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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js Jmol JavaScript applet jmolApplet0_object__992246723676664__ initializing getValue debug = null getValue logLevel = null getValue allowjavascript = null AppletRegistry.checkIn(jmolApplet0_object__992246723676664__) call loadScript javascripts\jsmol\core\corestate.z.js viewerOptions: { "name":"jmolApplet0_object","applet":true,"documentBase":"https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18095","platform":"J.awtjs2d.Platform","fullName":"jmolApplet0_object__992246723676664__","display":"jmolApplet0_canvas2d","signedApplet":"true","appletReadyCallback":"Jmol._readyCallback","statusListener":"[J.appletjs.Jmol.MyStatusListener object]","codeBase":"https://www.ebi.ac.uk/chebi/javascripts/jsmol/","syncId":"992246723676664","bgcolor":"#000" } (C) 2012 Jmol Development Jmol Version: 13.2.7 $Date: 2013-10-01 11:35:15 -0500 (Tue, 01 Oct 2013) $ java.vendor: j2s java.version: 0.0 os.name: j2s Access: ALL memory: 0.0/0.0 processors available: 1 useCommandThread: false appletId:jmolApplet0_object (signed) starting HoverWatcher_1 getValue emulate = null defaults = "Jmol" getValue boxbgcolor = null getValue bgcolor = #000 backgroundColor = "#000" getValue ANIMFRAMECallback = null getValue APPLETREADYCallback = Jmol._readyCallback APPLETREADYCallback = "Jmol._readyCallback" getValue ATOMMOVEDCallback = null getValue CLICKCallback = null getValue ECHOCallback = null getValue ERRORCallback = null getValue EVALCallback = null getValue HOVERCallback = null getValue LOADSTRUCTCallback = null getValue MEASURECallback = null getValue MESSAGECallback = null getValue MINIMIZATIONCallback = null getValue PICKCallback = null getValue RESIZECallback = null getValue SCRIPTCallback = null getValue SYNCCallback = null getValue STRUCTUREMODIFIEDCallback = null getValue doTranslate = null language=en_US getValue popupMenu = null getValue script = null Jmol applet jmolApplet0_object__992246723676664__ ready call loadScript javascripts\jsmol\core\corescript.z.js call loadScript javascripts\jsmol\J\script\FileLoadThread.js starting QueueThread0_2 script 1 started starting HoverWatcher_3 starting HoverWatcher_4 The Resolver thinks Mol HYP - Ideal conformer RDKit 3D starting HoverWatcher_5 Time for openFile( HYP - Ideal conformer RDKit 3D 18 18 0 0 0 0 0 0 0 0999 V2000 0.1680 1.3600 -0.2820 N 0 0 0 0 0 0 0 0 0 0 0 0 -0.3840 -0.0030 -0.4930 C 0 0 2 0 0 0 0 0 0 0 0 0 -1.8110 -0.0720 -0.0130 C 0 0 0 0 0 0 0 0 0 0 0 0 -2.2330 0.7640 0.7500 O 0 0 0 0 0 0 0 0 0 0 0 0 0.5150 -0.9240 0.3590 C 0 0 0 0 0 0 0 0 0 0 0 0 1.8470 -0.1590 0.5050 C 0 0 2 0 0 0 0 0 0 0 0 0 1.6400 1.1590 -0.2710 C 0 0 0 0 0 0 0 0 0 0 0 0 2.9170 -0.9110 -0.0710 O 0 0 0 0 0 0 0 0 0 0 0 0 -2.6140 -1.0630 -0.4330 O 0 0 0 0 0 0 0 0 0 0 0 0 -0.1070 1.9810 -1.0280 H 0 0 0 0 0 0 0 0 0 0 0 0 -0.3250 -0.2780 -1.5460 H 0 0 0 0 0 0 0 0 0 0 0 0 0.0660 -1.0920 1.3370 H 0 0 0 0 0 0 0 0 0 0 0 0 0.6780 -1.8730 -0.1530 H 0 0 0 0 0 0 0 0 0 0 0 0 2.0520 0.0480 1.5550 H 0 0 0 0 0 0 0 0 0 0 0 0 2.0180 1.0650 -1.2890 H 0 0 0 0 0 0 0 0 0 0 0 0 2.1320 1.9850 0.2430 H 0 0 0 0 0 0 0 0 0 0 0 0 3.7800 -0.4790 -0.0090 H 0 0 0 0 0 0 0 0 0 0 0 0 -3.5200 -1.0660 -0.0980 H 0 0 0 0 0 0 0 0 0 0 0 0 1 2 1 0 1 7 1 0 1 10 1 0 2 3 1 0 2 5 1 0 2 11 1 6 3 4 2 0 3 9 1 0 5 6 1 0 5 12 1 0 5 13 1 0 6 7 1 0 6 8 1 0 6 14 1 1 7 15 1 0 7 16 1 0 8 17 1 0 9 18 1 0 M END): 22 ms reading 18 atoms ModelSet: haveSymmetry:false haveUnitcells:false haveFractionalCoord:false 1 model in this collection. Use getProperty "modelInfo" or getProperty "auxiliaryInfo" to inspect them. Default Van der Waals type for model set to Babel 18 atoms created ModelSet: not autobonding; use forceAutobond=true to force automatic bond creation Script completed Jmol script terminated
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| InChI=1S/C5H9NO3/c7-3-1-4(5(8)9)6-2-3/h3-4,6-7H,1-2H2,(H,8,9)/t3-,4+/m1/s1 |
| PMMYEEVYMWASQN-DMTCNVIQSA-N |
| [C@H]1(C[C@@H](O)CN1)C(O)=O |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Arabidopsis thaliana
(NCBI:txid3702)
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See:
DOI
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
(via 4-hydroxyproline )
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
plant metabolite
Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
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View more via ChEBI Ontology
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(2S,4R)-4-hydroxy-2-pyrrolidinecarboxylic acid
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ChEBI
