Type II collagen distribution in rodents.

The anatomical distribution of type II collagen in animal ears was studied by immunohistochemical techniques, using defined monoclonal antibodies to type II collagen. Type II collagen was observed in the cartilage plate of the auricle and external auditory meatus, tympanic annulus, lamina propria of tympanic membrane (pars tensa), interossicular joints, stapes footplate, eustachian tube cartilage, enchondral layer and globuli interossei of the otic capsule, Rosenthal canal, cribriform base, osseous spiral lamina, spiral ligament, limbus, tectorial membrane, semicircular canal membrane and subepithelial layer of the ampullary crista, utricular and saccular maculae, and the endolymphatic duct and proximal part of the sac.

Sleep apnea in narcolepsy.

Polysomnographic and multiple sleep latency studies documented recurrent apneic episodes during NREM sleep stages 1 and 2 and REM sleep in 11 of 16 narcoleptic patients. Episodes were predominantly central, but obstructive and mixed events were also observed. Apneas were accompanied by mild to moderate oxygen desaturation.

Comparison of aortic and ear cartilage tropoelastins isolated from lathyritic pigs.

Tropoelastin was isolated from aortae and auricular cartilage obtained from lathyritic piglets. The two tissue-specific tropoelastins were judged homogeneous by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration on a high-pressure liquid chromatograph. Comparative studies of the tropoelastins were performed. Amino acid analysis revealed that the aortic and cartilage tropoelastins were very similar, if not identical, with the only exception that the cartilage tropoelastin contained more hydroxyproline and less lysine residues, both of which can be attributable to post-translational modifications. Both tropoelastins possess an apparent molecular weight of 70 000 and exhibit similar peptide fragments with limited trypsin cleavage. Antiserum raised to the aortic tropoelastin was used to show immunological identity between the two tissue tropoelastins.

Effect of diphosphonates on glycogen content of rabbit ear cartilage cells in culture.

The diphosphonates dichloromethanediphosphonate (Cl2MDP) and to a minor degree 1-hydroxyethane-1,1-diphosphonate (EDHP) increased the glycogen content in cultured cartilage cells of rabbit ear. This effect was not due to different concentrations of glucose in the medium.

The effect of frequency tolerance on audiometer accuracy.

Investigations into the methods used to calibrate audiometers reveal that the 6 000 Hz frequency is particularly liable to yield inconsistent results when calibrated in the usual way. It is shown that the TDH39 telephone receiver which is usually calibrated on a 9A coupler in accordance with the International Standards Organization recommendation R389 will depend to a considerable extent on the precise frequency used and may differ by as much as 7 db when the frequency is varied but still retained within the specified tolerance limits. A new telephone receiver, the TDH50, is much less sensitive to frequency variation. It is shown that this receiver should be calibrated with the same threshold figures as the TDH39.

Further evidence for the presence of androgen receptors in the lungs and in the head appendages of the cock.

The presence of cytoplasmic dihydrotestosterone receptors in the lungs, the comb, the wattle, and the ear lobes of the cock was demonstrated by sucrose density-gradient centrifugation. All these tissues exhibited saturable 'in vitro' binding of dihydrotestosterone in the 8-11S region of the gradient. When 0.5 M KCl was added to the lung, wattle, and comb cytosol and to the gradients, the radioactive dihydrotestosterone migrated in the 4-5S region. These studies suggest that the mechanism of action of androgens in the head appendages of the cock and in other target tissues is similar.

The distribution of different molecular species of collagen in fibrous, elastic and hyaline cartilages of the pig.

The distribution of type II collagen, considered to be characteristic of cartilaginous tissues, was determined in various specialized cartilages of the mature pig. The tissues examined were: (1) fibrocartilage of the semilunar meniscus of the knee; (2) elastic cartilage of the external ear; (3) hyaline cartilage of (a) the synovial joint (b) the thyroid plate of the larynx, and (c) the nasal septum. The predominant species of collagen in each tissue, whether type I or type II, was appraised semi-quantitatively by analysis of purified collagen solubilized by pepsin and of peptide fragments produced by cyanogen bromide. Cyanogen bromide-derived peptides were characterized by column chromatography on CM-cellulose and by electrophoresis in sodium dodecyl sulphate-polyacrylamide gels. The proportion of each type of collagen was determined precisely by isolating the homologous small peptides alpha1(II)CB6 [nomenclature of Miller (1973) Clin. Orthop. 92, 260-280], by column chromatography on phosphocellulose and determining their relative proportions by amino acid analysis. Thus collagen of the fibrocartilage of the meniscus proved to be all type I; type II was not detected. In contrast, collagen of elastic cartilage of the outer ear, after rigorous exclusion of perichondrium, was type II. Similarly, type II was the only collagen detected in all the mature hyalline cartilages examined.