Sequence Analysis of a cDNA for Lysyl Hydroxylase Isolated from Human Skin Fibroblasts from a Normal Donor: Differences from Human Placental Lysyl Hydroxylase cDNA

Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts

“…The existence of different enzymic forms of lysyl hydroxylase (LH) (Yeowell, 2002) was proposed to explain why the hydroxylation of lysine residues within the helical region of type I collagen appeared distinct from the hydroxylation of lysine residues in the collagen telopeptide (nonhelical) region (Gerriets et al, 1993;Royce and Barnes, 1985). The importance of LH1, the first form of LH to be described and characterized at the molecular level (Yeowell et al, 1994(Yeowell et al, , 1992Hautala et al, 1992), is demonstrated in patients with Ehlers-Danlos syndrome type VIA (EDSVIA: OMIM# 225400), the kyphoscoliotic form of EDS (Beighton et al, 1998). Their clinical phenotype results from a deficiency of LH caused by several different mutations in the LH1 gene (Yeowell and Walker, 2000), also named procollagen-lysine, 2-oxoglutarate 5-dioxygenase (PLOD).…”

Heterogeneous basis of the type VIB form of Ehlers–Danlos syndrome (EDS VIB) that is unrelated to decreased collagen lysyl hydroxylation

“…The decreased enzyme activity in EDS VIA patients has been previously shown to result from mutations in the LH1 gene. Although the first report of the linkage of EDS VI to a deficiency of LH activity appeared 30 years ago [Krane et al, 1972; Pinnell et al, 1972], the affected human gene (now referred to as LH1 ) was not characterized until 20 years later [Hautala et al, 1992; Yeowell et al, 1992, 1994]. Two additional members of the LH family, LH2 and LH3 , were isolated more recently [Valtavaara et al, 1997, 1998; Passoja et al, 1998; Yeowell and Walker, 1999] but, unlike LH1 , decreased expression of these genes has not been directly linked to any connective tissue disorder.…”

“…Total RNA (10 μg) was separated electrophoretically and transferred onto a GeneScreen Plus nylon membrane (Perkin Elmer, Boston, MA) [Yeowell et al, 1991]. The membrane blots were hybridized under conditions as described [Yeowell et al, 1992] with [α‐ 32 P]‐labeled cDNA probes for (1) LH1 using a full‐length 2.9 kb cDNA based on the coding sequence for LH1 between nts 19 and 2914, which detects a 3.4 kb LH1 mRNA [Yeowell et al, 1992, 1994]; (2) an 863 bp LH2 probe (between nts 9 and 872 of LH2 cDNA sequence [Valtavaara et al, 1997; Yeowell and Walker, 1999]) which detects a 4.2 kb mRNA encoding LH2; (3) a 1.8 kb probe for LH3 (between nts 447 and 2232 of LH3 sequence [Valtavaara et al, 1998] which detects a 3 kb mRNA encoding LH3, and (4) a 5′‐end [γ‐ 32 P]‐labeled 26‐mer oligonucleotide probe complementary to the sequence 4011–4036 of the human 28S rRNA [Barbu and Dautry, 1989]. The Northern radiographs were scanned using the Kodak Digital Science™ Electrophoresis Documentation and Analysis System 120 and the Kodak 1D Image Analysis Software.…”

Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2

“…While the tissue distribution of lh gene expression has been examined by Northern blot analysis, with the exception of lh3, there have been no published accounts of the in situ expression patterns of these genes during embryogenesis in any vertebrate species (Passoja et al, 1998b;Rautavuoma et al, 2004;Ruotsalainen et al, 1999;Valtavaara et al, 1997;Valtavaara et al, 1998;Yeowell et al, 1994;Yeowell and Walker, 1999). In this paper, we report the cloning of zebrafish lh1 and lh2 and their patterns of expression throughout the first two days of development.…”