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(2S,4R)-trans-4-hydroxyproline
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ChEBI
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δ-hydroxyproline
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NIST Chemistry WebBook
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Hydroxy-L-proline
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ChemIDplus
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Hydroxyproline
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ChemIDplus
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Hyp
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ChEBI
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Hypro
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ChemIDplus
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L-4-Hydroxyproline
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ChemIDplus
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L-threo-4-hydroxyproline
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ChEBI
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trans-4-hydroxy-L-proline
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ChEBI
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trans-4-Hydroxy-L-proline
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KEGG COMPOUND
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trans-Hydroxyproline
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NIST Chemistry WebBook
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trans-L-Hydroxyproline
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NIST Chemistry WebBook
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51-35-4
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CAS Registry Number
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KEGG COMPOUND
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51-35-4
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CAS Registry Number
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ChemIDplus
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51-35-4
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CAS Registry Number
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NIST Chemistry WebBook
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81441
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Reaxys Registry Number
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Reaxys
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Dong W, Zhang Y, Liu H, Gao B, Li D, Yang J (2009)
Detection of unsaturated disaccharides, pyridinoline, and hydroxyproline in urine of patients with Kashin-Beck disease: comparison with controls in an endemic area.
The Journal of rheumatology 36, 816-821 [PubMed:19286848]
[show Abstract]
ObjectiveTo investigate the pathologic status of adult patients with Kashin-Beck disease (KBD) in an endemic area of China through detection of 5 biochemical markers in their urine, and to study the correlations between these markers and KBD.MethodsA total of 55 patients with KBD over age 40 years were recruited and divided into groups, Grade 1 and Grade 2, according to clinical diagnosis criteria for KBD and our inclusion criteria; 25 healthy persons were enrolled into a control group. The first-time urine of the 80 participants was collected in the morning. Three unsaturated disaccharides, pyridinoline (PYD), and hydroxyproline (HYP) were detected in urine samples with high performance liquid chromatography, ELISA, and a chemical kit. Mean levels of these markers were compared in the 3 groups.ResultsThe mean concentrations of 3 unsaturated disaccharides and PYD in the Grade 2 group were significantly higher than levels in the Grade 1 group and controls (p<0.05). There was no significant difference between findings in the Grade 1 group and controls. Levels of 3 unsaturated disaccharides correlated with each other (p<0.01). The correlation coefficient between PYD and HYP was 0.470 (p<0.01). Except for HYP, the other markers all correlated with grade of KBD, rather than age or sex of subjects.ConclusionThe cartilage degradation of patients with Grade 2 KBD was more severe than that of Grade 1 patients and controls. The pathologic condition of Grade 1 patients was mild. Except for HYP, the markers we investigated specifically reflected the pathologic bone metabolism of adult patients with KBD. Trial registration number ChiCTR-TRC-00000140. | Knight J, Jiang J, Assimos DG, Holmes RP (2006)
Hydroxyproline ingestion and urinary oxalate and glycolate excretion.
