Temporal and spatial expression of alternative splice-forms of the α1(XI) collagen gene in fetal rat cartilage
| العنوان: | Temporal and spatial expression of alternative splice-forms of the α1(XI) collagen gene in fetal rat cartilage |
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| المؤلفون: | Gillian B.M. Davies, Lauri C. Hausafus, Julia Thom Oxford, Nicholas P. Morris, Barbara F. Smoody |
| المصدر: | Developmental Dynamics. 213:12-26 |
| بيانات النشر: | Wiley, 1998. |
| سنة النشر: | 1998 |
| مصطلحات موضوعية: | Gene isoform, Cartilage, Alternative splicing, Biology, Chondrogenesis, Cell biology, Collagen, type I, alpha 1, Exon, medicine.anatomical_structure, Biochemistry, RNA splicing, medicine, Endochondral ossification, Developmental Biology |
| الوصف: | Type XI collagen, a member of the group of fibrillar collagens, plays a regulatory role in the formation of the collagen fibril net- work in cartilage and consequently plays a pivotal role in the formation of the endochondral skeleton. The mechanism by which type XI colla- gen limits fibril growth appears to involve the large noncollagenous amino terminal domain. Complex alternative splicing occurs within this domain in two of the three constituent subunits, a1(XI) and a2(XI). In the a1(XI) chain, three alter- natively spliced exons encoding one very basic and two very acidic peptides generate six splice- forms and protein isoforms. In order to better understand the significance of this alternative splicing, we have examined fetal rat cartilage to determine: (a) the relationship between alterna- tive splicing and chondrogenesis in limb bud micromass culture; (b) the relative levels of expression of each of the splice-forms by ribo- nuclease protection; and (c) the distribution of splice-forms and protein isoforms by in situ hy- bridization and immunohistochemistry. The results indicate that the pattern of alternative splicing of the a1(XI) chain is tightly linked to chondrogenesis. The two most abundant splice- forms in fetal rib cartilage are vo, lacking all three exons, and v1b, containing the exon encod- ing the basic peptide. While most of the splice- forms show a general distribution in nasal, Meck- el's, and rib cartilage, v1b was restricted to the dorsal portion of the fetal rib. This distribution appears to correlate with the portion of the rib which will ultimately ossify, rather than with any of the differentiative states of chondrocytes. Together these results suggest that alternative splicing within the amino terminal domain of the a1(XI) chain may contribute to the function of type XI collagen and that expression of the basic v1b peptide may play a role in endochon- dral ossification. Dev. Dyn. 1998;213:12-26. |
| تدمد: | 1097-0177 1058-8388 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::47dd5d903ab17a9b188b168ffec1fe85 https://doi.org/10.1002/(sici)1097-0177(199809)213:1<12::aid-aja2>3.0.co;2-0 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi...........47dd5d903ab17a9b188b168ffec1fe85 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10970177 10588388 |
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