scholarly journals Structure–function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro

2000 ◽  
Vol 349 (3) ◽  
pp. 877-883 ◽  
Author(s):  
Christy A. THOMSON ◽  
Vettai S. ANANTHANARAYANAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Molar Ratio ◽  
Functional Assay ◽  
Type I ◽  
Ph Dependent ◽  
Ph Range

Hsp47, a 47kDa heat shock protein whose expression level parallels that of collagen, has been regarded as a collagen-specific molecular chaperone. Studies from other laboratories have established the association of Hsp47 with the nascent as well as the triple-helical procollagen molecule in the endoplasmic reticulum and its dissociation from procollagen in the Golgi. One of several roles suggested for Hsp47 in collagen biosynthesis is the prevention of aggregation of procollagen in the endoplasmic reticulum. However, no experimental evidence has been available to verify this suggestion. In the present study we have followed the aggregation of mature triple-helical collagen molecules into fibrils by using turbidimetric measurements in the absence and presence of Hsp47. In the pH range 6–7, fibril formation of type I collagen, as monitored by turbidimetry, proceeds with a lag of approx. 10min and levels off by approx. 60min. The addition of Hsp47 at pH 7 effectively inhibits fibril formation at and above a 1:1 molar ratio of Hsp47 to triple-helical collagen. This inhibition is markedly pH-dependent, being significantly diminished at pH 6. CD and fluorescence spectral data of Hsp47 in the pH range 4.2–7.4 reveal a significant alteration in its structure at pH values below 6.2, with a decrease in α-helix and an increase in β-structure. This conformational change is likely to be the basis of the decreased binding of Hsp47 to collagen in vitro at pH 6.3 as well as its inability to inhibit collagen fibril formation at this pH. Our results also provide a functional assay for Hsp47 that can be used in studies on collagen and Hsp47 interactions.

scholarly journals The Mammalian Chitinase-like Lectin, YKL-40, Binds Specifically to Type I Collagen and Modulates the Rate of Type I Collagen Fibril Formation

2006 ◽  
Vol 281 (30) ◽  
pp. 21082-21095 ◽  
Author(s):  
Heather F. Bigg ◽  
Robin Wait ◽  
Andrew D. Rowan ◽  
Tim E. Cawston
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis

2006 ◽  
Vol 17 (5) ◽  
pp. 2346-2355 ◽  
Author(s):  
Yoshihito Ishida ◽  
Hiroshi Kubota ◽  
Akitsugu Yamamoto ◽  
Akira Kitamura ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Type I Collagen ◽  
Intracellular Localization ◽  
Fibril Formation ◽  
Mouse Embryos ◽  
Type I ◽  
Collagen Types ◽  
Protease Digestion ◽  
Triple Helices ◽  
Increased Susceptibility

Heat-shock protein of 47 kDa (Hsp47) is a molecular chaperone that recognizes collagen triple helices in the endoplasmic reticulum (ER). Hsp47-knockout mouse embryos are deficient in the maturation of collagen types I and IV, and collagen triple helices formed in the absence of Hsp47 show increased susceptibility to protease digestion. We show here that the fibrils of type I collagen produced by Hsp47-/- cells are abnormally thin and frequently branched. Type I collagen was highly accumulated in the ER of Hsp47-/- cells, and its secretion rate was much slower than that of Hsp47+/+ cells, leading to accumulation of the insoluble aggregate of type I collagen within the cells. Transient expression of Hsp47 in the Hsp47-/- cells restored normal extracellular fibril formation and intracellular localization of type I collagen. Intriguingly, type I collagen with unprocessed N-terminal propeptide (N-propeptide) was secreted from Hsp47-/- cells and accumulated in the extracellular matrix. These results indicate that Hsp47 is required for correct folding and prevention of aggregation of type I collagen in the ER and that this function is indispensable for efficient secretion, processing, and fibril formation of collagen.

