2400, and 1600 nucleotides with Northern blot analysis. The usage of an alternative splice site within exon 3 was shown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359901110
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular characterization and chromosomal assignment of the canine protein C gene (1999)
    Springer
    Mammalian genome 10 (1999), S. 134-139 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Protein C is a precursor to a serine protease present in the plasma that plays an important physiological role in the regulation of blood coagulation. Mutations in the human protein C gene have been linked to some cases of Morbus Perthes disease, a thrombophilic condition that results in aseptic necrosis of the femur head and neck. We have cloned the canine protein C gene to investigate whether Morbus Perthes disease in dogs is also caused by mutations within this gene. A genomic λFIXII clone was isolated, and 11,420 bp of DNA sequence were determined containing the complete protein C gene (Acc No. AJ001979). As in humans, the gene consists of nine exons with the translation start codon located in the second exon. The 1.7-kb mRNA contains a 1368-bp open reading frame coding for 456 amino acids. With the genomic protein C clone as a probe in a FISH experiment, the canine protein C gene was assigned to Chromosome (Chr) 19q21-q22. To search for possible mutations, we amplified genomic DNA from one healthy and 15 clinically and pathohistologically confirmed Morbus Perthes patients. Sequence analysis did not reveal any amino acid differences between the affected dogs and the normal control. Several nucleotide polymorphisms were detected, which however, did not result in an amino acid exchange. From these data we conclude that in contrast to human, canine Morbus Perthes disease is most likely not caused by mutations within the protein C gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359900958
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  • 6
    Electronic Resource
    Electronic Resource
    Construction and characterization of a porcine P1-derived artificial chromosome (PAC) library covering 3.2 genome equivalents and cytogenetical assignment of six type I and type II loci (1999)
    Springer
    Mammalian genome 10 (1999), S. 569-572 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. A porcine P1-derived artificial chromosome (PAC) library of a male German Landrace pig was constructed in pCYPAC2. In total 90,240 clones were generated and individually transferred into microtiter plates. An average insert size of 119.1 kb was determined by analyzing 150 randomly selected PAC clones by pulsed field electrophoresis, yielding approximately 3.2 genome equivalents. The stability of nine clones was followed through 110 generations showing no reduction of the insert size. The probability of identifying a specific chromosomal region within the library was tested by screening for the presence of seven type I and five type II loci. The analysis showed that most loci (10/12) were present in the library at least twice. To determine the percentage of chimerism, six clones were analyzed by fluorescence in situ hybridization (FISH) on metaphase chromosomes. We assign one type I locus (Triadin) and three type II loci (SW855, S0300, SW1129).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359901046
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    Paper (German National Licenses)
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