Collagen-Derived Di-Peptide, Prolylhydroxyproline (Pro-Hyp): A New Low Molecular Weight Growth-Initiating Factor for Specific Fibroblasts Associated With Wound Healing
Many cells and soluble factors are involved in the wound healing process, which can be divided into inflammatory, proliferative and remodeling phases. Fibroblasts play a crucial role in cicatrising wounds, particularly during the proliferative phase and show heterogeneity depending on the lineage, distribution of tissues and the extent of differentiation. Fibroblasts of fabric stem cells rather than healthy tissues seep the wounds and proliferate. Some fibroblasts in the wound healing site express the mesenchymate stem cell marker, P75NTR. In the cell culture system, fibroblasts attached to collagen fibrils cease to grow, even in the presence of protein growth factors, thus imitating the nature of the quiescent nature of fibroblasts in healthy tissues.
Fibroblasts in wound healing sites proliferate and are surrounded by collagen fibrils. These facts indicate the presence of a new Growth Initiation Factor for Fibroblasts attached to collagen fibrils on the wound healing site, where the collagen derived peptide, proly-hydroxypolin (pro-hyp), is Generated. Pro-hy hyp triggers the growth of p75nt-positive fibroblasts grown on collagen gel but no p75ntr-negative fibroblasts. Thus, Pro-HYP is a low-growth initiation factor for the molecular weight for specific fibroblasts involved in the wound healing process. Pro-HYP is also supplied with tissues by oral administration of gelatin or collagen hydrolysate. Thus, the supplementation of gelatin or the collagen hydrolysate has a therapeutic potential for chronic wounds.
Animal studies and human clinical trials have shown that gelatin ingestion or collagen hydrolysat improves healing pressure ulcers in animals and humans and improves healing of delayed wound in diabetic animals . Therefore, the initiation factor in the growth of low molecular weight fibroblast, Pro-HYP, plays an important role in wound healing and has a therapeutic potential for chronic wounds.
Transforming the growth factor-β signaling into fibrotic diseases and fibroblasts associated with cancer
The transformation of the growth factor-β (TGF-β) is essential in the development of the embryo and the maintenance of normal homeostasis. In-depth evidence shows that TGF-β activation acts on several types of cells, including epithelial cells, fibroblasts and immune cells, in order to form a pro-fibrotic environment, finally leading to fibrotic diseases. TGF-β is stored in the matrix in a latent form; Once activated, it promotes a fibroblast of the transition of myofibroblast and regulates the extracellular matrix formation (ECM) and remodeling in fibrosis. TGF-β signaling can also promote cancer progression through its effects on tumor microenvironment.
In cancer, TGF-β contributes to the generation of fibroblasts associated with cancer (CAFS) with different molecular and cellular properties of activated or fibrotic fibroblasts. CAF promote the progression of tumor and chronic tumor fibrosis via TGF-β signaling. The progression of fibrosis fibrosis and the CAF negotiation share several common features and are closely linked. In this review, we examine the way TGF-β promotes the progression of fibrosis cancer and the mediation of the CAF.
We also discuss recent evidence suggesting inhibition of TGF-β as a defense against fibrotic disorders or the progression of mediated CAF cancer to highlight the potential implications of TGF-β targeted therapies for fibrosis and cancer. A total of 3412 patients with acute ischemic arc of China’s antihypertensive antihypertensive test from acute ischemic (Catis) with FGF-21 plasma measurements were included in this analysis. The main result was a combination of death or major disability (Modified Rankin balance score, ≥3) within one year after a stroke.
Collagen-Derived Di-Peptide, Prolylhydroxyproline (Pro-Hyp): A New Low Molecular Weight Growth-Initiating Factor for Specific Fibroblasts Associated With Wound Healing
M2B macrophages protect against myocardial remodeling after the prejudice of ischemia / EFFACTION by regulating the activation of growth factor receptor kinase derived from cardiac fibroblast platelets
Background: The myocardium injury is a major cause of myocardial remodeling. Macrophages are important in cardiac repair as a result of their interactions with fibroblasts. As regulatory macrophages, M2B macrophages modulate inflammatory immune responses without participating in wound healing and could have improved protective effects on the remodeling of myocardial. Therefore, we have tested the hypothesis that M2B macrophages could improve cardiac function and improve myocardial fibrosis after the myocardial injury of ischemia / edition (MI / RI).
