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Neurolin Ig domain 2 participates in retinal axon guidance and Ig domains 1 and 3 in fasciculation.

Leppert CA, Diekmann H, Paul C, Laessing U, Marx M, Bastmeyer M, Stuermer CA - J. Cell Biol. (1999)

Bottom Line: Repeated intraocular injections of a mAb against Ig domain 2 disturb the disk-directed growth: axons grow in aberrant routes and fail to reach the optic disk, but remain fasciculated. mAbs against Ig domains 1 and 3 disturb the formation of tight fascicles. mAb against Ig domain 2 significantly increases the incidence of growth cone departure from the disk-oriented fascicle track, while mAbs against Ig domains 1 and 3 do not.This was demonstrated by time-lapse videorecording of labeled growth cones.Thus, Ig domain 2 of neurolin is apparently essential for growth cone guidance towards the disk, presumably by being part of a receptor (or complex) for an axon guidance component.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, University of Konstanz, D-78457 Konstanz, Germany.

ABSTRACT
The optic disk-directed growth of retinal ganglion cell axons is markedly disturbed in the presence of polyclonal antineurolin antibodies, which mildly affect fasciculation (Ott, H., M. Bastmeyer, and C.A.O. Stuermer, 1998. J. Neurosci. 18:3363-3372). New monoclonal antibodies (mAbs) against goldfish neurolin, an immunoglobulin (Ig) superfamily cell adhesion/recognition molecule with five Ig domains, were generated to assign function (guidance versus fasciculation) to specific Ig domains. By their ability or failure to recognize Chinese hamster ovary cells expressing recombinant neurolin with deletions of defined Ig domains, mAbs were identified as being directed against Ig domains 1, 2, or 3, respectively. Repeated intraocular injections of a mAb against Ig domain 2 disturb the disk-directed growth: axons grow in aberrant routes and fail to reach the optic disk, but remain fasciculated. mAbs against Ig domains 1 and 3 disturb the formation of tight fascicles. mAb against Ig domain 2 significantly increases the incidence of growth cone departure from the disk-oriented fascicle track, while mAbs against Ig domains 1 and 3 do not. This was demonstrated by time-lapse videorecording of labeled growth cones. Thus, Ig domain 2 of neurolin is apparently essential for growth cone guidance towards the disk, presumably by being part of a receptor (or complex) for an axon guidance component.

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Ig domains 1 and 3 of neurolin contribute to axon fasciculation in vitro. When growth cones elongating on polylysine  meet another axon, 47.9% of the growth cones fasciculate with  the other axon in control cultures. In the presence of mAb N850  (against Ig domain 1) 36.3% of the growth cones fasciculate with  another axon, and 33.9% do so in the presence of mAb N100  (against Ig domain 3). Similar values (32.5%) were obtained in  an earlier study (Ott et al., 1998) with neurolin Fabs (shaded  bars). mAb N518 (against Ig domain 2) does not affect the level  of fasciculation (48.8%).
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Figure 2: Ig domains 1 and 3 of neurolin contribute to axon fasciculation in vitro. When growth cones elongating on polylysine meet another axon, 47.9% of the growth cones fasciculate with the other axon in control cultures. In the presence of mAb N850 (against Ig domain 1) 36.3% of the growth cones fasciculate with another axon, and 33.9% do so in the presence of mAb N100 (against Ig domain 3). Similar values (32.5%) were obtained in an earlier study (Ott et al., 1998) with neurolin Fabs (shaded bars). mAb N518 (against Ig domain 2) does not affect the level of fasciculation (48.8%).

Mentions: In the presence of mAb N850 (requiring Ig domain 1) 36.3% of the growth cones (n = 29) fasciculated with another axon, whereas 63.7% (n = 51) continued to elongate on polylysine (Fig. 2). Similar ratios were obtained with mAb N100 (requiring Ig domain 3) where 33.9% of the growth cones (n = 37) fasciculated, and 66.1% of the growth cones (n = 72) elongated on the polylysine substrate (Fig. 2). In the presence of mAb N518 (requiring Ig domain 2), however, 48.8% of the growth cones (n = 40) fasciculated, and 51.2% (n = 42) continued to grow on polylysine (Fig. 2). These ratios were similar in control culture where no mAbs were added: 47.9% of the growth cones (n = 45) fasciculated, and 52.1% (n = 49) elongated on polylysine. These findings show that mAbs against neurolin Ig domains 1 and 3 affect axonal fasciculation to the same extent as neurolin Fabs (Ott et al., 1998), whereas mAb N518 against Ig domain 2 does not notably interfere with the choice of growth cones for growth along another axon versus growth on polylysine. The average growth velocity of axons was not affected by neurolin Fabs (Ott et al., 1998) or by our mAbs.


