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Cargo proteins exported from the endoplasmic reticulum to the Golgi apparatus are typically transported in coat protein complex II (COPII)-coated vesicles of 60&#;90 nm diameter. Several cargo molecules including collagens and chylomicrons form structures that are too large to be accommodated by these vesicles, but their secretion still requires COPII proteins. Here, we first review recent progress on large cargo secretions derived especially from animal models and human diseases, which indicate the importance of COPII proteins. We then discuss the recent isolation of specialized factors that modulate the process of COPII-dependent cargo formation to facilitate the exit of large-sized cargoes from the endoplasmic reticulum. Based on these findings, we propose a model that describes the importance of the GTPase cycle for secretion of oversized cargoes. Next, we summarize reports that describe the structures of COPII proteins and how these results provide insight into the mechanism of assembly of the large cargo carriers. Finally, we discuss what issues remain to be solved in the future.
Cargoes exiting the endoplasmic reticulum (ER) to the Golgi apparatus are packaged into coat protein complex II (COPII)-coated vesicles that typically have diameters of 60&#;90 nm [1]. The formation of COPII vesicles occurs in particular regions of the ER called ER exit sites, also known as transitional ER (tER), which stain as punctuated dots scattered throughout the cytoplasm by immunofluorescence analysis of mammalian cells (Fig. ). The mechanisms to form transport vesicles is highly conserved from yeast to humans. The small GTPase Sar1 is activated by its guanine-nucleotide exchange factor (GEF), Sec12 [2&#;5]. After activation, Sar1 is recruited to the ER membrane [6&#;8] and forms the pre-budding complex [9&#;12], which consists of the inner coat complex Sec23/Sec24 and Sec24-bound cargo molecules [13&#;15]. Subsequently, the outer coat complex Sec13/Sec31 binds, and this binding event enhances the GTPase-activating protein activity of Sec23, thereby completing coat assembly [16&#;19]. Sec16 is the other factor essential in COPII biogenesis and functions as a scaffold to interact with particular coat proteins [20&#;25]. Recently, Sec16 has also been reported to negatively regulate GTP hydrolysis by Sar1 [26&#;28]. Additional factors involved in vesicle production have been identified, such as p125, TFG-1, and ALG2 [29&#;38]. The details of conventional COPII biogenesis have been reviewed extensively in other recently published articles [39&#;46].
Collagens synthesized in the ER fold into hetero- or homo-trimers, which form >300-nm-long rigid structures that are too large to fit into conventional COPII-coated vesicles [47&#;50]. However, imaging by fluorescent and electron microscopy indicates that collagen I exits the ER via the COPII-dependent process. Stephens and Pepperkok showed that microinjection of a GTPase-deficient mutant of Sar1a (Sar1a H79G) blocks the secretion of collagen I. Moreover, they showed that collagen I exits the ER in structures labeled with Sec24D, but segregates from vesicular stomatitis virus glycoprotein VSVG-ts045, a model of the conventional cargo proteins. The latter result implies that collagen transport to the Golgi is COPII dependent but distinct from conventional cargo trafficking [51]. Mironov et al. strengthened this finding by electron microscopy analysis, which showed that VSVG and collagen I exit the ER by a COPII-dependent process, but from distinct domains. Moreover, it was observed that protrusions from the ER domains in the vicinity of the ER exit sites form carriers containing either VSVG or collagen I. Interestingly, the formation of carriers is COPII dependent but does not seem to involve budding and fusion of COPII-coated vesicles [52].
The importance of COPII proteins for collagen secretion has also been suggested by analyzing human diseases and animal models (Table ). Two point mutations in Sec23A genes (F382L and M702V) have been identified as being responsible for cranio-lenticulo-sutural dysplasia (CLSD), an autosomal recessive disorder characterized by late-closing fontanels, facial dysmorphisms, and skeletal defects [53, 54]. Fibroblasts isolated from CLSD patients showed extensive dilation of the ER and accumulation of collagen I within the ER. Both mutations are located close to the binding site of Sec31. Biochemical and structural characterization suggests that Sec23A/F382L cannot recruit Sec13/Sec31 and therefore vesicle budding does not occur [18, 55]. In contrast, Sec23A/M702V is capable of interacting with Sec13/Sec31 and has no appreciable effects on vesicle budding in vitro. Interestingly, the M702V mutation seems to enhance Sar1B GTPase activity through an interaction with Sec13/Sec31 [56]. The zebrafish crusher mutation was obtained through a chemical mutagenesis screen to identify genes involved in craniofacial development [57]. Further analysis revealed that crusher has a nonsense mutation at residue 402 of the Sec23A gene. Crusher chondrocytes have distended ER with accumulated collagen II inside [58], further supporting that Sec23A is required for collagen export from the ER.
