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I McKinnell

Publications and source records attributed to I McKinnell.

4 recordsLinked to original sources
PubMed2005

Dynamic Id2 expression in the medial and lateral domains of avian dermamyotome.

Id2 cDNA was isolated from a subtractive screen of stage-12 quail caudal somites. In situ hybridisation analysis identified the previously un-described expression of Id2 mRNA in distinct medial and lateral domains of the somitic dermamyotome in both quail and chick embryos. Id2 expression in somites was highly dynamic being first initiated in the lateral domain of the dermamyotome of stage-8-10 embryos, followed by expression in a separate medial domain. Id2 mRNA during subsequent embryonic development could be detected in both medial and lateral domains in the anterior to mid regions while the posterior, recently segmented somites, showed expression only in the lateral domain, which was eventually down regulated in the anterior-most somites. Tissue manipulation studies revealed that Id2 expression in somites required positive signalling from not only axial structures and lateral plate mesoderm but also surface ectoderm. In addition, Id2 expression was also observed in anterior and posterior domains of developing avian limb buds and interdigital tissue.

Animals↗
PubMed2004

BMP controls nitric oxide-mediated regulation of cell numbers in the developing neural tube.

Balanced cell proliferation and cell death determines neural precursor cell numbers in early stages of neural tube (NT) development. We have previously shown that nitric oxide (NO) regulates cell numbers locally in the NT of eight to 12 somite embryos. Here, we demonstrate that bone morphogenetic protein-4 (BMP-4), which is expressed in the ectoderm and dorsal NT at these developmental stages, induces programmed cell death (PCD) and promotes entry into the S-phase, via nitric oxide synthase (NOS) activity. These effects can be reversed by BMP-4 antagonists, such as follistatin and noggin, or by specific NOS inhibitors, resulting in low NO levels that facilitate mitosis and reduce PCD. Ectopic BMP-4 induction of PCD is restricted to the dorsal NT, whereas promotion of the S-phase is evenly observed across the dorsal-ventral (D-V) axis. Prolonged exposure to either BMP-4 or NOS inhibitors, which results in high or low NO levels, respectively, causes NT defects. The results presented here throw new light on the BMP signaling pathway. The local presence of BMP-4 helps to regulate cell numbers in the developing NT by a NO-mediated pathway, which is essential for normal NT formation.

Animals↗
PubMed1999

Retinotectal ligands for the receptor tyrosine phosphatase CRYPalpha.

The cell adhesion molecule-like tyrosine phosphatase CRYPalpha is localized on retinal axons and their growth cones. We present evidence that two isoforms of this type IIa phosphatase, CRYPalpha1 and CRYPalpha2, have extracellular ligands along the developing retinotectal pathway. Using alkaline phosphatase fusion proteins containing the CRYPalpha1 ectodomain, we detect a prominent ligand on basement membranes of the early retina, optic stalk, and chiasm. A second ligand is observed in the endfeet region of radial processes in the developing stratum opticum, the site of initial retinal axon invasion. This latter ligand binds CRYPalpha2 preferentially. Further ligand interactions are detected for both CRYPalpha protein isoforms in retinorecipient tectal laminae and on retinal fibers themselves. CRYPalpha thus has cell- and matrix-associated ligands along the entire retinotectal projection. Moreover, these ligands appear to be heterotypic and interact with CRYPalpha through both its immunoglobulin and fibronectin type III regions. The anteroposterior levels of the ligands are relatively uniform within the retina and tectum, suggesting that the CRYPalpha protein within retinal axons does not directly recognise topographically graded guidance cues. We propose that CRYPalpha may have a permissive role in promoting retinal axon growth across the eye and tectum and that its functions are modulated temporally and spatially by isoform-specific interactions with cell- and matrix-associated ligands.

Alkaline Phosphatase↗