Collagen biosynthesis enzymes in serum and hepatic tissue in liver disease

Kuutti-Savolainen, Eeva-Riitta; Risteli, Juha; Miettinen, Tatu A.; Kivirikko, Kari I.

doi:10.1111/j.1365-2362.1979.tb01672.x

Cited by 60 publications

(14 citation statements)

References 28 publications

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“…High correlations have previously been found between the three serum markers in patients with various liver diseases (6,9,11), and are now demonstrated in sickle cell disease. Correlation of the two serum enzymes and serum aminoterminal propeptide of type III procollagen with tests of liver function have been reported earlier (10,11,13), and here there were significant correlations between the two serum enzymes of collagen and serum alanine aminotransferase, but a very week correlation was found between alanine aminotransferase and serum aminoterminal propeptide of type III procollagen. It thus seemed likely that the two serum enzymes and serum aminoterminal propeptide of type III procollagen primarily reflect in sickle cell disease the actual changes in hepatic, bone or spieen collagen formation.…”

Section: Discussionsupporting

confidence: 47%

“…The samples were assayed in düplicates and serum enzyme protein concentrations were expressed äs mg per liter. Serum aminoterminal propeptide of type III procollagen was measured using a radioimmunoassay kit (Behringwerke AG, Germany) based on the displacement of radioactively-labelled type III aminoterminal propeptide and the subsequent precipitation of the peptide-antibody complex by a second antibody (13). Serum galactosylhydroxylysyl glucosyltransferase activity was measured by the method of Myllyla et al (20), äs modified for human serum samples (21).…”

Section: Methodsmentioning

confidence: 99%

“…Increased serum immunoreactive prolyl hydroxylase protein and serum galactosylhydroxylysyl glucosyltransferase activity have been reported in patients with various liver diseases (5 -12). The two serum enzymes correlate significantly with the respective enzyme activities in liver biopsy specimens, which indicates that serum immunoreactive prolyl hydroxylase protein and serum galactosylhydroxylysyl glucosyltransferase activity may give useful Information on actual hepatic Collagen formation (10,12,13).…”

Section: Introductionmentioning

confidence: 91%

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Serum Enzymes of Collagen Synthesis and Type III Procollagen Amino-propeptide in Nigerian Patients with Sickle Cell Disease

Bolarín¹

1986

Clinical Chemistry and Laboratory Medicine

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i Summary: Serum immunoreactive prolyl hydroxylase protein, galactosylhydroxylysyl glucosyltransferase l activity and the aminoterminal propeptide of type III procollagen were measured in 20 patients with sickle cell disease and the values were compared with those in 20 apparently healthy Nigerians. The means for the two enzymes and serum aminoterminal propeptide of type III procollagen were significantly higher in the ! sickle cell disease patients. Significant correlations were found between the values for the two enzymes and ! the protein serum aminoterminal propeptide of type III procollagen within the sickle cell disease patients. The data confirm that collagen formation is found in the liver, bone and other organs of patients with this disease. The measurement of serum immunoreactive prolyl hydroxylase protein, serum galactosylhydroxylysyl ' < glucosyltransferase activity and serum aminoterminal propeptide of type III procollagen in prospective studies r might be helpful in predicting hepatic, bone or diffuse fibrogenesis in sickle cell disease. l Enzyme der Kollagensynthese und Typ III-Prokollagen-Aminopropeptid im Serum nigerianischer Patienten mit SichelzettkrankheitZusammenfassung: Immünreaktives Prolylhydroxylase-Protein, katalytische Aktivität von Galaktosylhydroxylysyl-Glucosyltransferase und das aminoterminale Propeptid vom Typ III Prokollagen wurden im Serum bei 20 Patienten mit Sichelzellanämie gemessen. Die Werte wurden mit denen von 20 offensichtlich gesunden Nigerianern verglichen. Die Mittelwerte für die beiden Enzyme und das aminoterminale Propeptid von Typ i III Prokollagen waren bei den Patienten mit Sichelzellanämie signifikant höher. Signifikante Korrelationen } wurden zwischen den Werten für die beiden Enzyme und das aminoterminale Propeptid von Typ III 5 Prokollagen innerhalb der Sichelzellanämiepatienten festgestellt. Die Daten bestätigen, daß Kollagenbildung ; in Leber, Knochen und anderen Organen von Patienten mit dieser Erkrankung vorkommt. Die Messung der l drei Kenngrößen bei prospektiven Studien könnte für die Vorhersage der Kollagenfaserbildung in der Leber, in Knochen, oder diffus bei Sichelzellanämie hilfreich sein.