Recently, Sec23A has been identified as a target of the ER-resident transcription factor BBF2H7, also known as Creb3L2 [59]. BBF2H7 is expressed in chondrocytes and normally degraded by the ubiquitin-proteasome pathway, but upon ER stress, the transcription factor is stabilized and transported to the Golgi, then activated by proteolysis with Golgi-localized site-1 protease (S1P) and site-2 protease (S2P). The cleaved N-terminus translocates to the nucleus to upregulate the expression of Sec23A [60&#;62]. BBF2H7 knockout mice were found to show severe chondrodysplasia. Chondrocytes from knockout mice have expanded ER, where collagen II and cartilage oligomeric matrix protein accumulate in large amounts [59]. A zebrafish mutant carrying a missense mutation in BBF2H7 (feelgood) also showed defects in chondrocyte development, and the accumulation of collagen II was observed in distended ER [63]. These results suggest that BBF2H7-mediated transcription activation of Sec23A is necessary for collagen transport in chondrocytes. The requirement of the BBF2H7-Sec23A pathway for collagen transport was also reported for dermal fibroblasts [64].
The vertebrate possesses four isoforms of Sec24, and these isoforms are considered to fulfill the demands to traffic varieties of cargo molecules, although they appear to be partially redundant in cargo recognition [65]. Recent studies in fish indicated that Sec24D is specifically important for collagen secretion from the ER. Mutagenesis screens performed in medaka and zebrafish independently led to the identification of the nonsense mutations named vbi and bulldog, respectively [57]. Both mutants showed craniofacial defects, and chondrocytes from these mutants failed to secrete collagen II and displayed dilated ER [66, 67]. Osteogenesis imperfecta, a disorder associated with reduced bone mass, increased bone fragility, and bone deformity, is caused primarily by heterozygotic mutations in genes encoding collagen I (COL1A1 or COL1A2) [68]. A recent clinical study revealed that mutations of Sec24D are also responsible for the osteogenesis imperfecta phenotype. Affected individuals either possess two missense mutations in each Sec24D allele or one missense and the other nonsense mutation. Fibroblasts from patients showed accumulation of collagen I within the dilated ER [69]. Interestingly, knockout of Sec24D in mice revealed early embryonic lethality [70]. These results imply that Sec24D-dependent cargo transport is required for early stages of development, and truncated or mutated forms of Sec24D from fish mutants and patients have marginal activity required for early development, but not sufficient for secreting collagen I from the ER. Interestingly, the expression pattern of Sec24d has been reported to change during development. It is ubiquitously expressed during the early stages of development, whereas the expression is restricted to craniofacial cartilage during later stages of development [66].
Sec13 functions by forming individual complexes in different locations within cells. Sec13 is known to constitute the nuclear pore complex (NPC) [71]. However, Sec13 interacts with Sec31 to serve as an outer layer of COPII vesicles. In addition, Sec13 has been recently suggested to form a complex with Sec16, serving as a template for the formation of Sec13/31 outer coats [25].
Townley et al. first reported that zebrafish Sec13 morphants exhibit defects in craniofacial development. In mammalian cells, depletion of Sec13 by siRNA impairs collagen I secretion without affecting conventional cargo transport [72]. Interestingly, a zebrafish mutant originally identified as the small-liver phenotype in a screen was revealed to have a C-terminal truncation of Sec13, which makes it incapable of binding to Sec31 [73]. The mutant fish exhibits a hypoplastic digestive organ and small eyes with disrupted retinal lamination, and chondrocytes of the mutant showed collagen II accumulation in the dilated ER structures [74, 75]. In this context, a Sec31A knockdown by morpholino was performed in fish and showed malformation of the digestive organ, as observed in Sec13 mutants. Moreover, chondrocytes from morphants accumulate collagen II within the dilated ER. These results strongly suggest that defects in digestive organ development and collagen secretion in Sec13 mutant fish are due to the compromised COPII function. The mutation in NPC component Nup107 exhibits failure of retinal lamination, although knockdown of both Sec31A and Sec31B or treatment with brefeldin A, an inhibitor of ER to Golgi trafficking, has no effect on eye development. Thus, the function of Sec13 in the NPC complex appears to be necessary for retinal development [76].