Neurolin Ig domain 2 participates in retinal axon guidance and Ig domains 1 and 3 in fasciculation.

Leppert CA, Diekmann H, Paul C, Laessing U, Marx M, Bastmeyer M, Stuermer CA - J. Cell Biol. (1999)

Ig domains 1 and 3 of neurolin contribute to axon fasciculation in vitro. When growth cones elongating on polylysine  meet another axon, 47.9% of the growth cones fasciculate with  the other axon in control cultures. In the presence of mAb N850  (against Ig domain 1) 36.3% of the growth cones fasciculate with  another axon, and 33.9% do so in the presence of mAb N100  (against Ig domain 3). Similar values (32.5%) were obtained in  an earlier study (Ott et al., 1998) with neurolin Fabs (shaded  bars). mAb N518 (against Ig domain 2) does not affect the level  of fasciculation (48.8%).
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Related In: Results  -  Collection

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Figure 2: Ig domains 1 and 3 of neurolin contribute to axon fasciculation in vitro. When growth cones elongating on polylysine meet another axon, 47.9% of the growth cones fasciculate with the other axon in control cultures. In the presence of mAb N850 (against Ig domain 1) 36.3% of the growth cones fasciculate with another axon, and 33.9% do so in the presence of mAb N100 (against Ig domain 3). Similar values (32.5%) were obtained in an earlier study (Ott et al., 1998) with neurolin Fabs (shaded bars). mAb N518 (against Ig domain 2) does not affect the level of fasciculation (48.8%).
Mentions: In the presence of mAb N850 (requiring Ig domain 1) 36.3% of the growth cones (n = 29) fasciculated with another axon, whereas 63.7% (n = 51) continued to elongate on polylysine (Fig. 2). Similar ratios were obtained with mAb N100 (requiring Ig domain 3) where 33.9% of the growth cones (n = 37) fasciculated, and 66.1% of the growth cones (n = 72) elongated on the polylysine substrate (Fig. 2). In the presence of mAb N518 (requiring Ig domain 2), however, 48.8% of the growth cones (n = 40) fasciculated, and 51.2% (n = 42) continued to grow on polylysine (Fig. 2). These ratios were similar in control culture where no mAbs were added: 47.9% of the growth cones (n = 45) fasciculated, and 52.1% (n = 49) elongated on polylysine. These findings show that mAbs against neurolin Ig domains 1 and 3 affect axonal fasciculation to the same extent as neurolin Fabs (Ott et al., 1998), whereas mAb N518 against Ig domain 2 does not notably interfere with the choice of growth cones for growth along another axon versus growth on polylysine. The average growth velocity of axons was not affected by neurolin Fabs (Ott et al., 1998) or by our mAbs.

Bottom Line: Repeated intraocular injections of a mAb against Ig domain 2 disturb the disk-directed growth: axons grow in aberrant routes and fail to reach the optic disk, but remain fasciculated. mAbs against Ig domains 1 and 3 disturb the formation of tight fascicles. mAb against Ig domain 2 significantly increases the incidence of growth cone departure from the disk-oriented fascicle track, while mAbs against Ig domains 1 and 3 do not.This was demonstrated by time-lapse videorecording of labeled growth cones.Thus, Ig domain 2 of neurolin is apparently essential for growth cone guidance towards the disk, presumably by being part of a receptor (or complex) for an axon guidance component.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, University of Konstanz, D-78457 Konstanz, Germany.

ABSTRACT
The optic disk-directed growth of retinal ganglion cell axons is markedly disturbed in the presence of polyclonal antineurolin antibodies, which mildly affect fasciculation (Ott, H., M. Bastmeyer, and C.A.O. Stuermer, 1998. J. Neurosci. 18:3363-3372). New monoclonal antibodies (mAbs) against goldfish neurolin, an immunoglobulin (Ig) superfamily cell adhesion/recognition molecule with five Ig domains, were generated to assign function (guidance versus fasciculation) to specific Ig domains. By their ability or failure to recognize Chinese hamster ovary cells expressing recombinant neurolin with deletions of defined Ig domains, mAbs were identified as being directed against Ig domains 1, 2, or 3, respectively. Repeated intraocular injections of a mAb against Ig domain 2 disturb the disk-directed growth: axons grow in aberrant routes and fail to reach the optic disk, but remain fasciculated. mAbs against Ig domains 1 and 3 disturb the formation of tight fascicles. mAb against Ig domain 2 significantly increases the incidence of growth cone departure from the disk-oriented fascicle track, while mAbs against Ig domains 1 and 3 do not. This was demonstrated by time-lapse videorecording of labeled growth cones. Thus, Ig domain 2 of neurolin is apparently essential for growth cone guidance towards the disk, presumably by being part of a receptor (or complex) for an axon guidance component.

Show MeSH
Related in: MedlinePlus