Kidney international 70, 1929-1934 [PubMed:17021603]
[show Abstract]
Endogenous synthesis of oxalate is an important contributor to calcium oxalate stone formation and renal impairment associated with primary hyperoxaluria. Although the principal precursor of oxalate is believed to be glyoxylate, pathways in humans resulting in glyoxylate synthesis are not well defined. Hydroxyproline, a component amino acid of collagen, is a potential glyoxylate precursor. We have investigated the contribution of dietary hydroxyproline derived from gelatin to urinary oxalate and glycolate excretion. Responses to the ingestion of 30 g of gelatin or whey protein were compared on controlled oxalate diets. The time course of metabolism of a 10 g gelatin load was determined as well as the response to varying gelatin loads. Urinary glycolate excretion was 5.3-fold higher on the gelatin diet compared to the whey diet and urinary oxalate excretion was 43% higher. Significant changes in plasma hydroxyproline and urinary oxalate and glycolate were observed with 5 and 10 g gelatin loads, but not 1 and 2 g loads. Extrapolation of these results to daily anticipated collagen turnover and hydroxyproline intake suggests that hydroxyproline metabolism contributes 20-50% of glycolate excreted in urine and 5-20% of urinary oxalate derived from endogenous synthesis. Our results also revealed that the kidney absorbs significant quantities of hydroxyproline and glycolate, and their metabolism to oxalate in this tissue warrants further consideration. | Açil Y, Mobasseri AE, Warnke PH, Terheyden H, Wiltfang J, Springer I (2005)
Detection of mature collagen in human dental enamel.
Calcified tissue international 76, 121-126 [PubMed:15558350]
[show Abstract]
Mature dental enamel is the most mineralized of all mammalian tissues and considered to be free of collagen. Hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP) are two nonreducible cross-links of mature collagen. Hydroxyproline (Hyp) is an amino acid that is believed to be indicative of the presence of collagen. We set out to assess the concentrations of Hyp, HP, and LP in dental enamel and dentin (control) to clarify whether there was minor collagen content in dental enamel. We studied 17.53 g of enamel and 22.12 g of dentin gained from 120 extracted human teeth. Enamel and dentin (control) were separated with a diamond dental drill under microscopic control by wasting a margin of enamel (Ca. 2 mm) at the dentin-enamel border. Collagen alpha-chains were analyzed by Sodium dodecylsulfate-polyacrylamide gel (SDS-PAGE) after decalcification and collagen extraction. Concentrations of HP and LP where measured by using high-performance liquid chromatography (HPLC). Hyp was analyzed by a spectrophotometric method. The pooled probe of enamel contained 0.23 mug/g of Hyp. This concentration was 49 times lower than that in dentin. Concentrations of HP and LP in enamel were 0.07 nmol/g and 0.02 nmol/g, respectively being 605.57 (HP) and 251.50 (LP) times lower in enamel as compared to dentin. Collagen type I was found in enamel; collagen types I and V were found in dentin samples. In reports of many studies and textbooks, collagen is considered to be completely absorbed in the course of the mineralization and maturation of dental enamel. We show that this is not the case. However, the concentration of collagen in enamel was considerably lower as compared to that in dentin. | Wittmann F, Prix N, Mayr S, Angele P, Wichmann MW, van den Engel NK, Hernandez-Richter T, Chaudry IH, Jauch KW, Angele MK (2005)
L-arginine improves wound healing after trauma-hemorrhage by increasing collagen synthesis.