As evidence accumulates, there is no doubt that collagen secretion from the ER requires COPII components. However, these results are not sufficient to conclude whether collagen is directly transported by modified COPII-coated structures, which can accommodate large-sized cargoes, or the COPII requirement for oversized-cargo secretion is limited and indirect. Recently, several molecules associated with ER exit sites have been identified to be specifically required for large cargo secretion and some models have been proposed. We will focus on this topic in the next section.
Collagen, often hailed as the &#;glue&#; that holds our bodies together, is a crucial protein for maintaining skin, joints, and connective tissues. While collagen is widely known, the science behind fish collagen and how it works deserves exploration. Fish collagen peptide is a distinctive and valuable ingredient for overall health and wellness.
It is derived from the pristine sources of fish skin, scales, and bones, the natural and bioactive compound offers a myriad of benefits for the human body. The unique helical structure and high bioavailability, hydrolyzed fish collagen peptide has become a focal point in various applications such as pharmaceuticals, nutraceuticals, skincare, and more. Let&#;s explore more about the science behind fish collagen peptide, its mode of action, benefits in skin & joint health, and how is it different from collagens derived from other sources.
Collagen is a fibrous protein with a triple helical structure, characterized by three polypeptide chains intertwined like a rope. Fish collagen, specifically derived from the scales, skin, or bones of fish, possesses a unique amino acid profile compared to other collagen sources such as bovine or porcine. The primary amino acids in fish collagen include glycine, proline, and hydroxyproline which are essential for collagen&#;s stability and function.
The helical structure of fish collagen peptides contributes to several beneficial properties, making it a popular ingredient in various applications. Here are some of the key benefits associated with the helical structure of fish collagen peptides:
Bioavailability- The body can more readily absorb and utilize collagen, leading to better results in terms of skin health, joint support, and other applications.
Structural Integrity- The unique structure provides collagen with its characteristic stability and structural integrity. It is crucial in supporting the connective tissues in the body, including skin, bones, tendons, and ligaments.
Improved Solubility- The improved solubility makes it easier to incorporate collagen into various products, such as beverages, nutraceutical formulations, powders, and topical formulations.
Cellular Interactions- The helical structure can facilitate interactions with cells and other components in the body, promoting cellular activities such as collagen synthesis and tissue regeneration.
Texture and Mouthfeel- The structure of fish collagen peptides can influence the texture and mouthfeel of the final product in the food & beverage sector, providing a smoother and more pleasant experience for consumers.
Upon consumption, fish collagen undergoes a series of processes within the body that facilitate its incorporation into the skin, joints, and other connective tissues. The digestive system breaks down fish collagen into smaller peptides through the action of enzymes like collagenase and peptidases. These peptides are then absorbed into the bloodstream, circulating and reaching target tissues.
One remarkable aspect of fish collagen is its bioavailability, referring to the extent and rate at which a substance is absorbed and becomes available for use in the body. Fish collagen peptides are known for their high bioavailability, meaning they are efficiently absorbed and utilized by the body compared to some other collagen sources.
Several factors contribute to the impressive absorption rates and bioavailability of fish collagen. The smaller size of marine fish collagen peptides, resulting from the hydrolysis process during production, plays a crucial role. The reduced molecular weight allows easier absorption through the intestinal barrier, enhancing the delivery of collagen peptides to target tissues.
Moreover, the composition of amino acids in fish collagen contributes to its bioavailability. The abundance of glycine facilitates rapid absorption. Studies have shown that fish collagen peptides reach higher levels in the bloodstream than other collagen types, making them an efficient choice for those seeking collagen supplementation.
Fish collagen is used for its potential benefits in addressing various skin and joint health issues. While individual responses can vary, here are some common problems in skin and joint health that fish collagen may potentially help address:
Wrinkles and Fine Lines- Fish collagen is believed to support skin elasticity and hydration, potentially reducing the appearance of wrinkles and fine lines.
