High impact information on Laryngeal Cartilages

• The four-generation KF2-01 family present with dominant form of the KFS where the sequence of vertebral fusion was confined to the cervical spine (always including the C2-3 fusion and reduced expression of the C4-5 and C6-7 fusions) in association with malformation of laryngeal cartilages and mild-to-severe vocal impairment [1].
• The methods are used to determine the diffusion coefficients of oxygen and ruthenium(III) hexamine [Ru(NH3)6(3+)] in laryngeal cartilage [2].
• Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate [3].
• Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage [4].
• Proteoglycans from pig laryngeal cartilage prepared by dissociative extraction in guanidine hydrochloride were studied in dilute solution by light-scattering and ultracentrifugation [5].

Anatomical context of Laryngeal Cartilages

• Proteoglycans extracted with 4M-guanidinium chloride from pig laryngeal cartilage and bovine nasal septum were purified by density-gradient centrifugation in CsCl under 'associative' followed by 'dissociative' conditions [Hascall & Sajdera (1969) J. Biol. Chem. 244, 2384-2396] [6].
• These novel polypeptide hormones (CDMP-1 and CDMP-2) have not been previously reported in laryngeal cartilage chondrocytes [7].

Associations of Laryngeal Cartilages with chemical compounds

• Purified proteoglycans extracted from pig laryngeal cartilage in 0.15 M-NaCl and 4 M-guanidinium chloride were analysed and their amino acid compositions determined [8].
• Purified proteoglycans labelled either in the chondroitin sulphate chains or in the core protein were obtained from laryngeal cartilage by short-term organ culture [9].
• 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 [10].
• Primary structure of the hyaluronic acid-binding region of porcine laryngeal cartilage proteoglycan [11].
• Three-dimensional (3D) images of the laryngeal cartilages and bones, 3D airway surface models, and sequential coronal and axial images were reconstructed for assessment [12].

Gene context of Laryngeal Cartilages

• In the present work, the interaction of aggrecan, decorin and biglycan isolated from pig laryngeal cartilage and of the three squid cartilage proteoglycans with collagen type I and II was studied [13].
• The MMPs of normal and malignant human laryngeal cartilage and of biopsy specimens were identified immunochemically and by zymography using gelatin or casein as substrates [14].
• MATERIALS AND METHODS: The pretreatment CT studies of 119 patients with glottic SCC (T1, n=61; T2, n=40; T3, n=14; T4, n=4) treated with curative intent by radiation therapy were reviewed for tumoral involvement of specific laryngeal anatomic subsites (including laryngeal cartilages) [15].
• 18 cases of primarily glottic laryngeal SCC were graded according to the criteria outlined by Jakobsson et al., and assessed for the presence of infiltration of laryngeal cartilage [16].
• In general, overexpression of c-erb B-2 oncoprotein was related to the more aggressive tumors with high capability of invading laryngeal cartilages [17].

References