The Formation of Collagen Hydroxylysine Studied with Tritiated Lysine.
نویسندگان
چکیده
Hydroxylysine was first isolated from gelatin (2) and probably does not occur in proteins of mammalian origin other than collagen (3). In rats, dietary lysine is an obligatory precursor of the hydroxylysine of collagen (4-7); when 14C-labeled lysine is either fed or given by injection it is incorporated into both the lysine and hydroxylysine of collagen, whereas labeled hydroxylysine is not incorporated int,o collagen at all (8). Since, very shortly after the injection of i4C-lysine into rats, the specific activity of hydroxylysine of skin collagen is exactly the same as that of collagen lysine, and since it remains the same for as long as 3 months (7), the hydroxylation of lysine must take place before it is incorporated into insoluble collagen. Recent reports from other laboratories (9, 10) make it seem probable that the hydroxylation of proline takes place after the amino acid is incorporated into a peptide chain, but before the peptide chain leaves the ribosome. It is possible that the hydroxylation of lysine takes place at the same time. The studies described in the present report were designed to aid in the understanding of the mechanism of the conversion of lysine to hydroxylysine. Conceivable mechanisms by which lysine could be hydroxylated are as follows. (a) Direct uptake of an oxygen atom on carbon 5 of the lysine chain
منابع مشابه
The Formation of Collagen Hydroxylysine Studied with Tritiated Lvsine*
Hydroxylysine was first isolated from gelatin (2) and probably does not occur in proteins of mammalian origin other than collagen (3). In rats, dietary lysine is an obligatory precursor of the hydroxylysine of collagen (4-7); when 14C-labeled lysine is either fed or given by injection it is incorporated into both the lysine and hydroxylysine of collagen, whereas labeled hydroxylysine is not inc...
متن کاملFurther studies on the effect of the collagen triple-helix formation on the hydroxylation of lysine and the glycosylations of hydroxylysine in chick-embryo tendon and cartilage cells.
The hydroxylation of lysine and glycosylations of hydroxylysine were studied in isolated chick-embryo tendon and cartilage cells under conditions in which collagen triple-helix formation was either inhibited or accelerated. The former situation was obtained by incubating the tendon cells with 0.6mm-dithiothreitol, thus decreasing their proline hydroxylase activity by about 99%. After labelling ...
متن کاملThe formation of collagen hydroxylysine.
The sole source of hydroxylysine in the skin collagen of rats has been found to be lysine (1, 2). Rats fed W-labeled lysine showed the same Cl4 specific activity in the hydroxylysine as in the lysine isolated from skin collagen (1). Labeled hydroxylysine, when injected into rats, was not incorporated into the collagen (2). To find whether hydroxylation of lysine is completed at the time of inco...
متن کاملHydroxylation of lysine and glycosylation of hydroxylysine during collagen biosynthesis in isolated chick-embryo cartilage cells.
Hydroxylation of lysine and glycosylation of hydroxylysine during collagen biosynthesis in isolated chick-embryo cartilage cells were studied by using continuous labelling and pulse-chase labelling experiments with [14C]lysine. Control experiments with [14C]proline indicated that in continuous labelling the hydroxylation of [14C]proline became linear with time after about 4 min and the secretio...
متن کاملThe source and state of the hydroxylysine of collagen. II. Failure of free hydroxylysine to serve as a source of the hydroxylysine or lysine of collagen.
The amino acid 5-hydroxylysine, first isolated from gelatin (2), has been found absent in all types of proteins other than collagen that have been examined (3). It is not an essential amino acid for animal nutrition (4), and hence must be formed from other material in the animal body. Previous papers from this laboratory (5, 6) have shown that lysine is the chief source of the hydroxylysine inc...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 240 شماره
صفحات -
تاریخ انتشار 1965