The Journal of trauma 59, 162-168 [PubMed:16096557]
[show Abstract]
BackgroundSeveral studies indicate impaired wound healing after trauma and shock. Wound immune cell dysfunction seems to be responsible for altered wound healing after trauma-hemorrhage (T-H). In this respect, administration of the amino acid L-arginine normalized wound immune cell function under those conditions. It remains unknown, however, whether L-arginine improves impaired wound healing after T-H.MethodsTo study this, male C3H/HeN mice were subjected to a midline laparotomy (i.e., soft tissue trauma induced), and polyvinyl sponges were implanted subcutaneously at the wound site before hemorrhage (35 +/- 5 mm Hg for 90 minutes) or were subjected to sham operation. During resuscitation, mice received 300 mg/kg body weight L-arginine or saline (vehicle). Seven days thereafter, hydroxyproline (OHP), a metabolite of collagen synthesis, was measured in the wound fluid using high-performance liquid chromatography. Collagen types I and III were determined in the wound by Western blot analysis. In addition, wound breaking strength was measured 10 days after T-H or sham operation.ResultsThe results indicate that OHP was significantly decreased in T-H mice. L-arginine, however, restored depressed OHP in the wound fluid in the T-H animals. Similarly, L-arginine treatment prevented a significant depression of collagen I synthesis after T-H. Collagen III was not significantly affected by T-H or L-arginine. Most important, L-arginine increased maximal wound breaking strength after severe blood loss. Therefore, L-arginine improves wound healing after T-H by increasing collagen synthesis.ConclusionBecause L-arginine improves wound healing, the results suggest that L-arginine might represent a novel and useful adjunct to fluid resuscitation for decreasing wound complications after trauma and severe blood loss. | Silva BM, Casal S, Andrade PB, Seabra RM, Oliveira MB, Ferreira MA (2004)
Free amino acid composition of quince (Cydonia oblonga Miller) fruit (pulp and peel) and jam.
Journal of agricultural and food chemistry 52, 1201-1206 [PubMed:14995121]
[show Abstract]
Twenty-one free amino acids present in several samples of quince fruit (pulp and peel) and quince jam (homemade and industrially manufactured) were analyzed by GC/FID. The analyses showed some differences between quince pulps and peels. Generally, the highest content in total free amino acids and in glycine was found in peels. As a general rule, the three major free amino acids detected in pulps were aspartic acid, asparagine, and hydroxyproline. For quince peels, usually, the three most abundant amino acids were glycine, aspartic acid, and asparagine. Similarly, for quince jams the most important free amino acids were aspartic acid, asparagine, and glycine or hydroxyproline. This study suggests that the free amino acid analysis can be useful for the evaluation of quince jam authenticity. It seems that glycine percentage can be used for the detection of quince peel addition while high alanine content can be related to pear addition. | Parker CR, Blackwell PJ, Freemont AJ, Hosking DJ (2002)
Biochemical measurements in the prediction of histologic subtype of renal transplant bone disease in women.
American journal of kidney diseases : the official journal of the National Kidney Foundation 40, 385-396 [PubMed:12148113]
[show Abstract]
Renal transplant osteodystrophy encompasses several histologic subtypes. Bone histomorphometric examination reliably distinguishes these groups but is invasive, is time-consuming, and delays diagnosis. Establishing a noninvasive method of correctly predicting histologic subtype in an individual to direct management is an attractive proposition. We identified 19 female renal transplant recipients with histologic evidence of hyperparathyroid bone disease (HPTH) and 14 with adynamic bone (ADB). We evaluated serum osteocalcin and bone-specific alkaline phosphatase as bone formation markers and urinary hydroxyproline (Hypro) and deoxypyridinoline cross-links as bone resorption markers. Mean concentrations for all markers were higher in the HPTH group, reaching significance for Hypro (HPTH, 24.8 +/- 4.2 micromol/mmol creatinine; ADB, 13.2 +/- 5.0 micromol/mmol creatinine; P = 0.01). A cutoff of 16.4 micromol/mmol creatinine for Hypro (Youden's index, 0.65) gave a sensitivity of 93% and specificity and positive predictive value (PPV) of 72% in predicting HPTH. In combination, Hypro greater than 16.4 micromol/mmol creatinine and parathyroid hormone greater than 80 pg/mL gave a specificity of 100%, sensitivity of 32%, and PPV of 100%. Conversely, for predicting ADB, Hypro less than 15.1 micromol/mmol creatinine (Youden's index, 0.45) gave a specificity of 93%, sensitivity of 53%, and PPV of 91%. Hypro less than 15.1 micromol/mmol creatinine plus osteocalcin less than 6.8 microg/L gave a specificity of 84.2%, sensitivity of 64.3%, and PPV of 75%. Significant associations between markers and histomorphometry were evident only for Hypro and osteocalcin (with osteoblast surface) and all markers (except deoxypyridinoline cross-links) with cortical volume. Markers have limited utility in identifying histologic subtype (Hypro was most effective) and, with the exception of Hypro and osteocalcin, showed little association with cell surface markers of bone cell activity. | Mazau D, Rumeau D, Esquerre-Tugaye MT (1988)
Two different families of hydroxyproline-rich glycoproteins in melon callus: biochemical and immunochemical studies.
