| 1. |
- Agarwal, Pallavi, et al.
(författare)
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Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure
- 2012
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 287:27, s. 22549-22559
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Tidskriftsartikel (refereegranskat)abstract
- The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures and supports the epidermis. In the skin, collagen I fibrils are the major structural component of the dermal ECM, decorated by proteoglycans and by fibril-associated collagens with interrupted triple helices such as collagens XII and XIV. Here we show that the cartilage oligomeric matrix protein (COMP), an abundant component of cartilage ECM, is expressed in healthy human skin. COMP expression is detected in the dermal compartment of skin and in cultured fibroblasts, whereas epidermis and HaCaT cells are negative. In addition to binding collagen I, COMP binds to collagens XII and XIV via their C-terminal collagenous domains. All three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin. Ultrastructural analysis by immunogold labeling confirmed colocalization and further revealed the presence of COMP along with collagens XII and XIV in anchoring plaques. On the basis of these observations, we postulate that COMP functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone.
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| 2. |
- Köhler, Anna, et al.
(författare)
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New specific HSP47 functions in collagen subfamily chaperoning
- 2020
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Ingår i: FASEB Journal. - 0892-6638. ; 34:9, s. 12040-12052
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Tidskriftsartikel (refereegranskat)abstract
- Although collagens are the most abundant proteins implicated in various disease pathways, essential mechanisms required for their proper folding and assembly are poorly understood. Heat-shock protein 47 (HSP47), an ER-resident chaperone, was mainly reported to fulfill key functions in folding and secretion of fibrillar collagens by stabilizing pro-collagen triple-helices. In this study, we demonstrate unique functions of HSP47 for different collagen subfamilies. Our results show that HSP47 binds to the N-terminal region of procollagen I and is essential for its secretion. However, HSP47 ablation does not majorly impact collagen VI secretion, but its lateral assembly. Moreover, specific ablation of Hsp47 in murine keratinocytes revealed a new role for the transmembrane collagen XVII triple-helix formation. Incompletely folded collagen XVII C-termini protruding from isolated HSP47 null keratinocyte membrane vesicles could be fully restored upon the application of recombinant HSP47. Thus, our study expands the current view regarding the client repertoire and function of HSP47, as well as emphasizes its importance for transmembrane collagen folding.
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| 3. |
- Mayorca-Guiliani, Alejandro E, et al.
(författare)
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Decellularization and antibody staining of mouse tissues to map native extracellular matrix structures in 3D
- 2019
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Ingår i: Nature Protocols. - : Springer Science and Business Media LLC. - 1750-2799 .- 1754-2189. ; 14, s. 3395-3425
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Tidskriftsartikel (refereegranskat)abstract
- The extracellular matrix (ECM) is a major regulator of homeostasis and disease, yet the 3D structure of the ECM remains poorly understood because of limitations in ECM visualization. We recently developed an ECM-specialized method termed in situ decellularization of tissues (ISDoT) to isolate native 3D ECM scaffolds from whole organs in which ECM structure and composition are preserved. Here, we present detailed surgical instructions to facilitate decellularization of 33 different mouse tissues and details of validated antibodies that enable the visualization of 35 mouse ECM proteins. Through mapping of these ECM proteins, the structure of the ECM can be determined and tissue structures visualized in detail. In this study, perfusion decellularization is presented for bones, skeletal muscle, tongue, salivary glands, stomach, duodenum, jejunum/ileum, large intestines, mesentery, liver, gallbladder, pancreas, trachea, bronchi, lungs, kidneys, urinary bladder, ovaries, uterine horn, cervix, adrenal gland, heart, arteries, veins, capillaries, lymph nodes, spleen, peripheral nerves, eye, outer ear, mammary glands, skin, and subcutaneous tissue. Decellularization, immunostaining, and imaging take 4-5 d.
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| 4. |
- Soedersten, Fredrik, et al.
(författare)
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Ultrastructural immunolocalization of cartilage oligomeric matrix protein, thrombospondin-4, and collagen fibril size in rodent Achilles tendon in relation to exercise
- 2007
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Ingår i: Connective Tissue Research. - : Informa UK Limited. - 1607-8438 .- 0300-8207. ; 48:5, s. 254-262
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Tidskriftsartikel (refereegranskat)abstract
- Fourteen 3-week-old Sprague-Dawley rats were housed in pairs in standard cages (5 controls) and in individual cages with a running wheel. Four of these rats had run 27-36 km/week (low training-LT) and 5 had run 56-92 km/week (high training-HT). After 4 weeks, the rats were euthanized and Achilles tendons were fixed for electron microscopy. The ultrastructural distribution of cartilage oligomeric matrix protein (COMP) and thrombospondin (TSP)-4 and collagen fibril thickness in two different extracellular compartments were studied. The immunolabeling of COMP decreased with longer running distance and was significantly lower in both the pericellular (p = 0.009) and interterritorial (p = 0.03) compartments of the HT rats compared with the controls. TSP-4 immunolabeling was higher in the pericellular compared with the interterritorial compartments in all rats (p = 0.013) but was not correlated with COMP immunolabeling. No alterations in collagen fibril size were found in relation to running; however, the gold markers representing COMP and TSP-4 were mostly found at the dark bands, representing the gap region of the fibril.
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