“In Vitro” Fibril Formation of type I Collagen from Different Sources: Biochemical and Morphological Aspects

1986 ◽  
Vol 15 (4) ◽  
pp. 235-244 ◽  
Author(s):  
Maurizia Valli ◽  
Luisa Leonardi ◽  
Rita Strocchi ◽  
Ruggero Tenni ◽  
Stefano Guizzardi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Fibril Formation ◽  
Type I ◽  
Morphological Aspects ◽  
Different Sources

scholarly journals Osteopontin regulates type I collagen fibril formation in bone tissue

2020 ◽  
Author(s):  
Baptiste Depalle ◽  
Catriona M. McGilvery ◽  
Sabah Nobakhti ◽  
Nouf Aldegaither ◽  
Sandra J. Shefelbine ◽  
...  
Keyword(s):  
Bone Tissue ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Effect of UV irradiation on type I collagen fibril formation in neutral collagen solutions

2001 ◽  
Vol 17 (3) ◽  
pp. 114-120 ◽  
Author(s):  
Julian M. Menter ◽  
Abrienne M. Patta ◽  
Robert M. Sayre ◽  
John Dowdy ◽  
Isaac Willis
Keyword(s):  
Uv Irradiation ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Characterization of Type I Collagen Fibril Formation Using Thioflavin T Fluorescent Dye

2009 ◽  
Vol 145 (5) ◽  
pp. 677-684 ◽  
Author(s):  
K. Morimoto ◽  
K. Kawabata ◽  
S. Kunii ◽  
K. Hamano ◽  
T. Saito ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Fluorescent Dye ◽  
Thioflavin T ◽  
Type I

scholarly journals Matrix metalloproteinase 14 is required for fibrous tissue expansion

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Susan H Taylor ◽  
Ching-Yan Chloé Yeung ◽  
Nicholas S Kalson ◽  
Yinhui Lu ◽  
Paola Zigrino ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibrous Tissue ◽  
Tissue Expansion ◽  
Collagen Fibrils ◽  
Collagen I ◽  
Type I ◽  
Tendon Development

Type I collagen-containing fibrils are major structural components of the extracellular matrix of vertebrate tissues, especially tendon, but how they are formed is not fully understood. MMP14 is a potent pericellular collagenase that can cleave type I collagen in vitro. In this study, we show that tendon development is arrested in Scleraxis-Cre::Mmp14 lox/lox mice that are unable to release collagen fibrils from plasma membrane fibripositors. In contrast to its role in collagen turnover in adult tissue, MMP14 promotes embryonic tissue formation by releasing collagen fibrils from the cell surface. Notably, the tendons grow to normal size and collagen fibril release from fibripositors occurs in Col-r/r mice that have a mutated collagen-I that is uncleavable by MMPs. Furthermore, fibronectin (not collagen-I) accumulates in the tendons of Mmp14-null mice. We propose a model for cell-regulated collagen fibril assembly during tendon development in which MMP14 cleaves a molecular bridge tethering collagen fibrils to the plasma membrane of fibripositors.

scholarly journals Structural Property of Decorin from Small Intestine and its Effect of Type I Collagen Fibril Formation

1998 ◽  
Vol 69 (8) ◽  
pp. 779-791
Author(s):  
Yoshihiro NOMURA ◽  
Takahiro MIZUTANI ◽  
Yasuhiro ISHII ◽  
Kunio SHIRAI
Keyword(s):  
Small Intestine ◽  
Structural Property ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

scholarly journals Restoration of Osteogenesis by CRISPR/Cas9 Genome Editing of the Mutated COL1A1 Gene in Osteogenesis Imperfecta

2021 ◽  
Vol 10 (14) ◽  
pp. 3141
Author(s):  
Hyerin Jung ◽  
Yeri Alice Rim ◽  
Narae Park ◽  
Yoojun Nam ◽  
Ji Hyeon Ju
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Disease Modeling ◽  
Bone Fragility ◽  
Osteogenic Potential ◽  
Type I ◽  
Gene Correction ◽  
Col1a1 Gene ◽  
Collagen Formation

Osteogenesis imperfecta (OI) is a genetic disease characterized by bone fragility and repeated fractures. The bone fragility associated with OI is caused by a defect in collagen formation due to mutation of COL1A1 or COL1A2. Current strategies for treating OI are not curative. In this study, we generated induced pluripotent stem cells (iPSCs) from OI patient-derived blood cells harboring a mutation in the COL1A1 gene. Osteoblast (OB) differentiated from OI-iPSCs showed abnormally decreased levels of type I collagen and osteogenic differentiation ability. Gene correction of the COL1A1 gene using CRISPR/Cas9 recovered the decreased type I collagen expression in OBs differentiated from OI-iPSCs. The osteogenic potential of OI-iPSCs was also recovered by the gene correction. This study suggests a new possibility of treatment and in vitro disease modeling using patient-derived iPSCs and gene editing with CRISPR/Cas9.

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