Murine semaphorin D/collapsin is a member of a diverse gene family and creates domains inhibitory for axonal extension

نویسندگان

  • Andreas W Püschel
  • Ralf H Adams
  • Heinrich Betz
چکیده

Members of the collapsin/semaphorin gene family have been proposed to act as growth cone guidance signals in vertebrates and invertebrates. To identify candidate molecules involved in axonal pathfinding during mouse embryogenesis, we isolated cDNAs encoding five new members of the semaphorin family (Sem A-Sem E). The murine semaphorin genes are differentially expressed in mesoderm and neuroectoderm before and during the time when axons select their pathways in the embryo. In explant cultures, recombinant Sem D/collapsin converts a matrix permissive for axonal growth into one that is inhibitory for neurites of peripheral ganglia. Our data demonstrate that semaphorins are a diverse family of molecules that may provide local signals to specify territories nonaccessible for growing axons.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Critical Role of Collapsin Response Mediator Protein- associated Molecule CRAM for Filopodia and Growth Cone Development in Neurons□D

Collapsin response mediator proteins (CRMPs) have been implicated in signaling of axonal guidance, including semaphorins. We have previously identified a unique member of this gene family, CRMP-associated molecule CRAM (CRMP-5), which is phylogenetically divergent from the other four CRMPs. In this study, we have examined the distribution and function of CRAM in developing neurons. Immunohistoc...

متن کامل

Neuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites.

The collapsin and semaphorin family of extracellular proteins contributes to axonal path finding by repulsing axons and collapsing growth cones. To explore the mechanism of collapsin-1 action, we expressed and purified a truncated collapsin-1-alkaline phosphatase fusion protein (CAP-4). This protein retains biological activity as a DRG growth cone collapsing agent and saturably binds to DRG neu...

متن کامل

Secreted Chick Semaphorins Bind Recombinant Neuropilin with Similar Affinities but Bind Different Subsets of Neurons In Situ

Collapsin-1, a member of the semaphorin family, activates receptors on specific growth cones, thereby inhibiting their motility. Neuropilin, a previously cloned transmembrane protein, has recently been identified as a candidate receptor for collapsin-1. We have completed the cloning of chick collapsin-3 and -5 and show that collapsin-1, -2, -3, and -5 bind to overlapping but distinct axon tract...

متن کامل

Critical role of collapsin response mediator protein-associated molecule CRAM for filopodia and growth cone development in neurons.

Collapsin response mediator proteins (CRMPs) have been implicated in signaling of axonal guidance, including semaphorins. We have previously identified a unique member of this gene family, CRMP-associated molecule CRAM (CRMP-5), which is phylogenetically divergent from the other four CRMPs. In this study, we have examined the distribution and function of CRAM in developing neurons. Immunohistoc...

متن کامل

Critical Role of CRMP-Associated Molecule CRAM for Filopodia and Growth Cone Development in Neurons

Collapsin response mediator proteins (CRMPs) have been implicated in signaling of axonal guidance including Semaphorins. We have previously identified a unique member of this gene family, CRMP-associated molecule CRAM (CRMP-5) which is phylogenetically divergent from the other four CRMPs. In this study we have examined the distribution and function of CRAM in developing neurons. Immunohistochem...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Neuron

دوره 14  شماره 

صفحات  -

تاریخ انتشار 1995