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Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain.

Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, Burgeson RE, Champliaud MF - J. Cell Biol. (1999)

Bottom Line: The gamma3 chain is also a prominent element of the apical surface of ciliated epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules.The distribution of gamma3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they are not found within ultrastructurally defined basement membranes.It seems likely that these apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.

View Article: PubMed Central - PubMed

Affiliation: The Cutaneous Biology Research Center, Massachusetts General Hospital, and the Department of Dermatology, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

ABSTRACT
Laminins are heterotrimeric molecules composed of an alpha, a beta, and a gamma chain; they have broad functional roles in development and in stabilizing epithelial structures. Here, we identified a novel laminin, composed of known alpha and beta chains but containing a novel gamma chain, gamma3. We have cloned gene encoding this chain, LAMC3, which maps to chromosome 9 at q31-34. Protein and cDNA analyses demonstrate that gamma3 contains all the expected domains of a gamma chain, including two consensus glycosylation sites and a putative nidogen-binding site. This suggests that gamma3-containing laminins are likely to exist in a stable matrix. Studies of the tissue distribution of gamma3 chain show that it is broadly expressed in: skin, heart, lung, and the reproductive tracts. In skin, gamma3 protein is seen within the basement membrane of the dermal-epidermal junction at points of nerve penetration. The gamma3 chain is also a prominent element of the apical surface of ciliated epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they are not found within ultrastructurally defined basement membranes. It seems likely that these apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.

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Localization of LAMC3 to chromosome 9, band q31-q34 by FISH. The position of LAMC3 was probed using a 1.3-kb  cDNA probe within predicted protein domains I and II of γ3.  The FISH signal (A) was superimposed over the DAPI-banded  chromosomes (B) to identify the location of the γ3 gene. Both alleles of the γ3 gene are labeled (A, arrow) at the end of the long  arm of chromosome 9 (B, 9).
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Figure 4: Localization of LAMC3 to chromosome 9, band q31-q34 by FISH. The position of LAMC3 was probed using a 1.3-kb cDNA probe within predicted protein domains I and II of γ3. The FISH signal (A) was superimposed over the DAPI-banded chromosomes (B) to identify the location of the γ3 gene. Both alleles of the γ3 gene are labeled (A, arrow) at the end of the long arm of chromosome 9 (B, 9).

Mentions: The γ3 chromosomal location was determined by searching the NCBI Human Genomic Sequencing Index data base with the γ3 cDNA sequence. The sequence is identical to a database, Sequence Tagged Sites (clone WI-14302), that has been localized to chromosome 9q33-q34. A 1.2-kb γ3 cDNA probe within domains I and II of the predicted protein, the regions of least homology among the γ chains, was used to localize LAMC3 by fluorescent in situ hybridization (FISH) analysis (SeeDNA Biotech, Inc.). The results confirm the localization to chromosome 9q31-q34 (Fig. 4).


Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain.

Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, Burgeson RE, Champliaud MF - J. Cell Biol. (1999)

Localization of LAMC3 to chromosome 9, band q31-q34 by FISH. The position of LAMC3 was probed using a 1.3-kb  cDNA probe within predicted protein domains I and II of γ3.  The FISH signal (A) was superimposed over the DAPI-banded  chromosomes (B) to identify the location of the γ3 gene. Both alleles of the γ3 gene are labeled (A, arrow) at the end of the long  arm of chromosome 9 (B, 9).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2185082&req=5

Figure 4: Localization of LAMC3 to chromosome 9, band q31-q34 by FISH. The position of LAMC3 was probed using a 1.3-kb cDNA probe within predicted protein domains I and II of γ3. The FISH signal (A) was superimposed over the DAPI-banded chromosomes (B) to identify the location of the γ3 gene. Both alleles of the γ3 gene are labeled (A, arrow) at the end of the long arm of chromosome 9 (B, 9).
Mentions: The γ3 chromosomal location was determined by searching the NCBI Human Genomic Sequencing Index data base with the γ3 cDNA sequence. The sequence is identical to a database, Sequence Tagged Sites (clone WI-14302), that has been localized to chromosome 9q33-q34. A 1.2-kb γ3 cDNA probe within domains I and II of the predicted protein, the regions of least homology among the γ chains, was used to localize LAMC3 by fluorescent in situ hybridization (FISH) analysis (SeeDNA Biotech, Inc.). The results confirm the localization to chromosome 9q31-q34 (Fig. 4).

Bottom Line: The gamma3 chain is also a prominent element of the apical surface of ciliated epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules.The distribution of gamma3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they are not found within ultrastructurally defined basement membranes.It seems likely that these apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.

View Article: PubMed Central - PubMed

Affiliation: The Cutaneous Biology Research Center, Massachusetts General Hospital, and the Department of Dermatology, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

ABSTRACT
Laminins are heterotrimeric molecules composed of an alpha, a beta, and a gamma chain; they have broad functional roles in development and in stabilizing epithelial structures. Here, we identified a novel laminin, composed of known alpha and beta chains but containing a novel gamma chain, gamma3. We have cloned gene encoding this chain, LAMC3, which maps to chromosome 9 at q31-34. Protein and cDNA analyses demonstrate that gamma3 contains all the expected domains of a gamma chain, including two consensus glycosylation sites and a putative nidogen-binding site. This suggests that gamma3-containing laminins are likely to exist in a stable matrix. Studies of the tissue distribution of gamma3 chain show that it is broadly expressed in: skin, heart, lung, and the reproductive tracts. In skin, gamma3 protein is seen within the basement membrane of the dermal-epidermal junction at points of nerve penetration. The gamma3 chain is also a prominent element of the apical surface of ciliated epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they are not found within ultrastructurally defined basement membranes. It seems likely that these apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.

Show MeSH