scholarly journals Comparative Study of The Yield and Physicochemical Properties of Collagen from Sea Cucumber (Holothuria scabra), Obtained through Dialysis and the Ultrafiltration Membrane

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2564
Author(s):  
Suryani Saallah ◽  
Jumardi Roslan ◽  
Flavian Sheryl Julius ◽  
Sharinee Saallah ◽  
Umi Hartina Mohamad Razali ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Sea Cucumber ◽  
Large Scale ◽  
Type I Collagen ◽  
Ultrafiltration Membrane ◽  
The Body ◽  
Type I ◽  
Holothuria Scabra ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Collagen was extracted from the body wall of sea cucumber (Holothuria scabra) using the pepsin-solubilized collagen method followed by isolation using dialysis and the ultrafiltration membrane. The yield and physicochemical properties of the collagen obtained from both isolation methods, denoted as D-PSC and UF-PSC, were compared. The ultrafiltration method affords a higher yield of collagen (11.39%) than that of the dialysis (5.15%). The isolated collagens have almost the same amino acid composition, while their functional groups, referred to as amide A, B, I, II, and III bands, were in accordance with commercial collagen, as verified by Fourier Transform Infrared (FT-IR) spectroscopy. The UV-Vis absorption peaks at 240 nm and 220 nm, respectively, indicated that the collagens produced are type-I collagen. The D-PSC showed interconnecting sheet-like fibrils, while the UF-PSC exhibited a flaky structure with flat-sheets arranged very close to each other. The higher yield and comparable physicochemical properties of the collagen obtained by ultrafiltration as compared with dialysis indicate that the membrane process has high potential to be used in large-scale collagen production for food and pharmaceutical applications.

Type I collagen from sea cucumber (Stichopus japonicus) and the role of matrix metalloproteinase-2 in autolysis

2021 ◽  
Vol 41 ◽  
pp. 100959
Author(s):  
Long-Jie Yan ◽  
Le-Chang Sun ◽  
Kai-Yuan Cao ◽  
Yu-Lei Chen ◽  
Ling-Jing Zhang ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Sea Cucumber ◽  
Type I Collagen ◽  
Matrix Metalloproteinase 2 ◽  
Type I ◽  
Stichopus Japonicus

Regulation of collagen I gene expression by ras

1992 ◽  
Vol 12 (10) ◽  
pp. 4714-4723
Author(s):  
J L Slack ◽  
M I Parker ◽  
V R Robinson ◽  
P Bornstein
Keyword(s):  
Type I Collagen ◽  
The Body ◽  
Transformed Cells ◽  
Type I ◽  
Mrna Levels ◽  
Oncogenic Ras ◽  
Genes Encoding ◽  
Flanking Region ◽  
Collagen Genes ◽  
I Gene

Although transformation of rodent fibroblasts can lead to dramatic changes in expression of extracellular matrix genes, the molecular basis and physiological significance of these changes remain poorly understood. In this study, we have investigated the mechanism(s) by which ras affects expression of the genes encoding type I collagen. Levels of both alpha 1(I) and alpha 2(I) collagen mRNAs were markedly reduced in Rat 1 fibroblasts overexpressing either the N-rasLys-61 or the Ha-rasVal-12 oncogene. In fibroblasts conditionally transformed with N-rasLys-61, alpha 1(I) transcript levels began to decline within 8 h of ras induction and reached 1 to 5% of control levels after 96 h. In contrast, overexpression of normal ras p21 had no effect on alpha 1(I) or alpha 2(I) mRNA levels. Nuclear run-on experiments demonstrated that the transcription rates of both the alpha 1(I) and alpha 2(I) genes were significantly reduced in ras-transformed cells compared with those in parental cells. In addition, the alpha 1(I) transcript was less stable in transformed cells. Chimeric plasmids containing up to 3.6 kb of alpha 1(I) 5'-flanking DNA and up to 2.3 kb of the 3'-flanking region were expressed at equivalent levels in both normal and ras-transformed fibroblasts. However, a cosmid clone containing the entire mouse alpha 1(I) gene, including 3.7 kb of 5'- and 4 kb of 3'-flanking DNA, was expressed at reduced levels in fibroblasts overexpressing oncogenic ras. We conclude that oncogenic ras regulates the type I collagen genes at both transcriptional and posttranscriptional levels and that this effect, at least for the alpha 1(I) gene, may be mediated by sequences located either within the body of the gene itself or in the distal 3'-flanking region.