Plant physiology 86, 540-546 [PubMed:16665943]
[show Abstract]
Two different families of hydroxyproline-rich glycoproteins, HRGP(1) and HRGP(2), have been isolated from melon callus and separated by ion exchange chromatography on CM-sepharose. HRGP(1) corresponds to an arabinogalactan protein. The sugar portion of HRGP(1) accounts for 94% of the molecule and contains galactose (66%) and arabinose (34%); these residues are present as polysaccharide side chains attached to hydroxyproline. Hydroxyproline is the main amino acid residue (46%) of the protein moiety. The arabinogalactan protein nature of HRGP(1) has been checked by its ability to positively react with the beta-glucosyl Yariv antigen; the (3)H-labeled deglycosylated HRGP(1) also called HRP(1) migrates upon electrophoresis as a single band of molecular weight 76,000. HRGP(2) was fractionated by affinity chromatography on heparin-Ultrogel into three different glycoproteins, HRGP(2a,2b) and (2c). Two of these glycoproteins behave as polycations (HRGP(2b) and (2c)) and are chemically distinct from HRGP(2a). HRGP(2b) is the most abundant component and contains 41% protein and 50% sugar. Hydroxyproline, lysine, tyrosine, and arabinose are the most prominent residues of their respective moiety. The glycosylation pattern of hydroxyproline indicates that HRGP(2b) is related to and possibly a precursor of the wall HRGP; as in melon cell wall HRGP, Hyp-Ara(3) predominates, and small amounts of a putative Hyp-Ara(5) a hitherto unreported hyp-arabinoside, are recorded. The molecular weight of HRP(2b), the protein portion of HRGP(2b) is 55,000 +/- 5,000, as estimated after deglycosylation of the molecule with trifluoromethane sulfonic acid. Antibodies have been raised against HRGP(2b) and HRP(2b). Immunodiffusion shows that each antigen (HRGP(2b) or HRP(2b)) reacts with its own IgG, and cross-reacts with the heterologous IgG, thereby indicating the presence of common (unglycosylated) and specific (glycosylated and deglycosylated) epitopes. The arabinogalactan protein HRGP(1) is not recognized by either antibody and HRGP(2b) does not react with the Yariv antigen. Immunoprecipitation of (3)H-labeled HRP(1) and HRP(2b) in the presence of goat antirabbit IgG, followed by gel electrophoresis, allows to recover HRP(2b) only. Again, HRP(2b) is immunoprecipitated by the two antisera. | Niell HB, Palmieri GM, Neely CL, Maxwell TA, Hopkins SC, Soloway MS (1983)
Total, dialyzable, and nondialyzable postabsorptive hydroxyproline. Values in patients with cancer.
Archives of internal medicine 143, 1925-1927 [PubMed:6625779]
[show Abstract]
The postabsorptive urinary total (T), dialyzable (D), and nondialyzable (ND) hydroxyproline (HYPRO) tests were evaluated to determine whether the patterns of excretion varied according to the predominance of osteoblastic v osteolytic bone involvement in 58 patients with neoplastic disease. In patients with osteolytic lesions from multiple myeloma, elevated T and D levels with normal ND HYPRO values were observed, along with elevated D/ND ratios. In prostate cancer, the T, D, and ND values were all elevated and the D/ND ratio was normal. Patients with Hodgkin's disease had elevated T, D, and ND HYPRO levels, and the D/ND ratio was in the range of patients with prostate cancer. The data suggest that these collagen markers may be useful in the long-term evaluation of these neoplasms in patients. | Niell HB, Neely CL, Palmieri GM, McDonald MW (1983)
The postabsorptive hydroxyproline in the long-term evaluation of patients with breast cancer.
Cancer 52, 1442-1447 [PubMed:6616407]
[show Abstract]
The postabsorptive urinary hydroxyproline excretion test (Spot-HYPRO) was evaluated for its usefulness in reflecting the presence or absence of bone metastasis in 75 women with breast cancer. A comparison was made between the Spot-HYPRO values and bone disease, as documented by bone scanning supported by skeletal x-rays. Breast cancer patients with skeletal metastasis had 3-4-fold elevations in Spot-HYPRO above the control values (P less than 0.001). Mild elevations were noted in breast cancer patients without skeletal metastasis (P less than 0.025). Thirty patients received serial Spot-HYPRO and bone scans for 6 to 48 months (average, 24 months). There was a 90% correlation between changes in Spot-HYPRO and simultaneous changes on bone scan. Elevations in Spot-HYPRO preceded changes found on bone scan by an average of 3 months. The authors conclude that the Spot-HYPRO is a simple, convenient, and accurate method of documenting and following bone metastasis in patients with breast cancer. | Niell HB, Palmieri GM, Neely CL, McDonald MW (1981)
Postabsorptive urinary hydroxyproline test in patients with metastatic bone disease from breast cancer.
