Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis–trans isomerases, is only partially inhibited by FK506

Zeng, Bijun; Macdonald, J. Randy; Bann, James G.; Beck, Konrad; Gambee, Jay E.; Boswell, Bruce A.; Bächinger, H P

doi:10.1042/bj3300109

Cited by 52 publications

(63 citation statements)

References 38 publications

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“…Beyond its prolyl 3 hydroxylase activity, the com plex functions as a PPIase and chaperone for collagen folding 13,19,23 . Indeed, the fast propagation of the triple helix requires the isomerization of cis peptide bonds that convert proline residues into trans configuration, mainly by PPIase B 24 (FIG. 3c).…”

Section: Mechanisms/pathophysiologymentioning

confidence: 99%

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Osteogenesis imperfecta

Marini

Forlino

Bächinger

et al. 2017

Nat Rev Dis Primers

545

582

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| Skeletal deformity and bone fragility are the hallmarks of the brittle bone dysplasia osteogenesis imperfecta. The diagnosis of osteogenesis imperfecta usually depends on family history and clinical presentation characterized by a fracture (or fractures) during the prenatal period, at birth or in early childhood; genetic tests can confirm diagnosis. Osteogenesis imperfecta is caused by dominant autosomal mutations in the type I collagen coding genes (COL1A1 and COL1A2) in about 85% of individuals, affecting collagen quantity or structure. In the past decade, (mostly) recessive, dominant and X-linked defects in a wide variety of genes encoding proteins involved in type I collagen synthesis, processing, secretion and post-translational modification, as well as in proteins that regulate the differentiation and activity of bone-forming cells have been shown to cause osteogenesis imperfecta. The large number of causative genes has complicated the classic classification of the disease, and although a new genetic classification system is widely used, it is still debated. Phenotypic manifestations in many organs, in addition to bone, are reported, such as abnormalities in the cardiovascular and pulmonary systems, skin fragility, muscle weakness, hearing loss and dentinogenesis imperfecta. Management involves surgical and medical treatment of skeletal abnormalities, and treatment of other complications. More innovative approaches based on gene and cell therapy, and signalling pathway alterations, are under investigation. NATURE REVIEWS | DISEASE PRIMERS VOLUME 3 | ARTICLE NUMBER 17052 | 1 PRIMER © 2 0 1 7 M a c m i l l a n P u b l i s h e r s L i m i t e d , p a r t o f S p r i n g e r N a t u r e . A l l r i g h t s r e s e r v e d .In this Primer, we provide an overview of epidemio logy, genetics and pathophysiology of osteogenesis imperfecta, as well as diagnosis and management. EpidemiologyStudies from Europe and the United States have found a birth prevalence of osteogenesis imperfecta of 0.3-0.7 per 10,000 births 5,6 . These birth cohort analyses reflect more severe types of osteogenesis imperfecta and do not include more subtle types that become apparent after birth. A population based study that used the Danish National Patient Register found an annual incidence of osteogenesis imperfecta of 1.5 per 10,000 births between 1997 and 2013 (REF. 7). Population surveys in countries with comprehensive medical databases, such as Finland, estimated a prevalence of about 0.5 per 10,000 individ uals 8 , with most having phenotypically milder osteo genesis imperfecta type I and type IV (BOX 1; TABLE 1). Because these birth cohort and population surveys are based on clinical findings and tend to find mutu ally exclusive populations, a reasonable estimate of the incidence of osteogenesis imperfecta is about 1 per 10,000 individuals. Most patients are heterozygous for mutations in COL1A1 or COL1A2. No difference in the prevalence between sexes was reported.Approximately 90% of the 3,000 individuals whose mutations ha...

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Section: Mechanisms/pathophysiologymentioning

confidence: 99%

“…Serpin H1 stabilizes the folded pro collagens in the rER and assists their shuttling into the cis Golgi [25][26][27] . FKBP65 also has PPIase activity 24 .…”

Section: Box 1 | Classification Of Osteogenesis Imperfectamentioning

confidence: 99%

Osteogenesis imperfecta

Marini

Forlino

Bächinger

et al. 2017

Nat Rev Dis Primers

545

582

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“…CypB Complex-The chicken P3H1⅐CRTAP⅐CypB complex was isolated from 15-17-day-old chick embryos following the previously published protocol (17,18) with modifications to improve both yield and purity of the complex. 12 dozen chick embryos were mixed with an equal volume of 10 mM Tris/HCl buffer, pH 7.5, containing 0.25 M sucrose and protease inhibitors (5 mM EDTA, 2 mM phenylmethylsulfonyl fluoride, 2 mM N-ethylmaleimide, 1 g/ml pepstatin A, and 1 g/ml leupeptin).…”

Section: Extraction and Purification Of The Chicken P3h1⅐crtap⅐mentioning

confidence: 99%

Biochemical Characterization of the Prolyl 3-Hydroxylase 1·Cartilage-associated Protein·Cyclophilin B Complex

Ishikawa

Wirz

Vranka

et al. 2009

Journal of Biological Chemistry

106

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The rough endoplasmic reticulum-resident protein complex consisting of prolyl 3-hydroxylase 1 (P3H1), cartilage-associated protein (CRTAP), and cyclophilin B (CypB) can be isolated from chick embryos on a gelatin-Sepharose column, indicating some involvement in the biosynthesis of procollagens. Prolyl 3-hydroxylase 1 modifies a single proline residue in the ␣ chains of type I, II, and III collagens to (3S)-hydroxyproline. The peptidyl-prolyl cistrans isomerase activity of cyclophilin B was shown previously to catalyze the rate of triple helix formation. Here we show that cyclophilin B in the complex shows peptidyl-prolyl cis-trans isomerase activity and that the P3H1⅐CRTAP⅐CypB complex has another important function: it acts as a chaperone molecule when tested with two classical chaperone assays. The P3H1⅐CRTAP⅐CypB complex inhibited the thermal aggregation of citrate synthase and was active in the denatured rhodanese refolding and aggregation assay. The chaperone activity of the complex was higher than that of protein-disulfide isomerase, a well characterized chaperone. The P3H1⅐CRTAP⅐CypB complex also delayed the in vitro fibril formation of type I collagen, indicating that this complex is also able to interact with triple helical collagen and acts as a collagen chaperone.

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“…It is still unclear which function of CypB is crucial during procollagen biosynthesis. FKBP65 was initially proposed to be a tropoelastin chaperone (34) and later was identified as a procollagen molecular chaperone during biosynthesis and maturation (12,35). This protein consists of four FKBP domains, two EF-hand motifs, and an rER retention signal.…”

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confidence: 99%

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Ishikawa

Bächinger

2014

Journal of Biological Chemistry

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Background: Procollagen biosynthesis requires a large number of foldases, chaperones, and modifying enzymes. Results: FKBP22 is a foldase and chaperone that interacts with a subset of collagens. Conclusion: Collagen type-specific chaperones and foldases exist in the rER. Significance: The lack of collagen type-specific rER proteins can lead to broader or overlapping phenotypes of connective tissue disorders.

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Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis–trans isomerases, is only partially inhibited by FK506

Cited by 52 publications

References 38 publications

Osteogenesis imperfecta

Osteogenesis imperfecta

Biochemical Characterization of the Prolyl 3-Hydroxylase 1·Cartilage-associated Protein·Cyclophilin B Complex

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

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