scholarly journals Collagen-Derived Peptides in CKD: A Link to Fibrosis

Toxins ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 10
Author(s):  
Emmanouil Mavrogeorgis ◽  
Harald Mischak ◽  
Agnieszka Latosinska ◽  
Antonia Vlahou ◽  
Joost P. Schanstra ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Estimated Glomerular Filtration Rate ◽  
Collagen Type ◽  
Strong Association ◽  
Post Translational Modifications ◽  
Collagen Peptides ◽  
Strong Negative Association ◽  
Main Protein ◽  
Healthy Participants

Collagen is a major component of the extracellular matrix (ECM) and has an imminent role in fibrosis, in, among others, chronic kidney disease (CKD). Collagen alpha-1(I) (col1a1) is the most abundant collagen type and has previously been underlined for its contribution to the disease phenotype. Here, we examined 5000 urinary peptidomic datasets randomly selected from healthy participants or patients with CKD to identify urinary col1a1 fragments and study their abundance, position in the main protein, as well as their correlation with renal function. We identified 707 col1a1 peptides that differed in their amino acid sequence and/or post-translational modifications (hydroxyprolines). Well-correlated peptides with the same amino acid sequence, but a different number of hydroxyprolines, were combined into a final list of 503 peptides. These 503 col1a1 peptides covered 69% of the full col1a1 sequence. Sixty-three col1a1 peptides were significantly and highly positively associated (rho > +0.3) with the estimated glomerular filtration rate (eGFR), while only six peptides showed a significant and strong, negative association (rho < −0.3). A similar tendency was observed for col1a1 peptides associated with ageing, where the abundance of most col1a1 peptides decreased with increasing age. Collectively the results show a strong association between collagen peptides and loss of kidney function and suggest that fibrosis, potentially also of other organs, may be the main consequence of an attenuation of collagen degradation, and not increased synthesis.

scholarly journals Putative amino acid sequence of HLA-DRB chain contributing to rheumatoid arthritis susceptibility.

1989 ◽  
Vol 169 (6) ◽  
pp. 2263-2268 ◽  
Author(s):  
Y Watanabe ◽  
K Tokunaga ◽  
K Matsuki ◽  
F Takeuchi ◽  
K Matsuta ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequences ◽  
Strong Association ◽  
Amino Acid Residues ◽  
Net Charge ◽  
Drb Gene ◽  
Polymerase Chain

The association between HLA-DR4 and rheumatoid arthritis (RA) has been established in many ethnic groups. To clarify the determinant of susceptibility to RA, a polymorphic segment of the HLA-DRB gene was amplified in vitro by polymerase chain reaction and analyzed with oligonucleotide probes specific for the HLA-DR4 DNA sequences. A particular sequence encoding amino acids Gln70-Arg71-Arg72-Ala73-Ala74 showed a strong association with RA (p less than 0.005, relative risk 6.0). This amino acid sequence occurs in the DRB molecules with three RA-associated specificities, DR4/Dw14, DR4/Dw15, and DR1. DR4/Dw4, which is common in Caucasian RA patients, has a strikingly similar amino acid sequence Gln70-Lys71-Arg72-Ala73-Ala74 in terms of polarity and charge profiles. Other RA nonassociated sequences differ from this sequence by at least one amino acid substitution that causes the change of the net charge. The composition of amino acid residues at the positions 70-74 may play a crucial role in the pathogenesis of RA.

Inhibition by Peptidic Fragments of Clq of Platelet - Collagen Interactions

1979 ◽  
Author(s):  
J.L. wautier ◽  
K.B.M. Reid ◽  
Y. Legrand ◽  
J.P. Caen
Keyword(s):  
Amino Acid ◽  
Platelet Aggregation ◽  
Amino Acid Sequence ◽  
Platelet Adhesion ◽  
Type Iii Collagen ◽  
Type I ◽  
Inhibit Platelet Aggregation ◽  
Pepsin Digestion ◽  
Type Iii ◽  
Collagen Peptides

