scholarly journals Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

1979 ◽  
Vol 177 (1) ◽  
pp. 81-98 ◽  
Author(s):  
Lola Cohen-Solal ◽  
Jane B. Lian ◽  
Dora Kossiva ◽  
Melvin J. Glimcher
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Proteinase Inhibitors ◽  
Organic Phosphorus ◽  
Bone Matrix ◽  
Bone Collagen ◽  
Insoluble Residue ◽  
Cationic Amino Acid ◽  
Chicken Bone ◽  
Covalently Bound

Non-collagenous phosphoproteins, almost all of which can be extracted in EDTA at neutral pH in the presence of proteinase inhibitors, are identified in the matrix of chicken bone, and are therefore not covalently bound to collagen. Similarly, all the peptides containing γ-carboxyglutamic acid are present in the EDTA extract and none in the insoluble residue, confirming that none is covalently linked to chicken bone collagen. However, organic phosphorus is also found to be present in chicken bone collagen, principally in the α2-chains. Of the total protein-bound organic phosphorus present in chicken bone matrix, approx. 80% is associated with the non-collagenous proteins and 20% with collagen. The soluble non-collagenous proteins contain both O-phosphoserine and O-phosphothreonine and these account for essentially of their organic phosphorus content. In contrast, collagen contains neither O-phosphoserine nor O-phosphothreonine. Indeed, no phosphorylated hydroxy amino acid, phosphoamidated amino acid or phosphorylated sugar could be identified in purified components of collagen, which contain approximately four to five atoms of organic phosphorus per molecule of collagen. Peptides containing organic phosphorus were isolated from partial acid hydrolysates and enzymic digests of purified collagen components, which contain an as-yet-unidentified cationic amino acid. These data, the very high concentrations of glutamic acid in the phosphorylated peptides, and the pH-stability of the organic phosphorus moiety in intact collagen chains strongly suggest that at least part of the organic phosphorus in collagen is present as phosphorylated glutamic acid. This would indicate that the two major chemically different protein fractions in chicken bone matrix that contain organic phosphorus may represent two distinct metabolic pools of organic phosphorus under separate biological control.

scholarly journals Collagen heterogeneity within different growth regions of long bones of rachitic and nonrachitic chicks

1972 ◽  
Vol 127 (4) ◽  
pp. 715-720 ◽  
Author(s):  
Bryan P. Toole ◽  
Andrew H. Kang ◽  
Robert L. Trelstad ◽  
Jerome Gross
Keyword(s):  
Vitamin D ◽  
Amino Acid ◽  
Bone Matrix ◽  
Bone Collagen ◽  
Long Bone ◽  
Long Bones ◽  
Collagen Structure ◽  
Collagen Molecules ◽  
Relationship Of ◽  
Chain Type

The different anatomical regions involved in osteogenesis in the chick long bone have been examined for heterogeneities in collagen structure that might relate to the mechanism of ossification. Experimentally induced lathyrism was employed to enhance collagen solubility, and vitamin D deficiency to allow accumulation of osteoid, the precursor of bone matrix. The extractable lathyritic collagens of the cartilaginous and osseous regions of growing long bones from rachitic and non-rachitic chicks were examined for α-chain type and amino acid composition. In both groups of animals the growth plate and cartilaginous regions of the epiphysis gave collagen molecules of the constitution [α1(II)]3, whereas the ossifying regions contained [α1(I)]2 α2. The degree of hydroxylation of the lysine moieties was increased by approximately 50% in the α1(I)-chain and α2-chain of rachitic bone collagen. Since uncalcified osteoid is greatly enriched in rachitic bone, it is concluded that the collagen of osteoid has the configuration [α1(I)]2 α2, similar to that of bone matrix, but has an elevated hydroxylysine content. The possible relationship of this difference to the mechanism of calcification is discussed.

Organic Phosphorus Content of the Alpha Chains of Chicken Bone Collagen

Nature ◽  
1967 ◽  
Vol 214 (5088) ◽  
pp. 621-622 ◽  
Author(s):  
C. J. FRANCOIS ◽  
M. J. GLIMCHER ◽  
S. M. KRANE
Keyword(s):  
Phosphorus Content ◽  
Organic Phosphorus ◽  
Bone Collagen ◽  
Chicken Bone

scholarly journals Collagen cross-linking. Isolation of cross-linked peptides from collagen of chicken bone

1973 ◽  
Vol 135 (3) ◽  
pp. 393-403 ◽  
Author(s):  
D. R. Eyre ◽  
M. J. Glimcher
Keyword(s):  
Amino Acid ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Cross Linking ◽  
Bacterial Collagenase ◽  
Chicken Bone ◽  
Cross Links ◽  
The Cross ◽  
Significant Pathway ◽  
Carboxy Terminal

