scholarly journals Laryngeal Cartilage

2020 ◽  
Author(s):  
Keyword(s):  
Laryngeal Cartilage

Surgical Management of Laryngeal Cartilage Fractures

2020 ◽  
Vol 71 (2) ◽  
pp. 102-102
Author(s):  
S. Chitose ◽  
K. Sato ◽  
H. Tanaka ◽  
M. Fukahori ◽  
T. Kurita ◽  
...  
Keyword(s):  
Surgical Management ◽  
Laryngeal Cartilage

scholarly journals Comparative Study between CT and MRI in Assessment of Laryngeal Cartilage Invasion in Laryngeal Carcinoma

2021 ◽  
Vol 89 (6) ◽  
pp. 873-880
Author(s):  
SHAIMA F. ELKHOLY, M.D.; MOHAMED A. KANDEEL, M.Sc. ◽  
MOMEN A. AMEEN HAMELA RAMY E. IBRAHIM ASAAD
Keyword(s):  
Comparative Study ◽  
Laryngeal Carcinoma ◽  
Laryngeal Cartilage ◽  
Cartilage Invasion ◽  
Ct And Mri

scholarly journals Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate

1992 ◽  
Vol 286 (3) ◽  
pp. 761-769 ◽  
Author(s):  
F P Barry ◽  
J U Gaw ◽  
C N Young ◽  
P J Neame
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Signal Peptidase ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Binding Region ◽  
Keratan Sulphate ◽  
Laryngeal Cartilage ◽  
Hyaluronan Binding

The hyaluronan-binding region (HABR) was prepared from pig laryngeal cartilage aggrecan and the amino acid sequence was determined. The HABR had two N-termini: one N-terminal sequence was Val-Glu-Val-Ser-Glu-Pro (367 amino acids in total), and a second N-terminal sequence (Ala-Ile-Ser-Val-Glu-Val; 370 amino acids in total) was found to arise due to alternate cleavage by the signal peptidase. The N-linked oligosaccharides were analysed by examining their reactivity with a series of lectins. It was found that the N-linked oligosaccharide on loop A was of the mannose type, while that on loop B was of the complex type. No reactivity was detected between the N-linked oligosaccharide on loop B' and any of the lectins. The location of keratan sulphate (KS) in the HABR was determined by Edman degradation of the immobilized KS-containing peptide. The released amino acid derivatives were collected and tested for the presence of epitope to antibody 5-D-4. On the basis of 5-D-4 reactivity and sequencing yields, the KS chains are attached to threonine residues 352 and 357. There is no KS at threonine-355. This site is not in fact in G1, but about 16 amino acid residues into the interglobular domain. Comparison of the structure of the KS chain from the HABR and from the KS domain of pig laryngeal cartilage aggrecan was made by separation on polyacrylamide gels of the oligosaccharides arising from digestion with keratanase. Comparison of the oligosaccharide maps suggests that the KS chains from both parts of the aggrecan molecule have the same structure.

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