scholarly journals Regulation of collagen I gene expression by ras.

1992 ◽  
Vol 12 (10) ◽  
pp. 4714-4723 ◽  
Author(s):  
J L Slack ◽  
M I Parker ◽  
V R Robinson ◽  
P Bornstein
Keyword(s):  
Type I Collagen ◽  
The Body ◽  
Transformed Cells ◽  
Type I ◽  
Mrna Levels ◽  
Oncogenic Ras ◽  
Genes Encoding ◽  
Flanking Region ◽  
Collagen Genes ◽  
I Gene

Although transformation of rodent fibroblasts can lead to dramatic changes in expression of extracellular matrix genes, the molecular basis and physiological significance of these changes remain poorly understood. In this study, we have investigated the mechanism(s) by which ras affects expression of the genes encoding type I collagen. Levels of both alpha 1(I) and alpha 2(I) collagen mRNAs were markedly reduced in Rat 1 fibroblasts overexpressing either the N-rasLys-61 or the Ha-rasVal-12 oncogene. In fibroblasts conditionally transformed with N-rasLys-61, alpha 1(I) transcript levels began to decline within 8 h of ras induction and reached 1 to 5% of control levels after 96 h. In contrast, overexpression of normal ras p21 had no effect on alpha 1(I) or alpha 2(I) mRNA levels. Nuclear run-on experiments demonstrated that the transcription rates of both the alpha 1(I) and alpha 2(I) genes were significantly reduced in ras-transformed cells compared with those in parental cells. In addition, the alpha 1(I) transcript was less stable in transformed cells. Chimeric plasmids containing up to 3.6 kb of alpha 1(I) 5'-flanking DNA and up to 2.3 kb of the 3'-flanking region were expressed at equivalent levels in both normal and ras-transformed fibroblasts. However, a cosmid clone containing the entire mouse alpha 1(I) gene, including 3.7 kb of 5'- and 4 kb of 3'-flanking DNA, was expressed at reduced levels in fibroblasts overexpressing oncogenic ras. We conclude that oncogenic ras regulates the type I collagen genes at both transcriptional and posttranscriptional levels and that this effect, at least for the alpha 1(I) gene, may be mediated by sequences located either within the body of the gene itself or in the distal 3'-flanking region.

scholarly journals Differences of bone alkaline phosphatase isoforms in metastatic bone disease and discrepant effects of clodronate on different skeletal sites indicated by the location of pain

1998 ◽  
Vol 44 (8) ◽  
pp. 1621-1628 ◽  
Author(s):  
Per Magnusson ◽  
Lasse Larsson ◽  
Gunnar Englund ◽  
Brita Larsson ◽  
Peter Strang ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Type I Collagen ◽  
Specific Antigen ◽  
Bone Alkaline Phosphatase ◽  
The Body ◽  
Skeletal Metastases ◽  
Type I ◽  
Apparent Difference ◽  
Hormone Refractory ◽  
Healthy Males