Archives of internal medicine 141, 1471-1473 [PubMed:7283558]
[show Abstract]
Postabsorptive urine hydroxyproline (HYPRO) excretion ("spot" HYPRO test) was compared with the 24-hour urine excretion of HYPRO in 45 patients with breast cancer and nine normal subjects on a low-gelatin diet. A good correlation was observed between the results of these two tests in both groups. Patients with skeletal metastasis showed a higher spot HYPRO value than those without bone involvement and the number of lesions by bone scanning correlated with the values of spot HYPRO. In 20 of 22 patients with bone metastasis followed up for three to 19 months, spot HYPRO values correlated well with the evolution of bone disease. We conclude that the spot HYPRO test is a simple, inexpensive, and accurate method for the diagnosis and follow-up of patients with skeletal metastasis from breast cancer. | Dupuis Y, Digaud A, Gaudin-Harding F (1981)
Effect of vitamin D deficiency on urinary excretion of connective tissue derivatives (hydroxyproline and glycosaminoglycans) in rats.
Calcified tissue international 33, 177-180 [PubMed:6783274]
[show Abstract]
The urinary excretion of two connective tissue metabolites was studied in both control and vitamin D deficient rats. Hydroxyproline (HyPRO) excretion was determined after 2, 13 and 22 months (experiment I). It decreased with aging in animals receiving the control diet. On the contrary, this excretion increased as a function of age in vitamin D deficient animals. At the age of 22 months, HyPRO excretion was respectively 31 and 1708 micrograms a day in control and deficient animals. HyPRO and glycosaminoglycans (GAG) excretion was measured on a group of both control and vitamin D deficient rats at the age of 21 months (experiment II). These results confirm the high excretion of HyPRO in deficient animals. On the contrary, the GAG excretion was higher in control animals than in deficient ones, the mean excretion being respectively 412 and 234 micrograms a day. | Niell HB, Neely CL, Palmieri GM (1981)
The postabsorptive urinary hydroxyproline (spot-HYPRO) in patients with multiple myeloma.
Cancer 48, 783-787 [PubMed:7248905]
[show Abstract]
The simple postabsorptive urine hydroxyproline (Spot-HYPRO) with dialyzable and non-dialyzable (ND) fractions was measured in 28 patients with multiple myeloma. Myeloma patients with bone disease had higher total Spot-HYPRO and dialyzable fractions (P less than 0.001) than myeloma patients without bone disease or controls. The ND fraction of the Spot-HYPRO was elevated in myeloma patients with renal disease as compared with myeloma patients without renal disease and controls (P less than 0.01). Follow-up studies of ten myeloma patients demonstrated a close correlation between Spot-HYPRO and the dialyzable fraction and the evolution of bone disease. The Spot-HYPRO and its dialyzable fraction constitute a simple, inexpensive, and accurate test for the diagnosis and follow-up of the skeletal disease in patients with multiple myeloma. | van Holst GJ, Klis FM, de Wildt PJ, Hazenberg CA, Buijs J, Stegwee D (1981)
Arabinogalactan Protein from a Crude Cell Organelle Fraction of Phaseolus vulgaris L.
Plant physiology 68, 910-913 [PubMed:16662024]
[show Abstract]
Sonication of a crude cell organelle fraction from hypocotyl tissue of dark-grown bean seedlings, and from suspension-cultured cells released a hydroxyproline-containing protein. The purification of this protein is described. It was found to be an arabinogalactan protein composed of 90% carbohydrate and 10% protein. The major sugars are galactose, arabinose, and uronic acids, and the major amino acids are hydroxyproline, serine, and alanine. Its molecular weight was estimated at 1.4 x 10(5) daltons and the isoelectric point at pH 2.3. The molecule is soluble in 5% trichloroacetic acid and can be precipitated with beta-galactosyl Yariv antigen. Pulse-chase experiments indicated that it was a secretory protein. The biosynthesis of arabinogalactan proteins is discussed. | Hey H, Tougaard L (1980)
Elevated bone phosphorus/hydroxyproline ratio following jejunoileal bypass surgery.
