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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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The complete amino acid sequence of human γ3 as predicted from the corresponding cDNA sequence. The amino acid  positions are numbered in accordance to the homologous locations within laminin γ1 (Pikkarainen et al., 1988). A 19–amino  acid signal sequence precedes the γ3 NH2 terminus (arrow marks  the signal peptide cleavage site). Peptide sequences obtained  from Edman analyses of the fragmented γ3t gel band (Fig. 1, Reduced) are underlined. Potential glycosylation sites are boxed,  and those conserved between γ1 and γ3 are also underlined. The  nidogen binding consensus sequence is boxed in bold type. The  sequence RGD is boxed and hatched.
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Figure 2: The complete amino acid sequence of human γ3 as predicted from the corresponding cDNA sequence. The amino acid positions are numbered in accordance to the homologous locations within laminin γ1 (Pikkarainen et al., 1988). A 19–amino acid signal sequence precedes the γ3 NH2 terminus (arrow marks the signal peptide cleavage site). Peptide sequences obtained from Edman analyses of the fragmented γ3t gel band (Fig. 1, Reduced) are underlined. Potential glycosylation sites are boxed, and those conserved between γ1 and γ3 are also underlined. The nidogen binding consensus sequence is boxed in bold type. The sequence RGD is boxed and hatched.

Mentions: The cDNA sequences of human γ1 and γ2 were used to probe the National Center for Biomedical Information (NCBI) expressed-sequence-tag database (dbEST), and a clone was identified that was homologous, but not identical, to γ1 and γ2. The sequence of this clone was used to design PCR primers for extensions at 3′ and 5′ ends (see Materials and Methods) using human placental cDNA, and additional sequence information was obtained by a combination of genomic DNA and placental cDNA sequencing. The resulting sequence is shown in Fig. 2. The deduced amino acid sequence contains regions with 100% identity to all three of the peptide sequences obtained from the 170-kD band (underlined in Fig. 2). The nucleotide sequence reported in this paper has been submitted to GenBank/EMBL Data Bank with the accession number AF041835.


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)

The complete amino acid sequence of human γ3 as predicted from the corresponding cDNA sequence. The amino acid  positions are numbered in accordance to the homologous locations within laminin γ1 (Pikkarainen et al., 1988). A 19–amino  acid signal sequence precedes the γ3 NH2 terminus (arrow marks  the signal peptide cleavage site). Peptide sequences obtained  from Edman analyses of the fragmented γ3t gel band (Fig. 1, Reduced) are underlined. Potential glycosylation sites are boxed,  and those conserved between γ1 and γ3 are also underlined. The  nidogen binding consensus sequence is boxed in bold type. The  sequence RGD is boxed and hatched.
© Copyright Policy
Related In: Results  -  Collection

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

Figure 2: The complete amino acid sequence of human γ3 as predicted from the corresponding cDNA sequence. The amino acid positions are numbered in accordance to the homologous locations within laminin γ1 (Pikkarainen et al., 1988). A 19–amino acid signal sequence precedes the γ3 NH2 terminus (arrow marks the signal peptide cleavage site). Peptide sequences obtained from Edman analyses of the fragmented γ3t gel band (Fig. 1, Reduced) are underlined. Potential glycosylation sites are boxed, and those conserved between γ1 and γ3 are also underlined. The nidogen binding consensus sequence is boxed in bold type. The sequence RGD is boxed and hatched.
Mentions: The cDNA sequences of human γ1 and γ2 were used to probe the National Center for Biomedical Information (NCBI) expressed-sequence-tag database (dbEST), and a clone was identified that was homologous, but not identical, to γ1 and γ2. The sequence of this clone was used to design PCR primers for extensions at 3′ and 5′ ends (see Materials and Methods) using human placental cDNA, and additional sequence information was obtained by a combination of genomic DNA and placental cDNA sequencing. The resulting sequence is shown in Fig. 2. The deduced amino acid sequence contains regions with 100% identity to all three of the peptide sequences obtained from the 170-kD band (underlined in Fig. 2). The nucleotide sequence reported in this paper has been submitted to GenBank/EMBL Data Bank with the accession number AF041835.

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