Abstract We compared clodronate with placebo administration in 42 primarily or secondarily hormone-refractory prostate cancer patients with skeletal metastases and persisting pain. Serum total alkaline phosphatase (ALP), bone ALP isoforms, osteocalcin, cross-linked carboxy-terminal telopeptide of type I collagen, and prostate-specific antigen were analyzed before and after 1 month of treatment. Six ALP isoforms were quantified by HPLC: one bone/intestinal, two bone (B1, B2), and three liver ALP isoforms. The most apparent difference compared with healthy males was observed for the bone ALP isoform B2. Patients and healthy males had a B2 activity corresponding to 75% and 35% of the total ALP activity, respectively (P <0.0001). We propose that the different bone ALP isoforms reflect different stages of osteoblast differentiation during the extracellular matrix maturation phase of osteogenesis. All bone markers except osteocalcin increased after 1 month of clodronate administration. These increases were associated with pain only in the upper part of the body. We suggest that the uptake of clodronate by the skeleton was not uniform during our treatment period.

A MODEL OF TYPE I COLLAGEN FIBRILLOGENESIS BASED ON DIFFUSION LIMITED AGGREGATION

1995 ◽  
Vol 03 (04) ◽  
pp. 1033-1039
Author(s):  
JOHN PARKINSON ◽  
KARL E. KADLER ◽  
ANDY BRASS
Keyword(s):  
Type I Collagen ◽  
Unit Length ◽  
The Body ◽  
Biological Macromolecules ◽  
Type I ◽  
Structural Protein ◽  
Diffusion Limited Aggregation ◽  
Mass Unit ◽  
Diffusion Limited

The development of shape and form is intrinsic to the structure and function of many biological macromolecules including tubulin, actin and collagen. Type I collagen is a major structural protein in the body, providing mechanical strength for tissues such as bone and skin. It is present in the form of fibrils which display a regular banding pattern known as D-periodicity (where D = 67 nm). Type I collagen is a long rod-like molecule (300 nm ×1.5 nm) consisting of a triple helix formed from three polypeptide chains. In vivo and in vitro studies have shown that collagen molecules self-assemble in a regular D-staggered array to form striated fibrils. Further studies have shown that the process, termed fibrillogenesis, is entropy driven. A model based on diffusion limited aggregation was used to investigate the properties of rod self-assembly. This simple model reproduced several experimentally observed features of collagen fibril morphology including a linear mass/unit length profile and a preference for tip growth.

scholarly journals Extraction and Characterization of Collagen from Sand Sea Cucumber (Holothuria scabra)

2021 ◽  
Vol 26 (3) ◽  
pp. 319-327
Author(s):  
Gita Syahputra ◽  
Hariyatun Hariyatun ◽  
Muhammad Firdaus ◽  
Pugoh Santoso
Keyword(s):  
Molecular Weight ◽  
Sea Cucumber ◽  
Type I ◽  
Indonesian Seas ◽  
Holothuria Scabra ◽  
Aquatic Product ◽  
Electron Microscopy Analysis ◽  
Main Component ◽  
Almost All

Sand sea cucumber (Holothuria scabra) is an aquatic product that belongs to Echinodermata, a habitant in almost all Indonesian seas. The main component of the sea cucumber is protein, one of which is collagen. This study aimed to extract and characterize collagen from the species using the acid-base extraction method. The characterization of sea cucumber collagen includes molecular weight, amino acid components, Fourier transform infrared spectrophotometry, and scanning electron microscopy analysis. This study has successfully extracted collagen from the sample using an extraction system: NaOH 0.1 M; CH3COOH 0.1 M; and distilled water under 45°C treatments, gave 6% yield. The collagen has a molecular weight 110-130 kDa. Based on the infrared spectra, the specific functional groups of the collagen are amide A (3379.29 cm-1), amide B (2924.09 cm-1), amide I (1681.93 cm-1), amide II (1560.41 cm-1), and amide III (1249.87 cm-1). The collagen falls into type I. We suggest an alternative resource of collagen from sand sea cucumber, other than poultry and mammals.   Keywords: characterization, collagen, extraction, fishery, sand sea cucumber

scholarly journals Crotoxin Modulates Events Involved in Epithelial–Mesenchymal Transition in 3D Spheroid Model

