1. Comparative studies on the extractability of collagen from aortas of stroke-prone spontaneously hypertensive and normotensive rats
- Author
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Toshinobu Takashima, Noboru Fujitani, Sueo Matsumura, Hideaki Higashino, Noribumi Ikeda, and Michio Muguruma
- Subjects
Male ,Aging ,medicine.medical_specialty ,Protein Conformation ,Aorta, Thoracic ,Peptide ,Rats, Inbred WKY ,Acetic acid ,chemistry.chemical_compound ,Hydrolysis ,Species Specificity ,Pepsin ,Rats, Inbred SHR ,Internal medicine ,medicine.artery ,medicine ,Animals ,Aorta, Abdominal ,Cyanogen Bromide ,Molecular Biology ,Incubation ,chemistry.chemical_classification ,Aorta ,biology ,Pepsin A ,Rats ,Cerebrovascular Disorders ,Spectrometry, Fluorescence ,Endocrinology ,chemistry ,Biochemistry ,Urea ,biology.protein ,Molecular Medicine ,Cyanogen bromide ,Collagen - Abstract
The molecular states of collagen in the aortas of age-matched stroke-prone spontaneously hypertensive (SHRSP) and normotensive Wistar Kyoto rats (WKY) were studied by analyzing its extractability under defined conditions. The monomeric and oligomeric collagen extractable with 0.5 M acetic acid/6 M urea from aortic homogenates of 9-month-old SHRSP and WKY comprised approx. 0.6 and 2.0%, respectively, of the total collagen. On incubation of the acetic acid/urea-extracted residues with pepsin at 4 degrees C, the levels of the collagen alpha 1(I) and alpha 2(I) chains solubilized from the SHRSP residues were both less than 50% of those from the WKY residues. When the residues were incubated with pepsin at 15 or 25 degrees C, the differences became smaller. When the acetic acid/urea residues were hydrolyzed with cyanogen bromide, nearly identical peptide maps were obtained for SHRSP and WKY. The aortas from 2-month-old SHRSP and WKY contained much larger proportions of acid/urea-extractable collagen than those of the older rats (8.2 and 13% of the respective total collagen). The levels of the alpha 1(I) and alpha 2(I) chains solubilizable from the respective residues by pepsin at 4 degrees C were similar to each other. These results indicate that aortic collagen fibrils in SHRSP are stiffened more prominently than those in WKY.
- Published
- 1992
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