Acta medica Scandinavica 208, 321-323 [PubMed:7446210]
[show Abstract]
The degree of bone mineralization, estimated as the bone phosphorus/hydroxyproline ratio (P/Hypro), was studied in 33 patients who had undergone jejunoileal bypass surgery for massive obesity. Low values of bone P/Hypro are expected in osteomalacia. We found an elevated mean bone P/Hypro (p < 0.001) with the highest values in patients with the longest postoperative periods (rS = 0.65, p < 0.001). The study indicates that bypass surgery, in spite of vitamin D deficiency, is associated with an increased average degree of bone mineralization or a defect in bone collagen synthesis. | Tougaard L, Rickers H, Rödbro P, Thaysen EH, Christensen MS, Lund B, Sörensen OH (1977)
Bone composition and vitamin D after Pólya gastrectomy.
Acta medica Scandinavica 202, 47-50 [PubMed:899882]
[show Abstract]
With the aim of evaluating bone phosphorus/hydroxyproline ratio (P/Hypro) as an index of osteomalacia, this bone index and the bone mineral content (BMC) have been investigated together with other indices of calcium metabolism in 27 gastrectomized patients. None of the patients had clinically manifest bone symptoms. The mean values of bone P/Hypro, BMC, plasma calcium and plasma magnesium were subnormal; the mean values of serum parathyroid hormone (iPTH) and plasma alkaline phosphatase were elevated. Mean serum 25-hydroxycholecalciferol (25-OH-D) did not differ from normal. A significant positive correlation was found between bone P/Hypro and serum 25-OH-D, but no significant correlation between bone P/Hypro and BMC. Serum 25-OH-D and bone P/Hypro were significantly lower and serum iPTH was significantly higher in a subgroup of 12 patients with no regular supplementary intake of vitamin D. In conclusion, the gastrectomized patients had blood biochemical evidence of a mild vitamin D insufficiency and the low bone P/Hypro values can be explained by mild osteomalacic changes in bone. | Palmierj GM, Hawrylko J (1977)
Effects of aldosterone on the urinary excretion of total and non-dialyzable hydroxyproline.
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme 9, 507-509 [PubMed:590925]
[show Abstract]
In order to explore the role of mineralocorticoids on collagen metabolism, the effects of aldosterone on the urinary excretion of total and non dialyzable hydroxyproline (HYPRO) was studied in rats. The administration of aldosterone in sesame oil, 75 microgram/100 g body weight to adrenalectomized rats maintained on 1% NaCl solution as drinking fluid and 1 mg of cortisone subcutaneously daily, provoked elevation of total and non dialyzable HYPRO in urine (P less than 0.001), when compared to similarly treated adrenalectomized rats receiving sesame oil but no aldosterone. Both groups showed a normal growth curve and had similar urinary excretion of creatinine. The effects of aldosterone are opposed to the known lowering effects of glucocorticoids on HYPRO excretion and may suggest an effect of aldosterone on collagen turnover. Alternatively, aldosterone may modify the metabolism or excretion of HYPRO in an opposite manner to that of glucocorticoids. | Tougaard L, Buhl S, Poulsen H (1977)
The degree of bone mineralization in different parts of human skeleton estimated from bone phosphorus/hydroxyproline.
Scandinavian journal of clinical and laboratory investigation 37, 27-31 [PubMed:616023]
[show Abstract]
To evaluation the uniformity of the degree of mineralization in the skeleton the bone phosphorus/hydroxyproline ratio (bone P/Hypro) was determined in different localizations of ten human skeletons. Marked differences in bone P/Hypro were found between cortical bone and spongy bone. No difference was found between cortical bone from humerus, femur and cranium. But the mean value of these cortical bones was significantly higher than the mean value of the studied spongy bones. No significant correlation was found between the two bone types. Differences in bone P/Hypro were also found between different spongy bones. In pelvis the value did not differ between four spongy bone localizations but the mean value was significantly lower than for the other spongy bones (thoracal column, lumbal column and clavicle). Between these other spongy bones no difference was found in mean bone P/Hypro, and the mean of the pelvic bone localizations correlated significantly to the other spongy bones. The study demonstrates differences in the chemical composition of the human skeleton. A value of bone P/Hypro in the iliac crest can be used to estimation of bone P/Hypro in other spongy bones but not in cortical bones. | Tougaard L (1976)
The degree of bone mineralization in hyperthyroidism estimated from the phosphorus to hydroxyproline ratio in bone.