Loss of Skin Elasticity- Collagen is a key component in maintaining skin firmness and elasticity. Fish collagen may contribute to restoring and preserving these qualities, addressing issues related to sagging or loss of skin elasticity.
Dry and Dehydrated Skin- Fish collagen peptides may enhance skin hydration by promoting the synthesis of hyaluronic acid, a molecule that helps retain water in the skin.
Dull Complexion- Improved skin hydration and collagen synthesis may produce a more vibrant and radiant complexion.
Skin Aging- As a natural part of aging, collagen production decreases, leading to changes in skin structure and appearance. Fish collagen may help counteract these effects.
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Wound Healing- Collagen is crucial for the wound healing process. Fish collagen may support the formation of granulation tissue and facilitate the migration and proliferation of skin cells, potentially aiding in wound healing.
Joint Pain and Discomfort- Fish collagen is thought to support joint health by influencing the synthesis of collagen in cartilage. It may help reduce joint pain and discomfort associated with conditions like osteoarthritis.
Reduced Joint Flexibility- Collagen is a major component of cartilage, which cushions and supports joints. Fish collagen may contribute to the maintenance and restoration of joint flexibility.
Cartilage Degeneration- Osteoarthritis and other joint conditions are often characterized by the degeneration of cartilage. Collagen peptides may play a role in supporting the regeneration of cartilage tissue.
Inflammation- Some research suggests that collagen peptides may have anti-inflammatory effects, which could be beneficial for managing joint inflammation.
Athletic Performance and Recovery- Athletes and individuals engaged in physical activities may benefit from collagen supplementation for joint support and enhanced recovery.
Numerous scientific studies have explored the efficacy of fish collagen in promoting skin health, joint function, and overall well-being. These studies provide valuable insights into the mechanisms through which fish collagen exerts its beneficial effects.
A study published in the Journal of Cosmetic Dermatology () investigated the effects of fish collagen peptides on skin hydration and elasticity. The results indicated a significant improvement in skin hydration and elasticity, suggesting that fish collagen supplementation could contribute to enhanced skin moisture and reduced signs of aging.
Research published in Marine Drugs () explored the potential of fish collagen in wound healing. The study demonstrated that fish collagen promoted cell migration and collagen synthesis, accelerating the wound-healing process. This suggests that fish collagen may not only benefit skin health but also support the body&#;s natural healing mechanisms.
A clinical trial published in the International Journal of Molecular Sciences () investigated the impact of fish collagen peptides on joint pain and function in individuals with osteoarthritis. The results indicated a significant reduction in joint pain and improved joint function in the group receiving fish collagen peptides, highlighting its potential as a supportive therapy for joint health.
Collagen is a structural protein found in the connective tissues of animals, and collagen supplements are derived from various sources. Fish collagen is one type of collagen that is distinct from collagen derived from other sources. Here are some key differences between fish collagen and collagen from other sources:
Bioavailability- Fish collagen is often considered to have high bioavailability due to its smaller peptide size and the helical structure of collagen peptides.
Fish Collagen Amino Acid Profile- It contains a unique amino acid profile, including high levels of glycine, proline, and hydroxyproline.
Allergen Potential- It is a suitable alternative for individuals with allergies to bovine or porcine collagen.
Taste and Odor- It may have a milder taste and odor compared to some other collagen sources, making it more versatile for various applications.
Texture and Application- It is often preferred in cosmetic and skincare products due to its texture and compatibility with formulations.
Sustainability- Fish Collagen Peptide is sourced from fish by-products may contribute to more sustainable practices.
The science behind fish collagen reveals a protein with a unique structure and exceptional bioavailability. The triple helix structure, amino acid composition, and hydrolysis process during production contribute to the effectiveness of fish collagen in promoting skin health, supporting joint function, and aiding in wound healing.
Scientific studies provide substantial evidence supporting the efficacy of fish collagen, further reinforcing its potential as a valuable supplement for those seeking to enhance overall well-being. As we continue to unravel the mysteries of collagen and its applications, fish collagen stands out as a promising option backed by cutting-edge research. Whether you&#;re interested in maintaining youthful skin or supporting joint health, understanding the science behind fish collagen empowers you to make informed choices for a healthier, more vibrant life.
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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC/
https://www.jstage.jst.go.jp/article/dmj/advpub/0/advpub_-446/_pdf
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC/
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