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Section: Discussionsupporting

confidence: 47%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 91%

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Serum Enzymes of Collagen Synthesis and Type III Procollagen Amino-propeptide in Nigerian Patients with Sickle Cell Disease

Bolarín¹

1986

Clinical Chemistry and Laboratory Medicine

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“…This enzyme is located in the membrane of rough endoplasmic reticulum in many different cells, including hepatocytes (25). Previous reports have demonstrated that serum concentrations of immunoreactive prolyl hydroxylase (26,27) and the p-subunit of prolyl 4-hydroxylase (13, [28][29][30] are elevated in chronic active liver disease and HCC in relation to increases in liver enzyme activity. Thus the serum level of prolyl hydroxylase appears to reflect actual changes in hepatic collagen biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin

Murawaki¹,

Kusakabe²,

Hirayama³

1991

Hepatology

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Lysyl oxidase was partially purified from serum by a diethylaminoethyl batch procedure in the presence of 6 mol/L urea and dialyzed against 3 mol/L KSCN. Using this method, we determined serum lysyl oxidase activity in 52 patients with liver disease and in 14 healthy controls, and we examined usefulness of serum lysyl oxidase in assessing liver fibrogenesis. For this purpose, serum lysyl oxidase activity in chronic liver disease was compared with serum levels of prolyl hydroxylase and laminin P1. As compared with controls, serum lysyl oxidase activity increased 1.6-fold in chronic persistent hepatitis, 4.4-fold in chronic active hepatitis and 11.8-fold in cirrhosis, indicating an increase in concert with the development of liver fibrosis. In hepatocellular carcinoma, the serum activity, although significantly increased, was lower than that in cirrhosis. Serum prolyl hydroxylase was significantly increased in chronic active hepatitis, in liver cirrhosis and in hepatocellular carcinoma. Serum laminin P1 was significantly increased in chronic active hepatitis, in cirrhosis and in hepatocellular carcinoma. Serum lysyl oxidase activity did not correlate significantly with serum levels of prolyl hydroxylase and laminin P1 in any subject or in any subgroup. The magnitude of the increase and the abnormal percentage of serum lysyl oxidase activity were larger than those for serum prolyl hydroxylase and laminin P1. These results suggest that serum lysyl oxidase activity is a more sensitive indicator of liver fibrosis than serum prolyl hydroxylase and laminin P1.

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“…The decline of prolyl hydroxylase activity after prolonged exposure of cells to ascorbate is unusual because changes in prolyl hydroxylase activity often accompany changes in collagen synthesis (4,35). One report, however, indicates an adverse effect of ascorbate on prolyl hydroxylase activity with no significant change in lysyl hydroxylase activity during culture growth (36).…”

Section: Methodsmentioning

confidence: 99%

Regulation of collagen synthesis by ascorbic acid.

Murad¹,

Grove²,

Lindberg³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

392

221

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After prolonged exposure to ascorbate, collagen synthesis in cultured human skin fibroblasts increased approximately 8-fold with no significant change in synthesis ofnoncollagen protein. This effect of ascorbate appears to be unrelated to its cofactor function in collagen hydroxylation. The collagenous protein secreted in the absence of added ascorbate was normal in hydroxylysine but was mildly deficient in hydroxyproline. In parallel experiments, lysine hydroxylase (peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase, EC 1.14.11.4) activity increased 3-fold in response to ascorbate administration whereas proline hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, EC 1.14.11.2) activity decreased considerably. These results suggest that collagen polypeptide synthesis, posttranslational hydroxylations, and activities of the two bydroxylases are independently regulated by ascorbate.Ascorbic acid is essential for normal collagen formation (1-3) by virtue ofthe fact that it is a required component in the synthesis of hydroxyproline and hydroxylysine in collagen (4). Hydroxyproline serves to stabilize the collagen triple helix (5, 6); its absence results in structurally unstable collagen (7, 8) which is not secreted from cells at a normal rate (9). Hydroxylysine is necessary for formation of the intermolecular crosslinks in collagen (10). In addition, specific carbohydrate residues are linked glycosidically to collagen through hydroxylysine, a process that may be important in the regulation of crosslink formation (11).It is generally believed that ascorbate modulates collagen production through its effect on prolyl hydroxylation (12). There have been indications, however, that ascorbate may have an additional role in collagen biosynthesis (13-16). Notable are the early studies by Jeffrey and Martin (13) who observed a substantial increase in the size of chicken long bones cultured in the presence of ascorbate, concomitant with an increase in the incorporation of proline into peptidyl hydroxyproline.In this study we have examined the long-term effect of ascorbate on collagen production by cultured human skin fibroblasts. The influence ofascorbate on prolyl hydroxylase (prolylglycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, EC 1.14.11.2) and lysyl hydroxylase (peptidyllysine, 2 oxoglutarate:oxygen 5-oxidoreductase, EC 1.14.11.4) levels was also examined simultaneously to understand better the interrelationship of collagen synthesis and posttranslational hydroxylation. The data indicate that ascorbate increases collagen synthesis by acting at a level other than hydroxylation. MATERIALS AND METHODSHuman skin fibroblasts from a normal 3-day-old boy (GM 970) were obtained from the Institute for Medical Research (Camden, NJ) and grown to confluent density in Dulbecco's modified Eagle's medium buffered with 24 mM sodium bicarbonate and 25 mM Hepes and supplemented with 20% fetal calf serum (GIBCO) which had been inactivated for 30 min at 560C. Cultures were growth arrested for 90 hr in ...

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Collagen biosynthesis enzymes in serum and hepatic tissue in liver disease

Cited by 60 publications

References 28 publications

Serum Enzymes of Collagen Synthesis and Type III Procollagen Amino-propeptide in Nigerian Patients with Sickle Cell Disease

Serum Enzymes of Collagen Synthesis and Type III Procollagen Amino-propeptide in Nigerian Patients with Sickle Cell Disease

Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin

Regulation of collagen synthesis by ascorbic acid.

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