Newt epidermal cell migration over collagen and fibronectin involves different mechanisms

1988 ◽  
Vol 90 (2) ◽  
pp. 325-333
Author(s):  
D.J. Donaldson ◽  
J.T. Mahan ◽  
G.N. Smith
Keyword(s):  
Synthetic Peptides ◽  
Cyanogen Bromide ◽  
Type I Collagen ◽  
Attachment Site ◽  
Inhibitory Effect ◽  
Type I ◽  
Fibroblast Attachment ◽  
Skin Explants ◽  
Cyanogen Bromide Fragment ◽  
Better Than

Effects of the synthetic peptides, Arg-Gly-Asp-Ser (RGDS), the amino acid sequence representing the fibroblast attachment site in fibronectin, and Arg-Gly-Glu-Ser (RGES), on collagen- and fibronectin-mediated migration in newt epidermal cells were compared. When RGDS at 50 micrograms ml-1 was included in the incubation medium of skin explants, migration in fibronectin-coated dishes was almost totally blocked. In type I collagen-coated dishes, this concentration of RGDS also inhibited migration, but to a lesser degree than on fibronectin. With 250 micrograms ml-1 of RGES in the medium, the reverse was true. Here, migration on collagen was practically non-existent, while migration on fibronectin was affected only moderately. Collagen-mediated migration was sensitive to RGDS even when the peptide was added after migration on the coated substratum was well underway. At a coating concentration of 10 micrograms ml-1 CB3, a cyanogen bromide fragment of the collagen alpha 1(I) chain, which contains no RGD sequences, was as good a migration substratum as intact collagen applied at the same coating concentration. At lower concentrations intact collagen was somewhat better than equivalent concentrations of CB3. The presence of RGDS in the medium throughout an experiment inhibited migration in CB3-coated dishes in a manner similar to its effect in dishes coated with collagen. On both substrata there appeared to be a peptide-sensitive and a peptide-insensitive component to migration. The inhibitory effect of RGES on CB3-mediated migration was also similar to its effect in collagen-coated dishes.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Activation of human neutrophils by type I collagen. Requirement of two different sequences

1990 ◽  
Vol 270 (2) ◽  
pp. 459-462 ◽  
Author(s):  
J C Monboisse ◽  
G Bellon ◽  
A Randoux ◽  
J Dufer ◽  
J P Borel
Keyword(s):  
Synthetic Peptides ◽  
Cyanogen Bromide ◽  
Type I Collagen ◽  
Competitive Inhibition ◽  
Polymorphonuclear Neutrophils ◽  
Human Neutrophils ◽  
Type I ◽  
Simultaneous Presence ◽  
Subsequent Activation ◽  
O2 Production

Contact between type I collagen purified from several species and human polymorphonuclear neutrophils (PMNs) triggers the production of O2.- by these cells. The activity of collagen is located in the alpha 1(I)-CB6 cyanogen bromide-cleaved (CB)-peptide, which is the C-terminal CB-peptide of the alpha 1(I) chain. Experiments based on the competitive inhibition of O2.- production by simultaneous incubation of PMNs with type I collagen and synthetic peptides identical to the conserved sequences of this collagen demonstrated that the binding of collagen to PMNs and the subsequent activation of these cells depend on the simultaneous presence of two sequences: Arg-Gly-Asp [residues 915, 916 and 917 of the complete alpha 1(I) chain, located in the helical part] Asp-Gly-Gly-Arg-Tyr-Tyr (residues 1034-1039, located in the C-terminal non-helical telopeptide).

scholarly journals Newt epidermal cell migration in vitro and in vivo appears to involve Arg-Gly-Asp-Ser receptors

1987 ◽  
Vol 87 (4) ◽  
pp. 525-534
Author(s):  
D.J. Donaldson ◽  
J.T. Mahan ◽  
G.N. Smith
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Wound Closure ◽  
Type I Collagen ◽  
Attachment Site ◽  
Epidermal Cells ◽  
Type I ◽  
Human Fibrinogen ◽  
Skin Explants