Acta endocrinologica 81, 482-486 [PubMed:946341]
[show Abstract]
The proportion between mineral and collagen in bone tissue, "the degree of mineralization", can be evaluated from the phosphorus to hydroxyproline ratio (P/Hypro ratio), determined in bone biopsies. The ratio was measured in 27 unselected hyperthyroid patients. No significant correlation was found between the P/Hypro ratio and the age of the patient, the duration of the disease or the value of serum thyroxine. The mean value of the P/Hypro ratio for the group studied was not significantly different from the normal mean. The results of the study indicate a normal degree of mineralization in the bone of patients with hyperthyroidism. | Schaadt O, Tougaard L (1975)
The degree of bone mineralization in chronic renal failure estimated from phosphorus/hydroxyproline ratio in bone biopsies.
Acta medica Scandinavica 198, 91-93 [PubMed:1166829]
[show Abstract]
The degree of bone mineralization is the proportion between the contents of mineral and collagen in bone. As phosphorus (P) and hydroxyproline (Hypro) constitute a constant fraction of bone mineral and collagen, respectively, the P/Hypro ratio in bone tissue provides an estimate of the degree of mineralization. The P/Hydro ratio has been studied in bone biopsies from 42 patients with severe chronic renal failure. A few of them had a subnormal P/Hypro ratio and these patients corresponded to the diagnosis of classical osteomalacia or probably hyperparathyroidism. However, the mean bone P/Hypro ratio was significantly higher than normal, indicating a general tendency towards a higher degree of bone mineralization in patients with chronic renal failure. | Harris ED, Hoffman GS, McGuire JL, Strosberg JM (1975)
Colchicine: effects upon urinary hydroxyproline excretion in patients with scleroderma.
Metabolism: clinical and experimental 24, 529-535 [PubMed:1117843]
[show Abstract]
Three patients with scleroderma were given intravenous infusions of colchicine (2-4 mg/day) for 3 days. Twenty-four-hour urine collections were assayed for total hydroxyproline (HYPRO), an index of collagen resorption, and for nondialyzable polypeptide HYPRO, an index of collagen synthesis. During the colchicine infusions there was a fall in total urinary HYPRO and a slight increase in the per cent nondialyzalbe HYPRO in each patient. The hydroxylysyl-galactosyl-glucose (HGG) to hydroxylysyl-galactose (HG) ratios were not strikingly different in two samples, with the greastest differences in HYPRO excretion. Our results suggested that total body collagen catabolism had diminished without a concomitant decrease in synthesis. In contrast to provocative reports in the literature, these data do not support the hypothesis that administration of colchicine in doses tolerated in man can either inhibit synthesis of new collagen, increase degradation of mature collagen, or be of use in treatment of fibrotic states. | Cleland R (1967)
Inhibition of formation of protein-bound hydroxyproline by free hydroxyproline in Avena coleoptiles.
Plant physiology 42, 1165-1170 [PubMed:16656634]
[show Abstract]
Free hydroxyproline inhibits the formation of protein-bound hydroxyproline from proline to a considerably greater extent than it does the incorporation of proline into protein of auxin-treated Avena coleoptiles. This inhibition is greater in the wall than in the cytoplasmic fraction. In the absence of auxin, free hydroxyproline exerts little or no inhibition of hydroxyproline formation. Furthermore free hydroxyproline has no effect on respiration, RNA synthesis or the incorporation of leucine into protein. Hydroxyproline is not a general inhibitor of metabolism or protein synthesis in Avena coleoptiles.These results suggest that free hydroxyproline may inhibit auxin-induced cell elongation by blocking the formation or utilization of a particular hydroxyproline-rich protein which must be incorporated into the cell wall during auxin-induced wall extension. | ROBERTSON WV (1964)
METABOLISM OF COLLAGEN IN MAMMALIAN TISSUES.
Biophysical journal 4, SUPPL93-114 [PubMed:14104082]
[show Abstract]
The amino acid composition of collagen is described and the status of knowledge about the synthesis of its unique amino acids, hydroxyproline and hydroxylysine, presented. This is followed by a schematic overview of collagen metabolism. Scurvy and lathyrism, the only two abnormalities of collagen metabolism which can now be reasonably elucidated at a molecular level, are then discussed in some detail. The paper concludes by stressing the importance of recognizing the role of histoarchitecture and of interactions of collagen with other compounds when studying collagen or its metabolism in the whole animal. |
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