Enzymes of collagen biosynthesis in skin and serum in dermatological diseases

Kuutti-Savolainen, Eeva-Riitta

doi:10.1016/0009-8981(79)90051-2

Cited by 20 publications

(8 citation statements)

References 9 publications

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“…The secretion of LH3 from cultured cells, as observed in this present study, and earlier findings that GGT activity can be measured in human serum (Anttinen, 1977; Kuutti‐Savolainen, 1979; Savolainen et al, 1981; Bolarin et al, 1984) suggest the possibility that GGT activity in serum is derived from LH3. Thus we measured GGT activity in mouse and human serum (Table 3).…”

Section: Resultssupporting

confidence: 89%

Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling

Salo

Wang

Sipilä

et al. 2006

Journal Cellular Physiology

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Lysyl hydroxylase 3 (LH3), the multifunctional enzyme associated with collagen biosynthesis that possesses lysyl hydroxylase and collagen glycosyltransferase activities, has been characterized in the extracellular space in this study. Lysine modifications are known to occur in the endoplasmic reticulum (ER) prior to collagen triple-helix formation, but in this study we show that LH3 is also present and active in the extracellular space. Studies with in vitro cultured cells indicate that LH3, in addition to being an ER resident, is secreted from the cells and is found both in the medium and on the cell surface associated with collagens or other proteins with collagenous sequences. Furthermore, in vivo, LH3 is present in serum. LH3 protein levels correlate with the galactosylhydroxylysine glucosyltransferase (GGT) activity of mouse tissues. This, together with other data, indicates that LH3 is responsible for GGT activity in the tissues and that GGT activity assays can be used to quantify LH3 in tissues. LH3 in vivo is located in two compartments, in the ER and in the extracellular space, and the partitioning varies with tissue type. In mouse kidney the enzyme is located mainly intracellularly, whereas in mouse liver it is located solely in the extracellular space. The extracellular localization and the ability of LH3 to modify lysyl residues of extracellular proteins in their native, nondenaturated conformation reveals a new dynamic in extracellular matrix remodeling, suggesting a novel mechanism for adjusting the amount of hydroxylysine and hydroxylysine-linked carbohydrates in collagenous proteins.

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Section: Resultssupporting

confidence: 89%

Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling

Salo

Wang

Sipilä

et al. 2006

Journal Cellular Physiology

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“…well within the range of the previously reported control values. This indicates that the glucosyltransferase activity assay gave values similar to those reported previously (23,24).…”

Section: Collagen Glycosyltransferase Activities Of the Purified Recosupporting

confidence: 88%

“…The amount of collagen glucosyltransferase activity in serum samples from healthy human subjects has been reported previously to range from 0.24 to 0.60 milliunit/ml (milliunit being defined as described previously (24)). The values obtained for the two serum samples assayed here together with the LH3 and its fragment preparations were 0.32 and 0.36 milliunit/ml, i.e.…”

Section: Collagen Glycosyltransferase Activities Of the Purified Recomentioning

confidence: 99%

Characterization of Three Fragments That Constitute the Monomers of the Human Lysyl Hydroxylase Isoenzymes 1–3

Rautavuoma

Takaluoma

Passoja

et al. 2002

Journal of Biological Chemistry

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Lysyl hydroxylase (LH) catalyzes the formation of hydroxylysine in collagens; three human isoenzymes have been cloned so far. We report here on the purification of all three recombinant isoenzymes to homogeneity from the medium of cultured insect cells, and we demonstrate that they are all homodimers. Limited proteolysis experiments identified two main protease-sensitive regions in the monomers of about 80 -85 kDa, corresponding to three fragments A-C (from the N to C terminus), with molecular masses of about 30, 37, and 16 kDa, respectively. Fragment A was found to play no role in LH activity as a recombinant B-C polypeptide constituted a fully active hydroxylase with K m values for cosubstrates and the peptide substrate that were identical to those of the full-length enzyme. LH3, but not LH1 and LH2, has also been reported recently (Heikkinen, J., Risteli, M., Wang, C., Latvala, J., Rossi, M., Valtavaara, M., and Myllylä , R. (2000) J. Biol. Chem. 275, 36158 -36163) to possess collagen glucosyltransferase activity. We confirm this highly surprising finding here and extend it by demonstrating that LH3 may also possess trace amounts of collagen galactosyltransferase activity. All the glucosyltransferase and galactosyltransferase activity of LH3 was found to reside in fragment A, which played no role in the hydroxylase activity of the polypeptide. This fragment is about 55% identical and 80% similar to the corresponding fragments of LH1 and LH2. However, the levels of the glycosyltransferase activities are so low that they may be of little biological significance. It is thus evident that human tissues must have additional glycosyltransferases that are responsible for most of the collagen glycosylation in vivo.

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“…S-GGT is high in primary biliary cirrhosis, portal cirrhosis, cancer with liver metastasis and acute hepatitis, but not usually in fatty liver or in a number of other liver diseases [7]. S-GGT is high in primary biliary cirrhosis, portal cirrhosis, cancer with liver metastasis and acute hepatitis, but not usually in fatty liver or in a number of other liver diseases [7].…”

Section: Discussionmentioning

confidence: 99%

Serum galactosylhydroxylysyl glucosyltransferase in acute myocardial infarction and during subsequent collagen scar formation

Anttinen

Järvensivu

Savolainen

1981

Eur J Clin Investigation

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Changes in serum galactosylhydroxylysyl glucosyltransferase, an enzyme catalysing one of the intracellular post-translational modifications in collagen biosynthesis, were studied in twenty-four patients with acute myocardial infarction. The enzyme activity was monitored for 18 days from the onset of infarction, and at least a two-peaked pattern was observed. The first peak corresponded to the stage of acute myocardial injury, there being a highly significant correlation between the maximal values for serum glucosyltransferase and alpha-hydroxybutyrate dehydrogenase. An average decreasing in serum glucosyltransferase activity of 41%, was noted during the following 24 h. A new gradual rise in serum glucosyltransferase activity, interpreted as indicating myocardial collagen scar formation, was observed 5 days after the onset of infarction, when the serum enzyme activities indicating myocardial injury had already declined. The average daily values for serum glucosyltransferase between 6 and 18 days correlated highly significantly with the maximal value for serum alpha-hydroxybutyrate dehydrogenase, which serves as a relative estimate of the size of the original myocardial infarction area. The data further suggest that certain other factors including heart failure and/or various drug treatments may also affect the magnitude of this second peak.

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Enzymes of collagen biosynthesis in skin and serum in dermatological diseases

Cited by 20 publications

References 9 publications

Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling

Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling

Characterization of Three Fragments That Constitute the Monomers of the Human Lysyl Hydroxylase Isoenzymes 1–3

Serum galactosylhydroxylysyl glucosyltransferase in acute myocardial infarction and during subsequent collagen scar formation

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