The effect of a synthetic peptide consisting of Arg-Gly-Asp-Ser (RGDS), the amino acid sequence representing the fibroblast attachment site in fibronectin (FN), was tested on migrating newt epidermal cells. In one approach, skin explants were placed on the bottom of plastic dishes coated with human FN, human fibrinogen (FGN), human serum spreading factor (SF), or bovine type I collagen. The explants were then incubated overnight in serum-free medium with or without RGDS. In these experiments exposure to 50 micrograms ml-1 of RGDS reduced migration over FN, FGN and SF to 2–7% of control levels. Two peptides structurally dissimilar to RGDS (Val-Gly-Ser-Glu and Thr-Pro-Arg-Lys), and two that are structurally similar (Lys-Gly-Asp-Ser and Arg-Gly-Glu-Ser), had no effect on explant migration even when used at concentrations higher than 50 micrograms ml-1. Upon removal of the RGDS peptide, inhibited explants quickly recovered. In collagen-coated dishes 50 micrograms ml-1 of RGDS was much less effective than in dishes coated with the other substrates. Raising the RGDS concentration in collagen-coated dishes tenfold did not greatly increase the RGDS effect. When added to the medium bathing wounded limbs, 50 micrograms ml-1 of RGDS only moderately inhibited wound closure. This concentration of peptide, however, severely inhibited migration from skin explants in newt-plasma-coated-dishes and migration over pieces of newt-plasma-coated plastic placed under one edge of a skin wound. Increasing the RGDS concentration to 500 micrograms ml-1 resulted in almost total suppression of wound closure. Wounds exposed to this same concentration of Lys-Gly-Asp-Ser closed normally. These results indicate that newt epidermal cells possess RGDS receptors and that these receptors are involved in epidermal wound closure in vivo and in migration from skin explants onto plastic coated with FN, FGN, SF and collagen. The relative RGDS-insensitivity of wound closure in vivo and in migration from explants onto collagen may reflect in these instances the presence of a relatively high density of RGDS receptor binding sites on the substrate; the presence of RGDS receptor binding sites of relatively high affinity; or the participation of receptors other than those involved in migration over plastic coated with FN, FGN or SF.

scholarly journals Identification of an immunosuppressive epitope of type II collagen that confers protection against collagen-induced arthritis.

1989 ◽  
Vol 170 (6) ◽  
pp. 1999-2010 ◽  
Author(s):  
L K Myers ◽  
J M Stuart ◽  
J M Seyer ◽  
A H Kang
Keyword(s):  
Amino Acids ◽  
Antibody Response ◽  
Synthetic Peptide ◽  
Synthetic Peptides ◽  
Cyanogen Bromide ◽  
Type I Collagen ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Induced Arthritis

We have previously reported that collagen-induced arthritis can be suppressed by intravenous injection of native type II (CII) but not type I collagen. We have now identified denatured fragments of CII capable of suppressing collagen-induced arthritis and inducing tolerance. Purified CII was cleaved with cyanogen bromide (CB), and the major resulting peptides were isolated. Female DBA/1 mice were administered OVA, native CII, or one of the CB peptides, intravenously, before immunization with native CII, 6 wk after immunization, mice tolerized with CII and CB11 had a markedly lower incidence of arthritis compared with controls. There was a correlation between the overall antibody response and the incidence of arthritis. In addition, animals tolerized with either CII or CB11 had a decreased antibody response not only to CII, but also to each of the other CB peptides tested. To identify the epitope involved in suppression of arthritis, five synthetic peptides, 21-26 amino acids in length, corresponding to selected regions of CB11, were generated. Each of the peptides was injected intravenously into mice before immunization. Only one of these, CB11 122-147, was capable of suppressing arthritis. In addition, mice given the synthetic peptide CB11 122-147 neonatally were suppressed for arthritis and antibody responsiveness when immunized with CII at 8 wk of age. Thus, we have identified CB11 122-147 as an epitope of CII important in induction of tolerance and suppression of disease. Further experiments narrowing down the pivotal amino acids for the immunogenicity of this epitope and the role this epitope plays in induction and regulation of disease will enhance our understanding of how the immune response to collagen affects autoimmune arthritis.

Immunoassay for quantifying type I collagen degradation products in urine evaluated

1994 ◽  
Vol 40 (11) ◽  
pp. 2022-2025 ◽  
Author(s):  
M Bonde ◽  
P Qvist ◽  
C Fledelius ◽  
B J Riis ◽  
C Christiansen
Keyword(s):  
Type I Collagen ◽  
Degradation Products ◽  
Mean Value ◽  
Collagen Degradation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Bone Resorption Marker ◽  
Type I ◽  
Analytical Recovery ◽  
Collagen Degradation Products ◽  
Better Than

Abstract An enzyme-linked immunosorbent assay (ELISA) for measuring type I collagen degradation products in urine < 3 h was evaluated. The measuring range was 0.5-10.5 mg/L with a detection limit of 0.2 mg/L. Within-run and total CVs were 5.3% and 6.6%, respectively. Analytical recovery averaged 100%. The mean (+/- SD) concentrations in urine samples from a healthy premenopausal population (n = 102) were 250 +/- 110 mg/mol creatinine (Cr). A group of healthy postmenopausal women (n = 410) gave a mean value of 416 +/- 189 mg/mol Cr. Values obtained in the ELISA correlated well (r = 0.83) to HPLC values for the established bone resorption marker deoxypyridinoline (n = 214), slightly better than the correlation to hydroxyproline measurements (r = 0.78, n = 421). We conclude that the assay described here presents a useful tool for further elucidating the importance of type I collagen degradation products in urine.

