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Estimation of transpalatal nasalance during production of voiced stop consonants by noncleft speakers using an oral-nasal mask.

OBJECTIVE: Our objective was to estimate nasalance due to transpalatal transfer of acoustic energy during production of voiced stop consonants by noncleft speakers. We also determined the relationship between the transpalatal nasalance and fundamental frequency (F0) of the speakers. METHOD: Participants were 8 men and 10 women (mean age = 21.9 years, SD = 4.0) without cleft palate who produced voiced stop (/b d g/) and nasal (/m n eta/) consonants in syllables embedded in a carrier phrase. Participants also read the Zoo Passage. A divided OroNasal Nasality System mask was used to simultaneously obtain acoustic nasalance and airflow during production of the consonants. Both F0-derived and first formant (F1)-derived nasalance were computed. RESULTS: F0-derived and F1-derived peak nasalance across all speakers ranged from a low of 20% to a high of 80% during production of stop consonants. An estimate of error from the combined sources of transoral transfer of energy (5%) and acoustic crossover between microphones (15%) was no greater than 20%. Analysis of variance revealed no significant effects of the sex of the speakers for either F0-derived or F1-derived nasalance of stops. There was a significant effect of the place of stop production for F0-derived nasalance (p;th< .05). Nonsignificant but positive correlations were found between the F0 of the speakers and F0-derived (r = .25) and F1-derived (r = .45) nasalance. CONCLUSIONS: Transpalatal transfer of oral acoustic energy accounts for most nasalance obtained during production of voiced stop consonants by noncleft speakers. F1-derived nasalance appears to better reflect transpalatal effects. Clinical implications are discussed.

Acoustics↗

Biology and pathological associations of the human papillomaviruses: a review.

Historical cottontail rabbit papillomavirus studies raised early indications of a mammalian DNA oncogenic virus. Today, molecular cloning recognises numerous animal and human papillomaviruses (HPVs) and the development of in vitro transformation assays has escalated oncological research in HPVs. Currently, their detection and typing in tissues is usually by Southern blotting, in-situ hybridization and polymerase chain reaction methods. The complete papillomavirus virion constitutes a protein coat (capsid) surrounding a circular, double-stranded DNA organised into coding and non-coding regions. 8 early (E1-E8) open reading frames (ORFs) and 2 late (L1, L2) ORFs have been identified in the coding region of all papillomaviruses. The early ORFs encode proteins which interact with the host genome to produce new viral DNA while late ORFs are activated only after viral DNA replication and encode for viral capsid proteins. All papillomaviruses are obligatory intranuclear organisms with specific tropism for keratinocytes. Three possible courses of events can follow papillomaviruses entry into cells: (1) viral DNA are maintained as intranuclear, extrachromosomal, circular DNA episomes, which replicates synchronously with the host cell, establishing a latent infection; (2) conversion from latent into productive infection with assembly of complete infective virions; (3) integration of viral DNA into host cellular genome, a phenomenon seen in HPV infections associated with malignant transformation. Human papillomaviruses (HPVs) essentially induce skin and mucosal epithelial lesions. Various skin warts are well known to be HPV-associated (HPVs 1, 2, 3, 7 and 10). Besides HPVs 3 and 10, HPVs 5, 8, 17 and 20 have been recovered from Epidermodysplasia verruciformis lesions. Anogenital condyloma acuminatum, strongly linked with HPVs 6 and 11 are probably sexually transmitted. The same HPVs, demonstrable in recurrent juvenile laryngeal papillomas, are probably transmitted by passage through an infected birth canal. HPVs described in uterine cervical lesions are generally categorized into those associated with high (16, 18), intermediate (31, 33, 35, 39, 45, 51, 52, 56, 58, 59, 68) and low (6, 11, 26, 40, 42, 43, 44, 53, 54, 55, 62, 66) risk of cervical squamous carcinoma. Cervical adenocarcinoma, clear cell carcinoma and small cell neuroendocrine carcinoma have also been linked to HPVs, especially HPV18. Other lesions reported to be HPV-associated are: papillomas, dysplasia and carcinomas in the nasal cavity (HPV 6, 11, 57); squamous papilloma, condyloma acuminatum, and verruca vulgaris of the oral cavity (HPV 6, 11), oral focal epithelial hyperplasia (HPV 13, 32); warty lip lesions (HPV 2): and conjunctival papillomas (HPV 6, 11).

Animals↗

Cloning, sequence analysis and expression pattern of mouse desmocollin 2 (DSC2), a cadherin-like adhesion molecule.

Desmocollins are cadherin-like adhesion molecules of desmosomes. We have determined the full cDNA sequence of a murine desmocollin, the homologue of human and bovine type 2 desmocollins (DSC2), and studied its tissue distribution and expression in stratified epithelia. An 8.5 day mouse embryo cDNA library was screened yielding overlapping clones which encoded the mouse DSC2. This gene has an open reading frame of 2710 base pairs (bp) encoding a polypeptide of 902 amino acids (aa). The polypeptide comprises a signal peptide, a precursor peptide, and a mature protein of 766 aa having an extracellular domain of 549 aa, a single transmembrane domain and a cytoplasmic domain of 184 aa. Like other desmocollins, murine DSC2 has two products, Dsc2a and Dsc2b, produced by alternative splicing of a 46 bp exon which encodes 11 COOH-terminal aa followed by an in-frame stop codon. Inclusion of this exon forms Dsc2b which is 54 aa shorter than Dsc2a. Mouse Dsc2a shows 75.7% amino acid identity to human and 63.3% identity to bovine Dsc2a. The mouse desmocollin is also homologous to the cadherins; 32.2% to the most closely related typical cadherin, human N-cadherin. DSC2 is ubiquitously expressed in epithelial tissues and the heart of adult mice and from the blastocyst stage of development. In situ hybridization shows that the gene is most strongly expressed suprabasally in stratified epithelia, similar to the expression of bovine DSC2.

Amino Acid Sequence↗