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Biomedical subjects

R D Terry

Publications and source records attributed to R D Terry.

At least 109 records · Page 6Linked to original sources
PubMed1979

Alzheimer neurofibrillary tangles: antiserum and immunohistological staining.

A 50,000-dalton polypeptide has been purified from fractions enriched with neurofibrillary tangles of paired helical filaments from human autopsy specimens of Alzheimer disease and senile dementia of the Alzheimer type. An antiserum to this polypeptide was raised in a rabbit. This antiserum formed an immunoprecipitation line with the purified antigen and with human neurotubules in ouchterlony double-diffusion plates. The reactivity of the anti-paired helical filament protein serum with neurofibrillary tangles was studied by immunofluorescence on cryostat sections of hippocampus from Alzheimer autopsy tissue and by the peroxidase-antiperoxidase technique on paraffin sections of an Alzheimer brain biopsy. The tangles were stained with the antiserum in both systems. Preimmune rabbit serum and unrelated hyperimmune sera, used as controls, did not stain the tangles. These results show that the 50,000-dalton polypeptide purified from the neurofibrillary tangle-enriched fractions is a constituent of Alzheimer neurofibrillary tangles and, perhaps, of the paired helical filaments of which the tangles are composed.

Alzheimer Disease↗
PubMed1978

Chemical relationship of the paired helical filaments of Alzheimer's dementia to normal human neurofilaments and neurotubules.

Intraneuronal fibrillary tangles are prominent features of several neurological diseases, including especially Alzheimer presenile and senile dementia, and to a much lesser degree in the normal aged human brain. These tangles are made up of abnormal fibrillar elements each about 22 nm at its widest, periodically reduced to 10 nm at about every 80 nm. Each abnormal fiber seems to be a pair of 10 nm filaments helically wound around each other. In this study the protein subunit of these paired helical filaments isolated from cases of Alzheimer's dementia was compared with the major protein subunits of normal neurofilaments and neurotubules by two-dimensional peptide maps of the tryptic or chymotryptic digests of these proteins labelled with 125I. The paired helical filament protein is very similar in its peptide maps to identically treated major neurofilament protein and to the beta monomer of neurotubule, while it is not so similar to the alpha tubulin. These data suggest that the paired helical filament protein subunit is closely related chemically to the normal neurofilament protein subunit, and the beta tubulin.

Alzheimer Disease↗
PubMed1978

Disuse atrophy of skeletal muscle. A morphometric study using image analysis.

A morphometric study of disuse atrophy was done on the rat anterior tibilalis muscle over a 13-day period after immobilization of the hind leg by pinning the knee and ankle joints. Cross-sectional areas of individual muscle fibers were measured using image analysis, a new and precise technique. Three types of muscle fibers, light, medium and dark, were defined using a modified myosin-ATPase reaction on cryostat-cut sections. Each of the 3 fiber types was found to show a degree and time course of atrophy unique to itself. At the 0.01 confidence level, the dark fibers (with strongest ATPase reaction) did not shrink significantly. Both the light (ATPase negative) and medium fiber did show significant atrophy at that level; the light shrinking more than the medium. Simple visualization of the light microscopic images was often found to be misleading. Thus, the need was documented for a precise technique for analysis of fiber size distribution.

Animals↗
PubMed1978

Senile dementia.

The Alzheimer type of senile dementia (SDAT) accounts for more than 50% of such cases, and is a very common disorder as well as being very costly in emotional, economic, and medical terms. It carries a markedly shortened life expectancy. Gray-to-white-matter ratios change and the brain shrinks slightly in the course of normal aging, but SDAT brains may not be significantly more atrophic than are normal controls. Cortical neurons are diminished in number in normal aging, but counts from frontal and midtemporal regions of SDAT specimens are not different from age-matched controls. There is loss of dendrites and of dendritic spines in both normal and abnormal aged specimens. Neurofibrillary tangles are made up of paired helical filaments that appear to be chemically and immunologically related to normal neurofibers. Neuritic plaques are made up of an amyloid core surrounded by abnormal axonal endings. Both plaques and tangles are to be correlated with the presence of senile dementia. There is some evidence for an infectious etiology of SDAT. Choline acetyltransferase is markedly reduced in cortical tissue of these patients, but the muscarinic receptors of acetylcholine are normal.

Aging↗
PubMed1976

Neurofibrillary tangles of paired helical filaments.

The abnormal aggregates of fibrillar material found in neurons in Alzheimer's disease, senile dementia, the Guam Parkinsonism-Dementia complex, Down's syndrome, and postencephalitic Parkinsonism were studied by means of tilt-stage electron microscopy and with X-ray images of scale models of a bifilar helix. The model fulfills the structural criteria established by electron microscopy. These studies showed that the "twisted tubule" which makes up the neurofibrillary tangle in many pathological situations is a bifilar helix made up of 130 A filaments.

Alzheimer Disease↗
PubMed1976

Retroperitoneal ganglioneuroblastoma: a kaleidoscope of neuronal degeneration. A light and electron microscopic study.

The light and electron microscopic features of an unique retroperitoneal ganglioneuroblastoma in a four-year-old female are described. The unprecedented concurrence of Hirano, zebra, membranous cytoplasmic (MCB), and Pick bodies in the same population of neoplastic, sympathetic ganglion cells provides further evidence for their non-specificity. Although the pathogenesis of the membranous cytoplasmic bodies in this tumor is unclear, they ostensibly arise within endoplasmic cisterns, similar to the proposed origin of membranous cytoplasmic bodies in Tay-Sachs disease. Both the apparent continuum between argyrophilic bodies and central chromatolysis, and the incorporation of various cytoplasmic constituents within neurofilamentous proliferations reflect some of the dynamic factors involved in the formation of Pick bodies.

Cell Count↗
PubMed1976

Lack of amyloidosis and renal disease in A strain mice.

Amyloid deposition in two sublines of the A strain mouse, a reputedly reliable murine model of spontaneous amyloidosis, was reevaluated using combined green polarization birefringence after Congo red staining and a fibrillar ultrastructure for amyloid identification. Both sublines were found to be devoid of amyloid at an age when the A strain mouse had been reported to have a high incidence of papillonephritis, amyloidosis, and death. This finding indicates a need for reassessment of this and other traditional models of spontaneous amyloidosis.

Adrenal Glands↗
PubMed1975

Chemical pathology of neurofibrils. Neurofibrillary tangles of Alzheimer's presenile-senile dementia.

A subcellular fraction enriched in twisted tubules was obtained by differential centrifugation of a homogenate of neurons isolated from areas of the brain with many neurofibrillary tangles from patients with Alzheimer's presenile-senile dementia. A unique protein (molecular weight 50,000 daltons) which does not co-migrate with either of the two tubulin monomers of the major neurofilament protein, both purified from human brain, was found in this subcellular fraction on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Similarly processed tissue from areas of the brain poor in neurofibrillary tangles contained low levels of this new protein. The new protein band could not be seen in control patients.

Alzheimer Disease↗