Thermal Properties of Mineralized and Non Mineralized Type I Collagen in Bone

2002 ◽  
Vol 724 ◽  
Author(s):  
L. F. Lozano ◽  
M. A. Peña-Rico ◽  
H. Jang-Cho ◽  
A. Heredia ◽  
E. Villarreal ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Combustion Process ◽  
Stability Loss ◽  
Human Bone ◽  
Type I ◽  
Global Effect ◽  
Cross Links ◽  
The Stability ◽  
Thermal Stability Of

AbstractThe research about the structural stability of bone, as a composite material, compromises a complete understanding of the interaction between the mineral and organic phases. The thermal stability of human bone and type I collagen extracted from human bone by different methods was studied in order to understand the interactions between the mineral and organic phases when is affected by a degradation/combustion process. The experimental techniques employed were calorimetry and infrared spectroscopy (FTIR) techniques. The extracted type I collagens result to have a bigger thermal stability with a Tmax at 500 and 530 Celsius degrees compared with the collagen present in bone with Tmax at 350 Celsius degrees. The enthalpy value for the complete degradation/combustion process were similar for all the samples, being 8.4 +- 0.11 kJ/g for recent bones diminishing with the antiquity, while for extracted collagens were 8.9 +- 0.07 and 7.9 +-1.01 kJ/g. These findings demonstrate that the stability loss of type I collagen is due to its interactions with the mineral phase, namely carbonate hydroxyapatite. This cause a change in the molecular properties of the collagen during mineralization, specifically in its cross-links and other chemical interactions, which have a global effect over the fibers elasticity, but gaining tensile strength in bone as a whole tissue. We are applying this characterization to analyze the diagenetic process of bones with archaeological interest in order to identify how the environmental factors affect the molecular structure of type I collagen. In bone samples that proceed from an specific region with the same environmental conditions, the enthalpy value per unit mass was found to diminish exponentially with respect to the bone antiquity.

scholarly journals Thermal stability of human-fibroblast-collagenase-cleavage products of type-I and type-III collagens

1987 ◽  
Vol 247 (3) ◽  
pp. 725-729 ◽  
Author(s):  
C C Danielsen
Keyword(s):  
Thermal Stability ◽  
Human Fibroblast ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Melting Temperatures ◽  
Large Type ◽  
Fibroblast Collagenase ◽  
Thermal Stability Of

Rat skin type-I and type-III collagens were degraded by human fibroblast collagenase at a temperature below the ‘melting’ temperature for the two resulting fragments, namely the N-terminal three-fourths, TCA, and the C-terminal one-fourth, TCB. The specific cleavage of the collagen was confirmed by electrophoresis and determination of molecular length by electron microscopy. The two fragments were separated by gel filtration and the thermal stabilities of the isolated fragments were determined. For type-I collagen, the ‘melting’ temperatures of the two fragments were found to differ by only 0.5 degrees C and were 4.5-5.0 degrees C below that of the uncleaved molecule. The ‘melting’ temperatures of the uncleaved molecule and the N-terminal fragment were independent of the extent of N-terminal intramolecular cross-linking. For type-III collagen, the ‘melting’ temperatures of the fragments were found to differ by 1.3 degrees C. The small fragments of the two types of collagen ‘melted’ at the same temperature, whereas the large type-III fragment ‘melted’ at a slightly higher temperature than did the large type-I fragment. Reduction of the disulphide bonds located in the C-terminal type-III fragment did not affect the thermal stability of this fragment. The thermal stability of uncleaved type-III collagen was found to be variable, but the reason for this is not known at present.

