scholarly journals Temperature-Responsive Gelation of Type I Collagen Solutions Involving Fibril Formation and Genipin Crosslinking as a Potential Injectable Hydrogel

2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Shunji Yunoki ◽  
Yoshimi Ohyabu ◽  
Hirosuke Hatayama
Keyword(s):  
Room Temperature ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I ◽  
Temperature Responsive ◽  
Moderate Change ◽  
Living Tissues ◽  
Cell Carriers ◽  
Temperature Responses ◽  
Gel System

We investigated the temperature-responsive gelation of collagen/genipin solutions using pepsin-solubilized collagen (PSC) and acid-solubilized collagen (ASC) as substrates. Gelation occurred in the PSC/genipin solutions at genipin concentrations 0–2 mM under moderate change in temperature from 25 to 37°C. The PSC/genipin solutions exhibited fluidity at room temperature for at least 30 min, whereas the ASC/genipin solutions rapidly reached gel points. In specific cases PSC would be preferred over ASC as an injectable gel system. The temperature-responsive gelation of PSC/genipin solutions was due to temperature responses to genipin crosslinking and collagen fibril formation. The elastic modulus of the 0.5% PSC/genipin gel system could be adjusted in a range of 2.5 to 50 kPa by the PSC and genipin concentrations, suggesting that a PSC/genipin solution is a potential injectable gel system for drug and cell carriers, with mechanical properties matching those of living tissues.

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 Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

2010 ◽  
Vol 285 (23) ◽  
pp. 17465-17470 ◽  
Author(s):  
Saori Kunii ◽  
Koichi Morimoto ◽  
Kouhei Nagai ◽  
Takuya Saito ◽  
Kenji Sato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
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.

scholarly journals Matrix fully loaded: Assembly and secretion of collagen fibrils

2003 ◽  
Vol 25 (5) ◽  
pp. 11-13
Author(s):  
Karl E. Kadler ◽  
Elizabeth G. Canty ◽  
Yinhui Lu
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Secretory Pathway ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Collagen Fibrils ◽  
Type I ◽  
Small Proteins ◽  
Unpublished Work ◽  
Structural Work

The secretory pathway operates like a well-oiled machine when it comes to secreting small proteins. But how does it cope with stiff rod-like molecules such as type I collagen, which spontaneously self-assembles into the millimetre-long collagen fibrils that are characteristic of the extracellular matrix (ECM)? A recent study in our laboratory shows that the secretory pathway adapts exquisitely to intracellular fibril formation by creating tubular vesicles that dock to specialized secretory nozzles in the plasma membrane (E.G. Canty, Y. Lu, R.M. Meadows, M. Shaw, D.F. Holmes and K.E. Kadler, unpublished work). This article gives a brief account of the biochemical and structural work that led up to these new observations.

scholarly journals Thermoneutral housing attenuates premature cancellous bone loss in male C57BL/6J mice

2019 ◽  
Vol 8 (11) ◽  
pp. 1455-1467 ◽  
Author(s):  
Stephen A Martin ◽  
Kenneth A Philbrick ◽  
Carmen P Wong ◽  
Dawn A Olson ◽  
Adam J Branscum ◽  
...  
Keyword(s):  
Bone Loss ◽  
Cancellous Bone ◽  
Room Temperature ◽  
Type I Collagen ◽  
Distal Femur ◽  
Volume Fraction ◽  
Lumbar Vertebra ◽  
Published Data ◽  
Type I ◽  
Housing Temperature

Mice are a commonly used model to investigate aging-related bone loss but, in contrast to humans, mice exhibit cancellous bone loss prior to skeletal maturity. The mechanisms mediating premature bone loss are not well established. However, our previous work in female mice suggests housing temperature is a critical factor. Premature cancellous bone loss was prevented in female C57BL/6J mice by housing the animals at thermoneutral temperature (where basal rate of energy production is at equilibrium with heat loss). In the present study, we determined if the protective effects of thermoneutral housing extend to males. Male C57BL/6J mice were housed at standard room temperature (22°C) or thermoneutral (32°C) conditions from 5 (rapidly growing) to 16 (slowly growing) weeks of age. Mice housed at room temperature exhibited reductions in cancellous bone volume fraction in distal femur metaphysis and fifth lumbar vertebra; these effects were abolished at thermoneutral conditions. Mice housed at thermoneutral temperature had higher levels of bone formation in distal femur (based on histomorphometry) and globally (serum osteocalcin), and lower global levels of bone resorption (serum C-terminal telopeptide of type I collagen) compared to mice housed at room temperature. Thermoneutral housing had no impact on bone marrow adiposity but resulted in higher abdominal white adipose tissue and serum leptin. The overall magnitude of room temperature housing-induced cancellous bone loss did not differ between male (current study) and female (published data) mice. These findings highlight housing temperature as a critical experimental variable in studies using mice of either sex to investigate aging-related changes in bone metabolism.

“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

scholarly journals Comparison of Physicochemical Characteristics and Fibril Formation Ability of Collagens Extracted from the Skin of Farmed River Puffer (Takifugu obscurus) and Tiger Puffer (Takifugu rubripes)

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 462 ◽  
Author(s):  
Wang ◽  
Yu ◽  
Sun ◽  
Liu ◽  
Zhou
Keyword(s):  
Type I Collagen ◽  
Molecular Form ◽  
Formation Rate ◽  
Helical Structure ◽  
Fibril Formation ◽  
Takifugu Rubripes ◽  
Type I ◽  
Soluble Collagen ◽  
Skin Collagen ◽  
Tiger Puffer

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin of river puffer (ASC-RP and PSC-RP) and tiger puffer (ASC-TP and PSC-TP) were extracted and physicochemically examined. Denaturation temperature (Td) for all the collagens was found to be 25.5–29.5 °C, which was lower than that of calf skin collagen (35.9 °C). Electrophoretic patterns indicated all four samples were type I collagen with molecular form of (α1)2α2. FTIR spectra confirmed the extracted collagens had a triple-helical structure, and that the degree of hydrogen bonding in ASC was higher than PSC. All the extracted collagens could aggregate into fibrils with D-periodicity. The fibril formation rate of ASC-RP and PSC-RP was slightly higher than ASC-TP and PSC-TP. Turbidity analysis revealed an increase in fibril formation rate when adding a low concentration of NaCl (less than 300 mM). The fibril formation ability was suppressed with further increasing of NaCl concentration, as illustrated by a reduction in the turbidity and formation degree. SEM analysis confirmed the well-formed interwoven structure of collagen fibrils after 24 h of incubation. Summarizing the experimental results suggested that the extracted collagens from the skin of river puffer and tiger puffer could be considered a viable substitute to mammalian-derived collagens for further use in biomaterial applications.

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