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Volumn 8, Issue 5, 1998, Pages 587-592

Receptors for collapsin/semaphorins

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; CHEMOREPELLENT; HYBRID PROTEIN; MUTANT PROTEIN; NERVE GROWTH FACTOR; NEUROPILIN; SEMAPHORIN; VASCULOTROPIN;

EID: 0032191129     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80085-8     Document Type: Article
Times cited : (118)

References (61)
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    • of outstanding interest. These two papers [18,19] report expression cloning of Sema III receptors. The cloning strategies adopted in these two studies are basically the same: COS cell cDNA expression libraries constructed using mRNA of E14 rat DRG or spinal cord were screened using an AP-tagged Sema III fusion protein. These two independent approaches have arrived at the same conclusion, namely that Sema III binds to a membrane protein homologous to neuropilin, which was previously isolated in various vertebrate species (see [21-24]).
    • of outstanding interest Kolodkin AL, Levengood DV, Rowe EG, Tai Y-T, Giger RJ, Ginty DD. Neuropilin is a semaphorin III receptor. Cell. 90:1997;753-762 These two papers [18,19] report expression cloning of Sema III receptors. The cloning strategies adopted in these two studies are basically the same: COS cell cDNA expression libraries constructed using mRNA of E14 rat DRG or spinal cord were screened using an AP-tagged Sema III fusion protein. These two independent approaches have arrived at the same conclusion, namely that Sema III binds to a membrane protein homologous to neuropilin, which was previously isolated in various vertebrate species (see [21-24]).
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    • of outstanding interest. This paper reports the phenotype of neuropilin-1 null mutant mice, which were generated by targeted disruption of the neuropilin (neuropilin-1) gene. The neuropilin-1 mutant mice were embryonic lethal, probably owing to abnormal development of the vascular system. Live homozygous mutant embryos were observed as late as E12.5, and showed severe abnormalities in the trajectory of the cranial and spinal nerves that expressed neuropilin-1 in normal embryos. The paper also reports that DRG growth cones of the neuropilin-1 mutants are perfectly protected from Sema III-induced collapse in vitro.
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    • of outstanding interest. This paper reports a new member of the neuropilin family, neuropilin-2, in mice. A rat neuropilin-2 homologue was reported in another paper (see [19]). In mice, several isoforms of neuropilin-2 have been isolated: neuropilin-2a, neuropilin-2b, and at least three other neuropilin-2a isoforms with insertions of amino acids. This paper also reports that neuropilin-2a is expressed in embryonic tissues, including neural tissue, and distributes in a mostly complementary manner to neuropilin-1 (see [24]). The paper also shows that neuropilin-1 can bind Sema III, Sema E and Sema IV, whereas neuropilin-2 binds Sema E and Sema IV but not Sema III. On the bases of these findings, the authors propose that the specificity of action of different semaphorin members to different neuron classes is determined by differential expression of neuropilin family members, even though the role of neuropilin-2 in semaphorin signaling has not yet been determined.
    • of outstanding interest Chen H, Chédotal A, He Z, Goodman CS, Tessier-Lavigne M. Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. Neuron. 19:1997;547-559 This paper reports a new member of the neuropilin family, neuropilin-2, in mice. A rat neuropilin-2 homologue was reported in another paper (see [19]). In mice, several isoforms of neuropilin-2 have been isolated: neuropilin-2a, neuropilin-2b, and at least three other neuropilin-2a isoforms with insertions of amino acids. This paper also reports that neuropilin-2a is expressed in embryonic tissues, including neural tissue, and distributes in a mostly complementary manner to neuropilin-1 (see [24]). The paper also shows that neuropilin-1 can bind Sema III, Sema E and Sema IV, whereas neuropilin-2 binds Sema E and Sema IV but not Sema III. On the bases of these findings, the authors propose that the specificity of action of different semaphorin members to different neuron classes is determined by differential expression of neuropilin family members, even though the role of neuropilin-2 in semaphorin signaling has not yet been determined.
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    • Secreted chick semaphorins bind recombinant neuropilin with similar affinities but different subsets of neurons in situ
    • of special interest. The authors produced AP-tagged Coll-1, Coll-2, Coll-3, and Coll-5, and then tested their binding to tissue sections and recombinant neuropilin (neuropilin-1) protein. All of the AP-tagged collapsins bound to recombinant neuropilin-1 protein with similar affinities, whereas each collapsin exhibited a different binding profile in neuronal tissue. The authors also report that the carboxyl tail of each collapsin binds strongly to neuropilin-1 even though the profile of its binding to tissue sections is not specific for each collapsin member. In contrast, the semaphorin domain binds to tissue sections in a pattern specific for each collapsin.
    • of special interest Feiner L, Koppel AM, Kobayashi H, Raper J. Secreted chick semaphorins bind recombinant neuropilin with similar affinities but different subsets of neurons in situ. Neuron. 19:1997;539-545 The authors produced AP-tagged Coll-1, Coll-2, Coll-3, and Coll-5, and then tested their binding to tissue sections and recombinant neuropilin (neuropilin-1) protein. All of the AP-tagged collapsins bound to recombinant neuropilin-1 protein with similar affinities, whereas each collapsin exhibited a different binding profile in neuronal tissue. The authors also report that the carboxyl tail of each collapsin binds strongly to neuropilin-1 even though the profile of its binding to tissue sections is not specific for each collapsin member. In contrast, the semaphorin domain binds to tissue sections in a pattern specific for each collapsin.
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    • of outstanding interest. This paper reports the phenotype of the Sema III mutant mouse, which was generated by targeted disruption of the Sema III gene. Sema III mutant mouse embryos exhibit a similar abnormality in the PNS as that observed in neuropilin-1 mutant mouse embryos (see [20]), even though the Sema III mutant mouse is viable after birth. This paper also reports the production of heterozygous knocked-in lacZ mice in which the lacZ gene was inserted into the Sema III locus, and shows that PNS axons avoid the lacZ-expressing areas. These findings indicate that Sema III is a chemorepulsive guidance signal for PNS axons in vivo.
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    • 165, containing exon 7) can bind to neuropilin-1 and neuropilin-2. Exon 7 of VEGF is a neuropilin-binding site, but has no sequence similarity to Sema III. The authors also report that co-expression of KDR (a high-affinity tyrosine kinase receptor) and neuropilin-1 in cells lacking endogenous VEGF receptors results in enhancement of the ability of VEGF to bind to KDR and increases mitogenic activity and chemotaxis toward gradients of VEGF, whereas there is no chemotaxis of parental PEA or PEA - neuropilin-1 toward VEGF. These findings suggest that neuropilin-1 acts as a co-receptor that activates VEGF signaling, even though its role in vasculo-angiogenesis is not yet known.
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