Changes in mechanical properties, thermal stability, reducible cross-links and glycosyl-lysines in rat skin induced by corticosteroid treatment

1982 ◽  
Vol 101 (2) ◽  
pp. 312-320 ◽  
Author(s):  
Hans Oxlund ◽  
Trevor Sims ◽  
Nicholas D. Light
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Corticosteroid Treatment ◽  
Biochemical Properties ◽  
Type Iii Collagen ◽  
Type I ◽  
Clinical Observations ◽  
Skin Collagen ◽  
Lysine Residues ◽  
Cross Links

Abstract. The effects of systemic cortisol treatment on the biophysical and biochemical properties of skin were investigated. Rats were injected sc with cortisol for 14, 60 and 120 days and samples of lumbar skin were studied. Corticosteroids exert a biphasic effect on the strength of skin: 1) a relatively fast increase in the strength and stability, caused by an increased collagen cross-linking and 2) an inhibited collagen synthesis which ultimately results in a thinning of the skin and a decrease of collagen content consistent with clinical observations. The thermal stability is increased indicating an increased proportion of thermostable cross-links in skin collagen. No changes are observed in the percentage type III collagen with respect to type I collagen. Increased amounts of glucose attached to the ε-amino group of lysine residues in the collagen are found after long-term treatments, an alteration which may play a role in hampering the tissue functions.

scholarly journals Embryonic avian cornea contains layers of collagen with greater than average stability.

1986 ◽  
Vol 103 (4) ◽  
pp. 1587-1593 ◽  
Author(s):  
T F Linsenmayer ◽  
E Gibney ◽  
J M Fitch
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Type I ◽  
Corneal Tissue ◽  
Tissue Sections ◽  
Triple Helical Domain ◽  
Thermal Stability Of

A unique morphological feature of the embryonic avian cornea is the uniformity of its complement of striated collagen fibrils, each of which has a diameter of 25 nm. We have asked whether this apparent morphological uniformity also reflects an inherent uniformity of the structural and physical properties of these fibrils. For this we have examined the in situ thermal stability of the type I collagen within these fibrils. Corneal tissue sections were reacted at progressively higher temperatures with conformation-dependent monoclonal antibodies directed against the triple-helical domain of the type I collagen molecule. These studies show that the cornea contains layers of collagen fibrils with greater than average stability. The two most prominent of these extend uninterrupted across the entire width of the cornea, and then appear to insert into thick bundles of scleral collagen, which in turn appear to insert into the scleral ossicles, a ring of bony plates which circumscribe the sclera of the avian eye. Once formed, the bands may act to stabilize the shape of the cornea or, conversely, to alter it during accommodation.

scholarly journals Characterization of N-glycosylated type I collagen in streptozotocin-induced diabetes

1981 ◽  
Vol 197 (2) ◽  
pp. 405-412 ◽  
Author(s):  
A Le Pape ◽  
J P Muh ◽  
A J Bailey
Keyword(s):  
Type I Collagen ◽  
Accelerated Aging ◽  
Diabetic Rats ◽  
Type I ◽  
Significant Extent ◽  
Streptozotocin Induced Diabetes ◽  
Cross Links ◽  
The Stability

The N epsilon-glycosylation of lysine and hydroxylysine residues in collagen from streptozotocin-induced-diabetic rats was confirmed and the stability of the complex shown to be due to an Amadori rearrangement. The studies also demonstrate the relative specificities of glucose, galactose and mannose in their reaction with collagen. The glycosylation of lysine in vitro occurs with glucose and galactose, but not with mannose, whereas only gucose reacts with hydroxylysine to any significant extent. Glycosylation of collagen occurs slowly during normal aging, but in contrast with reports suggesting accelerated aging of collagen in diabetic animals, we clearly demonstrated that the apparent increased stability is not due to an acceleration of the normal maturation process involving the reducible cross-links.

scholarly journals Difference in thermal stability of type-I and type-III collagen from rat skin

1982 ◽  
Vol 203 (1) ◽  
pp. 323-326 ◽  
Author(s):  
Carl Christian Danielsen
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Neutral Salt ◽  
Rat Skin ◽  
Thermal Stabilities ◽  
Type Iii ◽  
Thermal Stability Of ◽  
Salt Fractionation

Type-I and type-III collagens were obtained by differential salt fractionation of neutral-salt-soluble collagen from rat skin. Their thermal stabilities were determined by u.v. difference spectroscopy. The ‘melting’ temperature (Tm) in 5mm-acetic acid of type-III collagen was almost 2°C above that of type-I collagen. Intramolecular covalent cross-linking had no effect on the thermal stability.

scholarly journals Collagen molecular phenotypic switch between non-neoplastic and neoplastic canine mammary tissues

