Characterization of the α-chains of chick skin collagen and the nature of the amino-terminal cross-link region

Biochemistry ◽  
1969 ◽  
Vol 8 (9) ◽  
pp. 3648-3655 ◽  
Author(s):  
Andrew H. Kang ◽  
Karl A. Piez ◽  
Jerome Gross
Keyword(s):  
Cross Link ◽  
Amino Terminal ◽  
Skin Collagen

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

Self-assembly characterization of tilapia skin collagen in simulated body fluid with different salt concentrations

2021 ◽  
Author(s):  
Haohao Tian ◽  
Zhongyang Ren ◽  
Linfan Shi ◽  
Gengxin Hao ◽  
Jun Chen ◽  
...  
Keyword(s):  
Simulated Body Fluid ◽  
Self Assembly ◽  
Body Fluid ◽  
Skin Collagen

scholarly journals Preparation and Characterization of Magnetic Chitosan Microcapsules

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Xiaopeng Xiong ◽  
Yong Wang ◽  
Weiwei Zou ◽  
Jiangjiang Duan ◽  
Yun Chen
Keyword(s):  
Magnetic Properties ◽  
Strong Interaction ◽  
Liquid Paraffin ◽  
Hollow Microspheres ◽  
Composite Particles ◽  
Cross Link ◽  
Magnetic Chitosan ◽  
Starting Solution ◽  
Dense Shell

By dispersing aqueous precipitant in liquid paraffin to prepare a W/O emulsion then adding chitosan (CS) solution, CS microcapsules have been successfully prepared. It is a facile way to prepare polymer microcapsules by using aqueous precipitant or nonsolvent as template, which avoids the removal of template and would free from the necessity to cross-link the microcapsule as usual methods to directly form dense shell. The hollow feature of the obtained materials is revealed. The diameter of the microcapsules ranges from severalμm to over 100 μm. Magnetic CS microcapsules have been prepared in this way when Fe3+and Fe2+were mixed with CS to prepare a mixture starting solution. The appearance and microstructure of the composite microcapsules were studied. The results indicate that the formed Fe3O4nanoparticles are embedded in the CS matrix evenly due to strong interaction between the Fe3O4nanoparticles and the CS molecules. The Fe3O4content and the magnetic properties of the composite microcapsule were measured. The composite microcapsules were calcined in air at 700°C to prepare pure inorganic hollow microspheres. It is general to prepare hollow polymeric or composite particles by using this method.

scholarly journals Identification and characterization of a novel cytoskeleton-associated pp60src substrate.

1991 ◽  
Vol 11 (10) ◽  
pp. 5113-5124 ◽  
Author(s):  
H Wu ◽  
A B Reynolds ◽  
S B Kanner ◽  
R R Vines ◽  
J T Parsons
Keyword(s):  
Cell Structure ◽  
Transformed Cells ◽  
Cdna Clones ◽  
Amino Terminal ◽  
Multidomain Structure ◽  
Striking Change ◽  
Carboxyl Terminal ◽  
Amino Terminal Domain ◽  
Related Proteins

Transformation of cells by the src oncogene results in elevated tyrosine phosphorylation of two related proteins, p80 and p85 (p80/85). Immunostaining with specific monoclonal antibodies revealed a striking change of subcellular localization of p80/85 in src-transformed cells. p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. Sequence analysis of cDNA clones encoding p80/85 revealed an amino-terminal domain composed of six copies of a direct tandem repeat, each repeat containing 37 amino acids, a carboxyl-terminal SH3 domain, and an interdomain region composed of a highly charged acidic region and a region rich in proline, serine, and threonine. The multidomain structure of p80/85 and its colocalization with F-actin in normal and src-transformed cells suggest that these proteins may associate with components of the cytoskeleton and contribute to organization of cell structure.

