Therapeutic Effect of Nile Tilapia Type II Collagen on Rigidity in CD8+ Cells by Alleviating Inflammation and Rheumatoid Arthritis in Rats by Oral Tolerance

Abstract

Fibrillins are microfibril-associated macro glycoproteins found in connective tissues and structurally related to latent TGF-β-binding proteins (LTBPs). The special cellular immunity and blocking glycoprotein receptors IIb and IIIa of fibrillins are emerging topics in recent years. In this study, Nile Tilapia type IIcollagen (NTCII) was extracted and purified from the skull cartilages by a pepsin-soluble method. Amino acid analysis indicated that NTCII consisted of 315/1000 glycine residues, 72/1000 hydroxyproline residues and 108/1000 proline residues. SDS-PAGE analysis showed that NTCII was composed of three identical 130 kDa α-chains. The results of glycoprotein/carbohydrate assay indicated that the total polysaccharide content of NTCII was 5.6–19.0%. The IR spectrum of NTCII displayed five characteristic peaks of amide I, II, III, A, B. NTCII at 10–100 μg/mL concentration downregulated the content of cytokines in the presence or absence of LPS, especially the secretion of cytokines IL-6, IL-1β and TNF-α. Interestingly, NTCII promoted the secretion of Fas/Apo-1 compared to the control group and 25 μg/mL of NTCII resulted in a higher Fas/Apo-1 secretion level in CD8+ T cells. FITC-TCII fluorescence images confirmed that NTCII could bind to the membrane surface of CD8+ T cells, leading to the induction of rigidity. NTCII could bind to the membrane surface of CD8+ T cells that leads to the induction of rigidity, as evidenced by the FITC-NTCII fluorescence images. The qRT-PCR gene expression analysis of caspase-8 collected with Fas/Apo-1 was upregulated significantly in the 1 and 50 μg/mL NTCII-treated groups compared with the control group. Overall, the results conclude that the rigidity did not lead to an increase in inflammatory factors in CD8+ T cells treated with NTCII. The oral administration of NTCII 3 mg/kg dosage caused more prominent repair of damaged ankle cartilage than the 1 mg/kg dosage in Freund’s adjuvant-induced model of arthritis in rats. Therefore, this study disclosed the immunological and anti-arthritic effect of fibrillar collagen, which could be a potential biomaterial for practical applications with lower toxicity.

Stem-Cell-Regenerative and Protective Effects of Squid (Symplectoteuthis oualaniensis) Skin Collagen Peptides against H2O2-Induced Fibroblast Injury

“…The presence of hydrogen bonding was indicated by the observation of the amide III band at 1236 cm −1 . The IR ratio of the band positions at 1236 cm −1 (amide III) and 1539 cm −1 (amide II) was determined to be 1.24, indicating that both PSC and ASC maintained the intact triple-helix structure [ 48 ]. The amide III band of SCP was detected at 1408 cm −1 , likely indicating the participation of the N-H group in peptide synthesis.…”

Oral Administration of Protease-Soluble Chicken Type II Collagen Ameliorates Anterior Cruciate Ligament Transection–Induced Osteoarthritis in Rats

“…In PSCC-II, only pepsin-soluble undenatured C-II extracted from chicken sternal cartilage is available on the nutraceutical market. The use of marine pepsin-soluble undenatured C-II sourced from the skulls and cartilage of Nile tilapia and sturgeon is in the research stage [ 57 , 58 ]. Epidemiological studies have revealed that OA is a complex disease characterized by chronic joint pain, inflammation, synovitis, bone remodeling, and cartilage loss [ 59 , 60 ].…”

Collagen Supplementation for Joint Health: The Link between Composition and Scientific Knowledge

“…Insoluble undenatured native collagens are characterized for being non-soluble in water as well as for exhibiting antigenic sites (epitopes), which depend on collagen type and consequently on the raw material used. The preservation of certain collagen epitopes, associated to fibrillar structure, has been shown to be involved in immune-mediated effects [ 45 , 46 ]. Hence, if the raw material is mostly composed by cartilaginous tissue, such as chicken sternum, the resulting product is known as insoluble undenatured type II collagen [ 39 ].…”