neuropeptide-y and Foot-Diseases

neuropeptide-y has been researched along with Foot-Diseases* in 2 studies

Other Studies

2 other study(ies) available for neuropeptide-y and Foot-Diseases

ArticleYear
Neuropeptide- and tyrosine hydroxylase-immunoreactive nerve fibers in painful Morton's neuromas.
    Muscle & nerve, 2000, Volume: 23, Issue:8

    We examined the expression of three neuropeptides that have been implicated in nociceptive transmission, and the sympathetic nerve fiber marker tyrosine hydroxylase, in 11 painful human Morton's neuromas, using immunohistochemistry. Antibodies against the neural markers RT97 and PGP 9.5 were used to map the general nerve fiber organization of the neuromas. Four specimens of normal human peripheral nerves were used as controls. Substance P, calcitonin gene-related peptide, and neuropeptide Y immunoreactivities were more pronounced in neuroma tissue than in control nerves. Neuropeptide immunofluorescence was seen both in larger nerve fiber trunks and in masses of disorganized axon profiles dispersed in loose connective tissue. Tyrosine hydroxylase immunoreactivity was present at varying levels of expression in neuroma nerve fiber trunks, in connective tissue nerve fiber bundles, and around some blood vessels. Our findings suggest that neuropeptides are involved in the response to injury in Morton's neuromas and that they could play a role in initiation or modulation of pain. In addition, pain from Morton's neuromas could be influenced by sympathetic nerve fibers.

    Topics: Adult; Aged; Antibodies; Calcitonin Gene-Related Peptide; Cell Communication; Female; Foot Diseases; Humans; Male; Middle Aged; Nerve Fibers; Neuroma; Neurons, Afferent; Neuropeptide Y; Neuropeptides; Pain; Substance P; Sympathetic Nervous System; Thiolester Hydrolases; Tyrosine 3-Monooxygenase; Ubiquitin Thiolesterase

2000
The structure, innervation and location of arteriovenous anastomoses in the equine foot.
    Equine veterinary journal, 1994, Volume: 26, Issue:4

    In the foot of the horse, arteriovenous anastomoses (AVAs) of epithelioid type occurred in the dermis of the coronary band, in the coronary and terminal papillae, in neurovascular bundles and at the entrance to and along the length of the dermal laminae. A particular feature of the epithelioid segment of AVAs in the horse, compared with that of other species, was the height and surface complexity of many of the endothelial cells. They extended into the lumen, forming undercut and tunnel-like areas which correlated with the characteristic surface marking of AVAs observed in vascular casts. The number of cell organelles, including the concentration of vesicles in the luminal cytoplasm, suggested cells with a high metabolic activity. The luminal surface possessed numerous microvilli and long cytoplasmic cell processes which appeared to surround material in the lumen. The innervation of AVAs was more dense than that of the arteries and consisted of adrenergic and peptidergic nerves. Noradrenaline- and neuropeptide Y-containing nerves were identified as the vasoconstrictor components of the nerve supply and occurred along arteries and formed dense plexuses around AVAs. Calcitonin gene-related peptide, substance P and vasoactive intestinal polypeptide are vasodilators and were present in single nerve fibres which accompanied arteries and AVAs along the length of the dermal laminae. In this study the distribution, density and innervation of AVAs in the equine foot are correlated with their proposed role in the development of acute laminitis. The release of vasoactive peptides from diseased organs remote from the foot may induce inappropriate prolonged dilatation of AVAs and thus contribute to the laminar ischaemia of acute laminitis.

    Topics: Adrenergic Fibers; Animals; Arteriovenous Anastomosis; Calcitonin Gene-Related Peptide; Endothelium, Vascular; Female; Foot Diseases; Hoof and Claw; Horse Diseases; Horses; Immunohistochemistry; Male; Microscopy, Electron; Muscle, Smooth, Vascular; Neuropeptide Y; Norepinephrine; Substance P; Vasoactive Intestinal Peptide

1994