hydroxyproline


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hydroxyproline

 [hi-drok″sĭ-pro´lēn]
an amino acid produced in the digestion of hydrolytic decomposition of proteins, especially of collagens.

hydroxyproline

/hy·droxy·pro·line/ (-pro´lēn) a hydroxylated form of proline, occurring in collagen and other connective tissue proteins.

hydroxyproline

[-prō′lēn]
an amino acid whose level in the urine is elevated in diseases of the bone and certain genetic disorders, such as Marfan's syndrome. Its normal accumulation in urine after a 24-hour collection is 10 to 75 mg.

hydroxyproline

Biochemistry A hydroxylated amino acid which is most concentrated in collagen ↑ in urine Indicates ↑ turnover of bone matrix, often caused by osteoporosis ↓ in Malnutrition, ↑ by acromegaly, acute osteomyelitis, burns, congenital hyperphosphatasia, fibrous dysplasia, healing fractures, hyperparathyroidism, hyperthyroidism, Marfan syndrome, osteomalacia, Paget's disease of bone, parathyroid adenoma, rickets, bone tumors

hydroxyproline

Hyp; an amino acid derived from proline.
References in periodicals archive ?
2013) Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana.
VSD treatments generally induced higher levels of hydroxyproline than traditional treatment on POD 7, 10 and 15 (P<0.
For imino acids, gelatin had proline and hydroxyproline of 127 and 99 residues/1,000 residues, respectively.
However, the level of hydroxyproline in lenti-P4H[alpha]1 group was much higher than the other two groups (p < 0.
c) Hydroxyproline content of rat renal tissue in each group (mean [+ or -] SE, n = 10).
For the results of all days, tissue hydroxyproline levels of the sildenafil groups, dose dependently, were greater than of the pure carbopol and control groups, but difference was not statistically significant (p=0.
The most significant peak positions in mandible spectra appears at 25 ppm (assigned to Proline C) 30 ppm (assigned to Proline CAY) 37 ppm (assigned to Hydroxyproline C and Aspartate C ) and 40 ppm (as- signed to leucine CAY isoleucine CAY and phenylalanine CAY) as compare to other spectra.
Vitamin C is the cofactor for enzymes like lysyl hydroxylase and prolyl hydroxylase, enzymes that are very important for making hydroxylysine and hydroxyproline, which play a crucial role in the stability of the structure of collagen triple helix.
In an Indian cross sectional study it was found that bone formation markers (total and ionised calcium were significantly decreased, and alkaline phosphatise significantly increased) and bone resorption markers (urinary hydroxyproline was significantly increased) in postmenopausal as compared to premenopausal women.

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