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masahiko Terajima ◽  
Yuki Taga ◽  
Becky K. Brisson ◽  
Amy C. Durham ◽  
Kotaro Sato ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Mammary Carcinoma ◽  
Cancer Biology ◽  
Type I Collagen ◽  
Critical Role ◽  
Premature Death ◽  
Mammary Tissue ◽  
Type I ◽  
Cross Links

AbstractIn spite of major advances over the past several decades in diagnosis and treatment, breast cancer remains a global cause of morbidity and premature death for both human and veterinary patients. Due to multiple shared clinicopathological features, dogs provide an excellent model of human breast cancer, thus, a comparative oncology approach may advance our understanding of breast cancer biology and improve patient outcomes. Despite an increasing awareness of the critical role of fibrillar collagens in breast cancer biology, tumor-permissive collagen features are still ill-defined. Here, we characterize the molecular and morphological phenotypes of type I collagen in canine mammary gland tumors. Canine mammary carcinoma samples contained longer collagen fibers as well as a greater population of wider fibers compared to non-neoplastic and adenoma samples. Furthermore, the total number of collagen cross-links enriched in the stable hydroxylysine-aldehyde derived cross-links was significantly increased in neoplastic mammary gland samples compared to non-neoplastic mammary gland tissue. The mass spectrometric analyses of type I collagen revealed that in malignant mammary tumor samples, lysine residues, in particular those in the telopeptides, were markedly over-hydroxylated in comparison to non-neoplastic mammary tissue. The extent of glycosylation of hydroxylysine residues was comparable among the groups. Consistent with these data, expression levels of genes encoding lysyl hydroxylase 2 (LH2) and its molecular chaperone FK506-binding protein 65 were both significantly increased in neoplastic samples. These alterations likely lead to an increase in the LH2-mediated stable collagen cross-links in mammary carcinoma that may promote tumor cell metastasis in these patients.

Intrinsic Thermal Stability of Anisotropic Thin-Film Superconductors

1990 ◽  
Vol 112 (1) ◽  
pp. 10-15 ◽  
Author(s):  
M. I. Flik ◽  
C. L. Tien
Keyword(s):  
Thin Film ◽  
Thermal Stability ◽  
Stability Criterion ◽  
High Temperature Superconductors ◽  
Stability Criteria ◽  
Anisotropic Thermal Conductivity ◽  
Operating Current ◽  
Released Energy ◽  
The Stability ◽  
Thermal Stability Of

Intrinsic thermal stability denotes a situation where a superconductor can carry the operating current without resistance at all times after the occurrence of a localized release of thermal energy. This novel stability criterion is different from the cryogenic stability criteria for magnets and has particular relevance to thin-film superconductors. Crystals of ceramic high-temperature superconductors are likely to exhibit anisotropic thermal conductivity. The resultant anisotropy of highly oriented films of superconductors greatly influences their thermal stability. This work presents an analysis for the maximum operating current density that ensures intrinsic stability. The stability criterion depends on the amount of released energy, the Biot number, the aspect ratio, and the ratio of the thermal conductivities in the plane of the film and normal to it.

scholarly journals Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited

2009 ◽  
Vol 185 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Farideh Sabeh ◽  
Ryoko Shimizu-Hirota ◽  
Stephen J. Weiss
Keyword(s):  
Cancer Cells ◽  
Type I Collagen ◽  
Three Dimensional ◽  
Amoeboid Movement ◽  
Type I ◽  
Collagen Network ◽  
Normal Tissues ◽  
Tissue Invasion ◽  
Absolute Requirement ◽  
Cross Links

Tissue invasion during metastasis requires cancer cells to negotiate a stromal environment dominated by cross-linked networks of type I collagen. Although cancer cells are known to use proteinases to sever collagen networks and thus ease their passage through these barriers, migration across extracellular matrices has also been reported to occur by protease-independent mechanisms, whereby cells squeeze through collagen-lined pores by adopting an ameboid phenotype. We investigate these alternate models of motility here and demonstrate that cancer cells have an absolute requirement for the membrane-anchored metalloproteinase MT1-MMP for invasion, and that protease-independent mechanisms of cell migration are only plausible when the collagen network is devoid of the covalent cross-links that characterize normal tissues.

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