Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Decrease of lysyl hydroxylase 2 activity causes abnormal collagen molecular phenotypes, defective mineralization and compromised mechanical properties of bone.

Bone - 1 Jan 2022

Saito Tomoaki, Terajima Masahiko, Taga Yuki, Hayashi Fumihiko, Oshima Sachi, Kasamatsu Atsushi, Okubo Yasuhiko, Ito Chizuru, Toshimori Kiyotaka, Sunohara Masataka, Tanzawa Hideki, Uzawa Katsuhiro, Yamauchi Mitsuo

Abstract excerpt

Lysyl hydroxylase 2 (LH2) is an enzyme that catalyzes the hydroxylation of lysine (Lys) residues in fibrillar collagen telopeptides, a critical post-translational modification for the stability of intermolecular cross-links. Though abnormal LH2 activities have been implicated in various diseases including Bruck syndrome, the molecular basis of the pathologies is still not well understood. Since LH2 null mice die...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Collagen
Share to Collagen Type I

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Osteogenesis Imperfecta

Share to Phenotype

Share to Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase

Source

Identifiers

PMID: 34718219
DOI: 10.1016/j.bone.2021.116242

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Decrease of lysyl hydroxylase 2 activity causes abnormal collagen molecular phenotypes, defective mineralization and compromised mechanical properties of bone.PMID 34718219Read ↗

Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomesSemantic proximity Read ↗

Loss of Type I Collagen Telopeptide Lysyl Hydroxylation Causes Musculoskeletal Abnormalities in a Zebrafish Model of Bruck Syndrome.Semantic proximity Read ↗

Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17.Semantic proximity Read ↗

Loss of the long form of Plod2 phenocopies contractures of Bruck syndrome-osteogenesis imperfecta.Semantic proximity Read ↗

Lysyl hydroxylase 2 deficiency promotes filopodia formation and fibroblast migration.Semantic proximity Read ↗

Loss of lysyl hydroxylase 2 activates CRP-mediated cancer invasion through MEK/ERK/MMP9 signaling in the bone-microenvironmentSemantic proximity Read ↗

Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2.Semantic proximity Read ↗

Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.Semantic proximity Read ↗

Tissue-specific changes in the hydroxylysine content and cross-links of collagens and alterations in fibril morphology in lysyl hydroxylase 1 knock-out mice.Semantic proximity Read ↗

Collagens and their abnormalities in a wide spectrum of diseases.Semantic proximity Read ↗

Collagens: molecular biology, diseases, and potentials for therapy.Semantic proximity Read ↗

Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.