Molecular cloning and characterization of an activated human c-raf-1 gene

1987 ◽  
Vol 7 (5) ◽  
pp. 1776-1781
Author(s):  
M Fukui ◽  
T Yamamoto ◽  
S Kawai ◽  
F Mitsunobu ◽  
K Toyoshima
Keyword(s):  
Dna Sequences ◽  
Promoter Sequence ◽  
Small Population ◽  
Dna Transfection ◽  
Amino Terminal ◽  
Human Dna ◽  
Nih 3T3 ◽  
Amino Terminal Sequence ◽  
Tumor Dna

Results of previous studies have shown that a raf-related transforming DNA sequence is present in NIH 3T3 transformants that are derived from GL-5-JCK human glioblastoma DNA transfection. The transforming DNA was molecularly cloned by using cosmid vector pJB8 to determine its structure and origin. Analyses of selected clones revealed that the transforming DNA consisted of three portions of human DNA sequences, with the 3' half of the c-raf-1 gene as its middle portion. This raf region was about 20 kilobases long and contained exons 8 to 17 and the poly(A) addition site. RNA blot analysis showed that the raf-related transforming DNA was transcribed into 5.3-, 4.8-, and 2.5-kilobase mRNAs; the 2.5-kilobase transcript was thought to be the major transcript. Immunoprecipitation analyses revealed that a 44-kilodalton raf-related protein was specifically expressed in the NIH 3T3 transformants. The raf-related transforming DNA was considered to be activated when its amino-terminal sequence was truncated and the DNA was coupled with a foreign promoter sequence. On hybridization analysis of the original GL-5-JCK glioblastoma DNA, no rearrangement of c-raf-1 was detectable in the tumor DNA. The rearrangement of c-raf-1 may have occurred during transfection or may have been present in a small population of the original tumor cells as a result of tumor progression.

scholarly journals Characterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid

2014 ◽  
Vol 5 (12) ◽  
pp. 954-957 ◽  
Author(s):  
Jia Kong ◽  
Bo Xu ◽  
Wei Wei ◽  
Xin Wang ◽  
Wei Xie ◽  
...  
Keyword(s):  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain ◽  
Hiv 1 ◽  
Dependent Interaction

scholarly journals Identification and biological activity of ovine and caprine calcitonin receptor-stimulating peptides 1 and 2

2008 ◽  
Vol 198 (2) ◽  
pp. 429-437 ◽  
Author(s):  
Christopher J Charles ◽  
Takeshi Katafuchi ◽  
Timothy G Yandle ◽  
Naoto Minamino
Keyword(s):  
Plasma Renin ◽  
New Members ◽  
Amino Terminal ◽  
Peptide Family ◽  
Plasma Camp ◽  
Receptor Activity Modifying Proteins ◽  
Conscious Sheep ◽  
Dose Dependent

We have recently reported the isolation of three new members of the calcitonin (CT) gene-related peptide family of peptides, the CT receptor (CT-R)-stimulating peptides (CRSPs). We now report the sequencing and characterization of ovine/caprine CRSP-1 and caprine CRSP-2. Mature ovine and caprine CRSP-1 are identical and have strong structural homology to CRSP-1s identified to date from other species. As with other CRSP-1s, ovine/caprine CRSP-1 binds to and activates the CT-R but not the CT-like receptor (CL-R) in combination with the receptor activity-modifying proteins (RAMPs). By contrast, caprine CRSP-2 does not activate any of these receptor-RAMP complexes. Intravenous infusions of ovine CRSP-1 to normal conscious sheep induced dose-dependent reduction in plasma total Ca levels (P=0.02) and corrected Ca levels (P=0.017) associated with increases in plasma cAMP (P=0.002). CRSP-1 reduced both plasma amino-terminal pro-C-type natriuretic peptide levels (P=0.006) and plasma renin activity (P=0.028). There were no significant effects observed on hemodynamic or renal indices measured. In conclusion, we have sequenced ovine/caprine CRSP-1 and caprine CRSP-2 precursors. This newly identified CRSP-1 has been shown to share the structural and biological features of CRSP-1s known to date. In vivo studies confirm that ovine CRSP-1 reduces plasma Ca levels in sheep, presumably via a cAMP-mediated mechanism. By contrast, caprine CRSP-2 did not stimulate any combination of CT-R, CL-R, and RAMPs. Accession numbers of cDNA determined in this study are caprine CRSP-1, AB364646; caprine CRSP-2, AB364647; and ovine CRSP-1, AB364648.

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