Collagen Secretion
Collagen Secretion - Related Videos
07:25
Collagen Hydrogels
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2023
Collagen is another widely used biomaterial that has found popularity in commercial applications, such as photography. Collagen has more recently been used in tissue engineering applications, by creating hydrogels that provide structure to engineered tissue. This video introduces collagen as a biomaterial, demonstrates how it is harvested from porcine skin, and shows how the material is used to create a hydrogel for tissue engineering applications. Finally, several applications of the material...
07:03
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Cited by 18 •
2014
This procedure demonstrates in vivo near IR fluorescence imaging of collagen remodeling activities in mice as well as ex vivo staining of collagens in tissue sections using caged collagen mimetic peptides that can be photo-triggered to hybridize with denatured collagen strands.
07:48
Three-Dimensional In Vitro Biomimetic Model of Neuroblastoma Using Collagen-Based Scaffolds
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Cited by 9 •
2021
This paper lists the steps required to seed neuroblastoma cell lines on previously described three-dimensional collagen-based scaffolds, maintain cell growth for a predetermined timeframe, and retrieve scaffolds for several cell growth and cell behavior analyses and downstream applications, adaptable to satisfy a range of experimental aims.
05:17
An Improved Method for the Preparation of Type I Collagen From Skin
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Cited by 23 •
2014
Traditional procedures for the isolation of soluble type 1 collagen (COL1) require about 10 days from start to finish because of lengthy buffer incubations and laborious resuspensions of fibrils. Here, we describe a means to purify COL1 from small dermal biopsies in less than 3 hr.
01:11
Fibril-associated Collagen
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2023
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix. For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Hydroxylation modifies selected amino acids in newly synthesized procollagen before the molecule advances through the secretory pathway. This early processing step links production in the endoplasmic reticulum to later packaging by the Golgi apparatus. Because collagen must be modified before extracellular assembly, events inside the cell directly influence the structural matrix that developing tissues eventually form.
Terminal propeptides keep newly secreted collagen molecules from assembling prematurely inside the cell. After exocytosis, extracellular enzymes remove these terminal regions, permitting the molecules to align into fibrils and then larger fibers. This spatial separation helps coordinate intracellular production with extracellular matrix organization, allowing fibril formation to occur where tissue construction requires it.
Several sequential stages can influence the final matrix: procollagen synthesis, amino-acid hydroxylation in the endoplasmic reticulum, Golgi modification and packaging, exocytosis, and extracellular propeptide removal. Each stage connects cellular activity with later fibril and fiber assembly. Examining the sequence helps explain how cells convert molecular processing into organized mechanical support during development.
The sequence begins with procollagen synthesis in the endoplasmic reticulum and includes hydroxylation of selected amino acids. The molecule then undergoes further modification and packaging in the Golgi apparatus before leaving the cell by exocytosis. Outside the cell, enzyme-mediated removal of terminal propeptides enables assembly into fibrils and progressively larger fibers.
By supplying an organized extracellular matrix, collagen secretion helps developing tissues acquire strength, shape, and mechanical support. These matrix properties contribute to tissue morphogenesis, the coordinated shaping of tissues, as well as cell migration and organ development. Consequently, secretion links cellular biosynthetic activity with the physical architecture required as tissues and organs form.
Disrupting collagen secretion can interfere with extracellular matrix formation and alter tissue architecture. Because collagen supports tissue strength, shape, and mechanical organization, defects in its production, processing, export, or extracellular assembly may affect morphogenesis, cell migration, or organ development. The resulting changes show why coordinated secretion is important for normal developmental outcomes.