Cross-linked peptides were isolated from chicken bone collagen that had been digested with CNBr or with bacterial collagenase. Analyses of 3H radioactivity in disc electrophoretic profiles of the CNBr peptides from bone collagens that had been treated with NaB3H indicated that a major site of intermolecular cross-linking in chicken bone collagen is located between the carboxy-terminal region of an α1 chain and a small CNBr peptide, probably situated near the amino-terminus of an α1 or α2 chain in an adjacent collagen molecule. A small amount of this cross-linked CNBr peptide was isolated from a CNBr digest of chicken bone collagen by column chromatography. Amino acid analysis showed that the CNBr peptide, α1CB6B, the carboxy-terminal peptide of the α1 chain, was the major CNBr peptide in the preparation, and the reduced cross-linking components were identified as hydroxylysinohydroxynorleucine (HylOHNle), with a smaller amount of hydroxylysinonorleucine (HylNle). However, the composition and the low recovery of the cross-linking amino acids suggested that the preparation was a mixture of CNBr peptides α1CB6B and α1CB6B cross-linked to a small CNBr peptide whose identity could not be determined. A small cross-linked peptide was isolated from chicken bone collagen that had been reduced with NaB3H4 and digested with bacterial collagenase. This peptide was the major cross-linked peptide in the digest and contained a stoicheiometric amount of the reduced cross-linking compounds. A peptide which had the same amino acid composition, but contained the cross-linking compounds in their reducible forms, was isolated from a collagenase digest of chicken bone collagen that had not been treated with NaBH4. The absence of the reduced cross-links from this peptide indicates that, at least for the cross-linking site from which the peptide derives, natural reduction is not a significant pathway for biosynthesis of stable cross-links. However, most of the reducible cross-linking component in the peptide appeared to stabilize in the bone collagen by rearrangement from aldimine to ketoamine form.

A bone matrix calcification-initiator noncollagenous protein

1977 ◽  
Vol 232 (3) ◽  
pp. C115-C127 ◽  
Author(s):  
M. R. Urist ◽  
A. J. Mikulski ◽  
M. Nakagawa ◽  
K. Yen
Keyword(s):  
Calcium Binding ◽  
Binding Capacity ◽  
Bone Matrix ◽  
Bone Collagen ◽  
Chemical Extraction ◽  
Insoluble Residue ◽  
Affinity Constant ◽  
Sequential Chemical Extraction

When completely demineralized, the densely packed structure of bone matrix does not recalcify, neither in physiologic solutions in vitro nor in implants in vivo. Even when inorganic and organic calcification inhibitors (which normally are stored in bone matrix) are removed first by autolytic digestion in neutral buffers at 37C and then by sequential chemical extraction, implants of the EDTA insoluble residue will not recalcify after as long as 4 wk in a muscle pouch. However, if first demineralized in cold dilute HCl, second, extracted and autodigested in buffers solution at 37C, and then further extracted in EDTA and other solutions at 2C, a calcification initiator protein (Cp) is unmasked, and the residue will invariable recalcify. CIP, isolated by gel filtration and column chromatography, is a disulfide-bonded glycoprotein aggregate composed of subunites of a moleclar mass of 55,000. CIP is composed of a large proportion of acidic amino acids and has a calcium binding capacity of about 1.8 times greater than albumin. The affinity constant CaCIP, calculated by ultrafiltration of physiologic solutions of Ca2+, is log K, 2.9. Observations on implants of residues that containe a) CIP but not a bone morphogenetic property (BMP), B) BMP accompanied by CIP activity, or c) neither BMP nor CIP activity suggested that BMP covers CIP and that the two are attached to bone collagen in tandem. Whether CIP plays a part in calcification of the normal skeleton requires further investigation.

Collagen-the Ultrastructural Element of the Bone Matrix

2018 ◽  
Vol 69 (7) ◽  
pp. 1706-1709
Author(s):  
Nicoleta Dumitru ◽  
Andra Cocolos ◽  
Andra Caragheorgheopol ◽  
Constantin Dumitrache ◽  
Ovidiu Gabriel Bratu ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Bone Microarchitecture ◽  
Complex Structure ◽  
Bone Matrix ◽  
Organic Matrix ◽  
Bone Diseases ◽  
Bone Collagen ◽  
Type I ◽  
New Therapeutic Approaches ◽  
And Function

There is an increased interest and more studies highlight the fact that bone strength depends not only on bone tissue quantity, but also on its quality, which is characterized by the geometry and shape of bones, trabecular bone microarchitecture, mineral content, organic matrix and bone turnover. Fibrillar type I collagen is the major organic component of bone matrix, providing form and a stable template for mineralization. The biomedical importance of collagen as a biomaterial for medical and cosmetic purposes and the improvement of the molecular, cellular biology and analytical technologies, led to increasing interest in establishing the structure of this protein and in setting of the relationships between sequence, structure, and function. Bone collagen crosslinking chemistry and its molecular packing structure are considered to be distinct features. This unique post-translational modifications provide to the fibrillar collagen matrices properties such as tensile strength and viscoelasticity. Understanding the complex structure of bone type I collagen as well as the dynamic nature of bone tissues will help to manage new therapeutic approaches to bone diseases.

scholarly journals Phosphoproteins of chicken bone matrix. Proof of synthesis in bone tissue.

1984 ◽  
Vol 259 (1) ◽  
pp. 290-293
Author(s):  
M J Glimcher ◽  
D Kossiva ◽  
D Brickley-Parsons
Keyword(s):  
Bone Tissue ◽  
Bone Matrix ◽  
Chicken Bone

scholarly journals Rational design of novel amphipathic antimicrobial peptides focused on the distribution of cationic amino acid residues

MedChemComm ◽  
2019 ◽  
Vol 10 (6) ◽  
pp. 896-900 ◽  
Author(s):  
Takashi Misawa ◽  
Chihiro Goto ◽  
Norihito Shibata ◽  
Motoharu Hirano ◽  
Yutaka Kikuchi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Human Cell ◽  
Hemolytic Activity ◽  
Rational Design ◽  
Cell Cytotoxicity ◽  
Amino Acid Residues ◽  
High Antimicrobial Activity ◽  
Cationic Amino Acid ◽  
Helical Peptide

Amphipathic helical peptideStripeshowed high antimicrobial activity, low hemolytic activity, and low human cell cytotoxicity.

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