Journal
JOURNAL OF EXPERIMENTAL BIOLOGY
Volume 220, Issue 18, Pages 3327-3335Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jeb.163824
Keywords
Fibrillar collagen; X-ray diffraction; Microscopy; Soft; coral; D-period; Red Sea
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Funding
- US Department of Energy, Basic Energy Sciences, Office of Science [W-31-109-ENG-38]
- National Institutes of Health [RR-08630]
- DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
- National Institute of General Medical Sciences of the National Institutes of Health [R24GM111072]
- National Science Foundation [MCB-0644015 CAREER]
- US Army Research Laboratory
- US Army Research Office [W911NF-11-2-0018-P00002]
- Israeli Ministry of Science [00040047000]
- Israel Cohen Chair in Environmental Zoology
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR008630] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R24GM111072, P41GM103622] Funding Source: NIH RePORTER
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We report here the biochemical, molecular and ultrastructural features of a unique organization of fibrillar collagen extracted from the octocoral Sarcophyton ehrenbergi. Collagen, the most abundant protein in the animal kingdom, is often defined as a structural component of extracellular matrices in metazoans. In the present study, collagen fibers were extracted from the mesenteries of S. ehrenbergi polyps. These fibers are organized as filaments and further compacted as coiled fibers. The fibers are uniquely long, reaching an unprecedented length of tens of centimeters. The diameter of these fibers is 9 +/- 0.37 mu m. The amino acid content of these fibers was identified using chromatography and revealed close similarity in content to mammalian type I and II collagens. The ultrastructural organization of the fibers was characterized by means of high-resolution microscopy and X-ray diffraction. The fibers are composed of fibrils and fibril bundles in the range of 15 to 35 nm. These data indicate a fibrillar collagen possessing structural aspects of both types I and II collagen, a highly interesting and newly described form of fibrillar collagen organization.
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