Toxins ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 830
Author(s):  
Ellen Emi Kato ◽  
Sandra Coccuzzo Sampaio
Keyword(s):  
Tumor Cells ◽  
Type I Collagen ◽  
Epithelial Mesenchymal Transition ◽  
Metastatic Cancer ◽  
A549 Cells ◽  
The Body ◽  
Antitumor Action ◽  
Type I ◽  
Collagen Gels ◽  
Mesenchymal Transition

Epithelial–mesenchymal transition (EMT) occurs in the early stages of embryonic development and plays a significant role in the migration and the differentiation of cells into various types of tissues of an organism. However, tumor cells, with altered form and function, use the EMT process to migrate and invade other tissues in the body. Several experimental (in vivo and in vitro) and clinical trial studies have shown the antitumor activity of crotoxin (CTX), a heterodimeric phospholipase A2 present in the Crotalus durissus terrificus venom. In this study, we show that CTX modulates the microenvironment of tumor cells. We have also evaluated the effect of CTX on the EMT process in the spheroid model. The invasion of type I collagen gels by heterospheroids (mix of MRC-5 and A549 cells constitutively prepared with 12.5 nM CTX), expression of EMT markers, and secretion of MMPs were analyzed. Western blotting analysis shows that CTX inhibits the expression of the mesenchymal markers, N-cadherin, α-SMA, and αv. This study provides evidence of CTX as a key modulator of the EMT process, and its antitumor action can be explored further for novel drug designing against metastatic cancer.

Analysis of type I and IV collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue

2006 ◽  
Vol 386 (7-8) ◽  
pp. 1961-1966 ◽  
Author(s):  
Cyril Petibois ◽  
Gilles Gouspillou ◽  
Katia Wehbe ◽  
Jean-Paul Delage ◽  
Gérard Déléris
Keyword(s):  
Skeletal Muscle ◽  
Ir Spectroscopy ◽  
Connective Tissue ◽  
Type I ◽  
Molecular Investigation ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

scholarly journals Evidence for a Saponin Biosynthesis Pathway in the Body Wall of the Commercially Significant Sea Cucumber Holothuria scabra

Marine Drugs ◽  
2017 ◽  
Vol 15 (11) ◽  
pp. 349 ◽  
Author(s):  
Shahida Mitu ◽  
Utpal Bose ◽  
Saowaros Suwansa-ard ◽  
Luke Turner ◽  
Min Zhao ◽  
...  
Keyword(s):  
Sea Cucumber ◽  
Body Wall ◽  
The Body ◽  
Biosynthesis Pathway ◽  
Holothuria Scabra ◽  
Saponin Biosynthesis

scholarly journals Sea Cucumber Derived Type I Collagen: A Comprehensive Review

Marine Drugs ◽  
2020 ◽  
Vol 18 (9) ◽  
pp. 471 ◽  
Author(s):  
Tharindu R.L. Senadheera ◽  
Deepika Dave ◽  
Fereidoon Shahidi
Keyword(s):  
Sea Cucumber ◽  
Type I Collagen ◽  
Marine Invertebrates ◽  
Collagen Type I ◽  
Type I ◽  
Health Related ◽  
Alternative Sources ◽  
Living Organisms ◽  
Seafood Processing ◽  
By Products

Collagen is the major fibrillar protein in most living organisms. Among the different types of collagen, type I collagen is the most abundant one in tissues of marine invertebrates. Due to the health-related risk factors and religious constraints, use of mammalian derived collagen has been limited. This triggers the search for alternative sources of collagen for both food and non-food applications. In this regard, numerous studies have been conducted on maximizing the utilization of seafood processing by-products and address the need for collagen. However, less attention has been given to marine invertebrates and their by-products. The present review has focused on identifying sea cucumber as a potential source of collagen and discusses the general scope of collagen extraction, isolation, characterization, and physicochemical properties along with opportunities and challenges for utilizing marine-derived collagen.

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