scholarly journals In vitro glycoxidation alters the interactions between collagens and human polymorphonuclear leucocytes

2000 ◽  
Vol 350 (3) ◽  
pp. 777-783 ◽  
Author(s):  
Jean-Claude MONBOISSE ◽  
Laure RITTIE ◽  
Hasnae LAMFARRAJ ◽  
Roselyne GARNOTEL ◽  
Philippe GILLERY
Keyword(s):  
Diabetes Mellitus ◽  
Type I Collagen ◽  
Inhibitory Effect ◽  
Type I ◽  
Polymorphonuclear Leucocytes ◽  
Type Iv ◽  
And Migration ◽  
Significant Stimulatory Effect

Glycation and glycoxidation processes, which are increased in diabetes mellitus, are generally considered causative mechanisms of long-term complications. With reference to our previous studies, type-I and -IV collagens could induce differentially the adhesion and stimulation of polymorphonuclear leucocytes (PMNs). As PMNs play a role in sustained diabetic oxidative stress, the present study was designed to determine whether in vitro glycoxidation of these macromolecules could alter PMN adhesion, activation and migration. The adhesion of PMNs to in vitro-glycoxidized collagens was significantly increased when compared with control collagens: +37% (P < 0.05) and +99% (P < 0.01) for collagens I and IV, respectively. Glycoxidized type-I collagen increased the chemotactic properties of PMNs without significant stimulatory effect on respiratory burst, whereas pre-incubation of PMNs with glycoxidized type-I collagen induced a priming on subsequent stimulation by N-formyl-methionyl-leucyl-phenylalanine. Glycoxidation of type-IV collagen suppressed its inhibitory effect on further PMN stimulation or migration. Collectively, these results indicate that glycoxidation of two major extracellular-matrix collagens considerably alters their ability to modulate PMN migration and production of reactive oxygen species. This imbalance in PMN metabolism may be a major event in the increased oxidative status that characterizes diabetes mellitus.

scholarly journals Effects of Toll-Like Receptors 3 and 4 in the Osteogenesis of Stem Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Chen Qi ◽  
Xu Xiaofeng ◽  
Wang Xiaoguang
Keyword(s):  
Stem Cells ◽  
Western Blot ◽  
Type I Collagen ◽  
Wnt Signaling Pathway ◽  
Inhibitory Effect ◽  
Type I ◽  
Toll Like Receptors ◽  
Blank Group ◽  
Alizarin Red ◽  
Marrow Mesenchymal Stem Cells

Objective. To investigate the effects of Toll-like receptors in stem cell osteogenesis.Methods. Bone marrow mesenchymal stem cells (BMSCs) were divided into the blank group, the TLR-3 activated group, and the TLR-4 activated group. After 10 days’ osteogenic-promoting culture, expression of type I collagen and osteocalcin was determined by Western blot. Osteoblasts (OBs) were also divided into three groups mentioned above. Alkaline phosphatase (ALP) and alizarin red staining were performed after 10 days’ ossification-inducing culture. The expression ofβ-catenin was investigated by Western blot.Results. Both the TLR-3 and TLR-4 activated groups had increased expression of type I collagen and osteocalcin; the effect of TLR-4 was stronger. The intensity of alizarin red and ALP staining was strongest in the TLR-3 activated group and weakest in the TLR-4 activated group. Activation of TLR-4 decreased the expression ofβ-catenin, whilst activation of TLR-3 did not affect the expression ofβ-catenin.Discussion. This study suggested that both TLR-3 and -4 promoted differentiation of BMSCs to OBs. TLR-3 had an inducing effect on the ossification of OBs to osteocytes, whilst the effect of TLR-4 was the opposite because of its inhibitory effect on the Wnt signaling pathway.

Mechanism of Endotoxin Inhibition of Human Gingival Fibroblast Attachment to Type I Collagen

1990 ◽  
Vol 69 (9) ◽  
pp. 1602-1606 ◽  
Author(s):  
S. Pitaru ◽  
D. Madgar ◽  
Z. Metzger ◽  
H. Hekmati
Keyword(s):  
Type I Collagen ◽  
Human Gingival Fibroblast ◽  
Type I ◽  
Gingival Fibroblast ◽  
Fibroblast Attachment

Insulin-like growth factor-I attenuates the inhibitory effect of type I collagen through β1 integrin receptor

2005 ◽  
Vol 336 (3) ◽  
pp. 836-841 ◽  
Author(s):  
Niraporn Chutivongse ◽  
Piyamas Sumrejkanchanakij ◽  
Tussanee Yongchaitrakul ◽  
Prasit Pavasant
Keyword(s):  
Growth Factor ◽  
Type I Collagen ◽  
Inhibitory Effect ◽  
Type I ◽  
Β1 Integrin ◽  
Insulin Like Growth Factor ◽  
Integrin Receptor ◽  
Factor I ◽  
Growth Factor I
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