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A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: identification, expression, and functional characterization.

Koch M, Murrell JR, Hunter DD, Olson PF, Jin W, Keene DR, Brunken WJ, Burgeson RE - J. Cell Biol. (2000)

Bottom Line: In addition, beta-netrin is expressed in a limited set of fiber tracts within the brain, including the lateral olfactory tract and the vomeronasal nerve.Functional studies were performed and show that beta-netrin promotes neurite elongation from olfactory bulb explants.Together, these data suggest that beta-netrin is important in neural, kidney, and vascular development.

View Article: PubMed Central - PubMed

Affiliation: Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

ABSTRACT
The netrins are a family of laminin-related molecules. Here, we characterize a new member of the family, beta-netrin. beta-Netrin is homologous to the NH(2) terminus of laminin chain short arms; it contains a laminin-like domain VI and 3.5 laminin EGF repeats and a netrin C domain. Unlike other netrins, this new netrin is more related to the laminin beta chains, thus, its name beta-netrin. An initial analysis of the tissue distribution revealed that kidney, heart, ovary, retina, and the olfactory bulb were tissues of high expression. We have expressed the molecule in a eukaryotic cell expression system and made antibodies to the expressed product. Both in situ hybridization and immunohistochemistry were used to describe the cellular source of beta-netrin and where beta-netrin is deposited. beta-Netrin is a basement membrane component; it is present in the basement membranes of the vasculature, kidney, and ovaries. In addition, beta-netrin is expressed in a limited set of fiber tracts within the brain, including the lateral olfactory tract and the vomeronasal nerve. Functional studies were performed and show that beta-netrin promotes neurite elongation from olfactory bulb explants. Together, these data suggest that beta-netrin is important in neural, kidney, and vascular development.

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Genetic relationship of the netrins with the NH2-terminal regions of selected laminin chains in mouse. Netrin-1 and -3 are closely related to the laminin γ chains, whereas β-netrin shares greater amino acid identity with the laminin β chains.
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Figure 2: Genetic relationship of the netrins with the NH2-terminal regions of selected laminin chains in mouse. Netrin-1 and -3 are closely related to the laminin γ chains, whereas β-netrin shares greater amino acid identity with the laminin β chains.

Mentions: The β-netrin V and VI domains are 43% identical to the laminin β1 chain V and VI domains, 42% identical to those in the laminin β2 chain, and 38% identical to those in the laminin β3 chain (Fig. 2). The V and VI domains of β-netrin are 32% identical to those in the laminin γ1 chain; for comparison, netrin-1 has 50% identity with the laminin γ1 chain. Full-length mouse β-netrin is 31% identical to mouse netrin-1 and 28% identical to mouse netrin 3. Among all the netrins, the second EGF-like repeat is the most highly conserved (β-netrin versus netrin-1, 54% amino acid identity; β-netrin versus netrin 3, 56% identity); the EGF-like repeats 1 and 3 ranged from 26 to 39% amino acid identity.


A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: identification, expression, and functional characterization.

Koch M, Murrell JR, Hunter DD, Olson PF, Jin W, Keene DR, Brunken WJ, Burgeson RE - J. Cell Biol. (2000)

Genetic relationship of the netrins with the NH2-terminal regions of selected laminin chains in mouse. Netrin-1 and -3 are closely related to the laminin γ chains, whereas β-netrin shares greater amino acid identity with the laminin β chains.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2192657&req=5

Figure 2: Genetic relationship of the netrins with the NH2-terminal regions of selected laminin chains in mouse. Netrin-1 and -3 are closely related to the laminin γ chains, whereas β-netrin shares greater amino acid identity with the laminin β chains.
Mentions: The β-netrin V and VI domains are 43% identical to the laminin β1 chain V and VI domains, 42% identical to those in the laminin β2 chain, and 38% identical to those in the laminin β3 chain (Fig. 2). The V and VI domains of β-netrin are 32% identical to those in the laminin γ1 chain; for comparison, netrin-1 has 50% identity with the laminin γ1 chain. Full-length mouse β-netrin is 31% identical to mouse netrin-1 and 28% identical to mouse netrin 3. Among all the netrins, the second EGF-like repeat is the most highly conserved (β-netrin versus netrin-1, 54% amino acid identity; β-netrin versus netrin 3, 56% identity); the EGF-like repeats 1 and 3 ranged from 26 to 39% amino acid identity.

Bottom Line: In addition, beta-netrin is expressed in a limited set of fiber tracts within the brain, including the lateral olfactory tract and the vomeronasal nerve.Functional studies were performed and show that beta-netrin promotes neurite elongation from olfactory bulb explants.Together, these data suggest that beta-netrin is important in neural, kidney, and vascular development.

View Article: PubMed Central - PubMed

Affiliation: Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

ABSTRACT
The netrins are a family of laminin-related molecules. Here, we characterize a new member of the family, beta-netrin. beta-Netrin is homologous to the NH(2) terminus of laminin chain short arms; it contains a laminin-like domain VI and 3.5 laminin EGF repeats and a netrin C domain. Unlike other netrins, this new netrin is more related to the laminin beta chains, thus, its name beta-netrin. An initial analysis of the tissue distribution revealed that kidney, heart, ovary, retina, and the olfactory bulb were tissues of high expression. We have expressed the molecule in a eukaryotic cell expression system and made antibodies to the expressed product. Both in situ hybridization and immunohistochemistry were used to describe the cellular source of beta-netrin and where beta-netrin is deposited. beta-Netrin is a basement membrane component; it is present in the basement membranes of the vasculature, kidney, and ovaries. In addition, beta-netrin is expressed in a limited set of fiber tracts within the brain, including the lateral olfactory tract and the vomeronasal nerve. Functional studies were performed and show that beta-netrin promotes neurite elongation from olfactory bulb explants. Together, these data suggest that beta-netrin is important in neural, kidney, and vascular development.

Show MeSH
Related in: MedlinePlus