Clq (first component of complement) has been shown to inhibit platelet aggregation induced by collagen. Platelet aggregation and adhesion to purified type I or type III collagen have been studied in the presence of various fragment of Clq.The collagen like region was obtained by digestion of Clq by pepsin and by isolation of the fragments by chromatography on sephadex G 200. The globular region was prepared by digestion of Clq by collagenase, and filtration. The collagen like region is as effective as native Clq in inhibiting platelet aggregation or adhesion in the presence of type I or type III collagen, while the globular region was without effect.Using peptides obtained from the collagen like region of Clq (reduction and alkylation, performic oxidation, CNBr treatment, extensive pepsin digestion) it could be shown that the fragment (FR II = 70 Amino Acid) was responsible for the inhibition of the platelet adhesion and aggregation induced by type I or type III collagen.The Amino Acid sequence of this fragment was compared to the known sequence of the collagen peptides involved in platelet adhesion (see Fauvel et al).

scholarly journals Palaeoproteomic evidence identifies archaic hominins associated with the Châtelperronian at the Grotte du Renne

2016 ◽  
Vol 113 (40) ◽  
pp. 11162-11167 ◽  
Author(s):  
Frido Welker ◽  
Mateja Hajdinjak ◽  
Sahra Talamo ◽  
Klervia Jaouen ◽  
Michael Dannemann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Europe ◽  
Collagen Type ◽  
Transitional Period ◽  
Upper Paleolithic ◽  
Amino Acid Sequence Analysis ◽  
Physiological Information ◽  
Anatomically Modern Humans ◽  
Mass Spectometry

In Western Europe, the Middle to Upper Paleolithic transition is associated with the disappearance of Neandertals and the spread of anatomically modern humans (AMHs). Current chronological, behavioral, and biological models of this transitional period hinge on the Châtelperronian technocomplex. At the site of the Grotte du Renne, Arcy-sur-Cure, morphological Neandertal specimens are not directly dated but are contextually associated with the Châtelperronian, which contains bone points and beads. The association between Neandertals and this “transitional” assemblage has been controversial because of the lack either of a direct hominin radiocarbon date or of molecular confirmation of the Neandertal affiliation. Here we provide further evidence for a Neandertal–Châtelperronian association at the Grotte du Renne through biomolecular and chronological analysis. We identified 28 additional hominin specimens through zooarchaeology by mass spectrometry (ZooMS) screening of morphologically uninformative bone specimens from Châtelperronian layers at the Grotte du Renne. Next, we obtain an ancient hominin bone proteome through liquid chromatography-MS/MS analysis and error-tolerant amino acid sequence analysis. Analysis of this palaeoproteome allows us to provide phylogenetic and physiological information on these ancient hominin specimens. We distinguish Late Pleistocene clades within the genus Homo based on ancient protein evidence through the identification of an archaic-derived amino acid sequence for the collagen type X, alpha-1 (COL10α1) protein. We support this by obtaining ancient mtDNA sequences, which indicate a Neandertal ancestry for these specimens. Direct accelerator mass spectometry radiocarbon dating and Bayesian modeling confirm that the hominin specimens date to the Châtelperronian at the Grotte du Renne.

scholarly journals Amino Acid Sequence, Post-translational Modifications, Binding and Labelling of Porcine Odorant-binding Protein

1998 ◽  
Vol 23 (6) ◽  
pp. 689-698 ◽  
Author(s):  
S. Paolini ◽  
A. Scaloni ◽  
A. Amoresano ◽  
S. Marchese ◽  
E. Napolitano ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Post Translational Modifications ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

scholarly journals Amino acid sequence of the triple-helical domain of human collagen type VI.

1988 ◽  
Vol 263 (35) ◽  
pp. 18601-18606 ◽  
Author(s):  
M L Chu ◽  
D Conway ◽  
T C Pan ◽  
C Baldwin ◽  
K Mann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Collagen Type ◽  
Helical Domain ◽  
Collagen Type Vi ◽  
Human Collagen ◽  
Triple Helical Domain

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

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