scholarly journals Duplication of type IV collagen COOH-terminal repeats and species-specific expression of alpha 1(IV) and alpha 2(IV) collagen genes.

1987 ◽  
Vol 262 (19) ◽  
pp. 9231-9238
Author(s):  
J C Myers ◽  
P S Howard ◽  
A M Jelen ◽  
A S Dion ◽  
E J Macarak
Development ◽  
1988 ◽  
Vol 102 (2) ◽  
pp. 339-347 ◽  
Author(s):  
P. Simon-Assmann ◽  
F. Bouziges ◽  
C. Arnold ◽  
K. Haffen ◽  
M. Kedinger

The production and deposition of extracellular matrix proteins and the cellular origin of type-IV collagen have been analysed immunocytochemically in cocultured or transplanted intestinal epithelial-mesenchymal cell associations. In the first experimental model, rat intestinal endodermal cells were cultured on top of confluent monolayers of rat intestinal or skin fibroblastic cells. Under these conditions, interstitial matrix and basement membrane proteins were deposited within the fibroblastic layer over the whole culture period; interactions between the epithelial cells and the fibroblastic cell population, whatever their organ of origin, were required for the production of the basement membrane. In addition, its formation was progressive as assessed by the shift of a spot-like labelling to a continuous linear pattern at the epithelial-mesenchymal interface, and paralleled epithelial cell differentiation. In the second experimental model, chick-rat epithelial-mesenchymal recombinants developed as intracoelomic grafts were used, and the immunocytochemical detection of a basement membrane protein, type-IV collagen, was performed with species-specific antibodies. The major role of the mesenchyme in the deposition of type-IV collagen is supported by the fact that anti-chick but not anti-mammalian antibodies stained this antigen in chick mesenchyme-rat endoderm recombinants. These observations emphasize the role of tissue interactions in the formation of a basement membrane and show that the mesenchymal compartment is the principal endogenous source of type-IV collagen.


1996 ◽  
Vol 7 (5) ◽  
pp. 702-709 ◽  
Author(s):  
N Heiskari ◽  
X Zhang ◽  
J Zhou ◽  
A Leinonen ◽  
D Barker ◽  
...  

Conditions for polymerase chain-reaction amplification of ten exon regions (Exons 3, 7, 11 through 13, and 15 through 19) of the collagen COL4A5 gene and four exon regions (Exons 2, and 12 through 14) of the COL4A6 gene were sequenced and established in this study. These Type IV collagen genes contain 51 and 48 exons, respectively. The sequences of these exons were determined in the two genes in 250 male patients with hematuria and suspected Alport syndrome. Seventeen mutations were found in nine of the ten exons studied in the COL4A5 gene in 17 patients, whereas no mutations were identified in COL4A6. One mutation was identical in two patients known to be unrelated. The results indicate that mutations in COL4A5 that leading to renal failure are more frequent than those involved in classic Alport syndrome, and also that mutations in COL4A6 are not likely to cause this disease. Furthermore, mutations in COL4A5 are distributed quite randomly and no "hot spots" were found.


1993 ◽  
Vol 123 (1) ◽  
pp. 255-264 ◽  
Author(s):  
M H Sibley ◽  
J J Johnson ◽  
C C Mello ◽  
J M Kramer

The nematode Caenorhabditis elegans has two type IV collagen genes homologous to the mammalian alpha 1(IV) and alpha 2(IV) collagen genes. We demonstrate by transgenic rescue of mutant animals that the genetic locus encoding the C. elegans alpha 2(IV) collagen gene is let-2 on the X chromosome. The most severe effect of mutations in let-2 is temperature-sensitive embryonic lethality. The embryonic lethal phenotype is similar to that seen in animals with mutations in the alpha 1(IV) collagen gene, emb-9. The sequence of the entire C. elegans alpha 2(IV) collagen gene is presented. Comparisons with mammalian type IV collagen sequences show high amino acid sequence conservation in the C-terminal NCl domain and of crosslinking residues (Cys and Lys) in the N-terminal 7S domain. RT-PCR analysis shows that transcripts of the C. elegans alpha 2(IV) collagen gene are alternatively spliced. Transcripts contain one of two mutually exclusive exons, exon 9 or 10. These exons encode very similar products, differing primarily in the sequence of a 9-10 amino acid Gly-X-Y interruption. The expression of these alternatively spliced alpha 2(IV) collagen transcripts is developmentally regulated. In embryos over 90% of the alpha 2(IV) collagen mRNA contains exon 9, while larval and adult RNAs contain 80-90% exon 10. This shift in expression of alternative alpha 2(IV) collagen transcripts suggests that C. elegans embryos may require a different form of alpha 2(IV) collagen than do larvae and adults.


1988 ◽  
Vol 263 (36) ◽  
pp. 19274-19277
Author(s):  
P Kaytes ◽  
L Wood ◽  
N Theriault ◽  
M Kurkinen ◽  
G Vogeli

1995 ◽  
Vol 270 (45) ◽  
pp. 26863-26867 ◽  
Author(s):  
Toshitaka Oohashi ◽  
Yasuyoshi Ueki ◽  
Manabu Sugimoto ◽  
Yoshifumi Ninomiya

1980 ◽  
Vol 191 (2) ◽  
pp. 517-522 ◽  
Author(s):  
J Risteli ◽  
D Schuppan ◽  
R W Glanville ◽  
R Timpl

Antisera against mouse and human basement-membrane type IV collagen showed in radioimmunoassays distinct binding with large pepsin fragments obtained from the C-terminal portions of alpha 1 (IV)- and alpha 2 (IV)-chains. These reactions were specific for each constituent polypeptide chain. The data were confirmed by immunoadsorption, allowing the separation of antibodies with restricted chain specificity. Inhibition assays with CNBr peptides demonstrated the different localizations of antigenic determinants, which were either species-specific or shared by the human and mouse antigens.


1990 ◽  
Vol 580 (1 Structure, Mo) ◽  
pp. 97-111 ◽  
Author(s):  
KARL TRYGGVASON ◽  
RAIJA SOININEN ◽  
SIRKKA LIISA HOSTIKKA ◽  
ARUPA GANGULY ◽  
MERJA HUOTARI ◽  
...  

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