Methods: Vivo, MI / RI models have been established with sprague-dawley rats (SD) and M2B macrophages (MT group) or the same vehicle volume (CK group) have been injected into the ischemic zone. Two weeks after the operation, the cardiac function and the diameters were determined by examination of echocardiography. The level of myocardial fibrosis has been measured by the Sirius red coloring and the expression of fibrosis-related factors. In vitro cardiac fibroblasts (CFS) were co-cultivated with m2b macrophages or grown with the M2B macrophage supernatant. The expression of α-smooth muscle actin (α-SMA) and the growth factor of the connective tissue (CCN2 / CTGF) in the CFS were measured by Western spots and immunofluorescence. In addition, the expression of growth factors derived from platelets (PDGF), the expression of growth factor receptors derived from platelets (PDGFR) and the phosphorylation of the PDGFRS were detected by Western blotting.
Results: A significantly higher rat survival rate, an improved left ventricularization system (LV), a decrease in the diameter of the LV and attenuated myocardial fibrosis was observed in the MT group than in the CK group. In vitro, the activation of CFS has been considerably reduced by M2B macrophages treatments, compared to the blank order. In addition, the activation of the Kinase of PDGFRS has been reduced by M2B macrophage treatments in vivo and in vitro.
FGF-1 Fibroblast Growth Factor-Acidic Human Recombinant Protein, Sf9
Description: Fibroblast Growth Factor-1 Human Recombinant (FGF-1) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of 15803 Dalton. ;The FGF-a is purified by proprietary chromatographic techniques.
FGF17 Fibroblast Growth Factor 17 Human Recombinant Protein
Description: FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.
FGF-2 Fibroblast Growth Factor Basic Bovine protein
Description: FGF-2 Bovine purified from bovine pituitary is a single, glycosylated, polypeptide chain having a molecular mass of 16kDa.;The basic-FGF is purified by proprietary chromatographic techniques.
FGF4 Fibroblast Growth Factor-4 Human Recombinant Protein
Description: FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. ;The FGF4 is purified by proprietary chromatographic techniques.
Description: FGF19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.8 kDa.;The FGF-19 is purified by proprietary chromatographic techniques.
FGF-8 Fibroblast Growth Factor-8 Human Recombinant Protein
Description: FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.
FGF-21 Fibroblast Growth Factor-21 Human Recombinant Protein
Description: Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and an N-terminal Methionin (bold), having a molecular weight of 19.5 kDa. ;The FGF-21 is purified by proprietary chromatographic techniques.
Description: FGF-2 Human Recombinant produced in rice is a single, non-glycosylated polypeptide chain containing 146 amino acids and having a molecular mass of ~17kDa.;The FGF-b protein is purified by proprietary chromatographic techniques.
FGFR2 Fibroblast Growth Factor Receptor 2 Fc ChimeraHuman Recombinant Protein
Description: Soluble FGFR-2a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain and having a molecular mass of 195 kDa. ;The FGFR2 is purified by proprietary chromatographic techniques.
Description: FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu28-Ala207) containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.
FGFR4 Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant Protein
Description: Soluble FGFR-4a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain and having a molecular mass of 170 kDa. ;The FGFR4 is purified by proprietary chromatographic techniques.
Description: FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.
FGF-21 Fibroblast Growth Factor-21 Mouse Recombinant Protein, His Tag
Description: Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.;The FGF-21 is purified by proprietary chromatographic techniques.
Conclusions: Our study has shown that M2B macrophages administration could mitigate myocardial remodeling after MI / RI. The regulation of the activation of CFS CFS is an important part of the protection mechanism.
Felicia
