J Biol Chem
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1980 Nov 10;255(21):10451-9.Bovine glomerular basement membrane. Properties of the collagenous domain.West TW, Fox JW, Jodlowski M, Freytag JW, Hudson BG.Isolation and characterization of two alpha chain size collagenous polypeptide chains C and D from glomerular basement membrane.Collagenous architecture of the growth plate and perichondrial ossification The orientation of collagen fibers in the growth plate and contiguous structures of a growing long bone was demonstrated by polarized light microscopy.
Five major groups of collagen fibers were demonstrated: transphyseal (longitudinal), perichondrial-periosteal (longitudinal), epiphyseal (radial), perichondrial ring (circumferential), and metaphyseal bone (circumferential). Transphyseal collagen fibers extend from spicules of calcified cartilage in the metaphysis across the growth plate and into the epiphyseal cartilage and secondary ossification center. The transphyseal fibers interdigitate with radially oriented epiphyseal fibers which lie between the secondary ossification center and the zone of resting cells. A radial columnar alignment of cells, similar to the longitudinal cell columns of the growth plate, was correlated with the radial epiphyseal collagen fibers. Collagen fibers that are longitudinally oriented predominate in the perichondrium-periosteum. In the primary spongiosa, bone collagen is oriented obliquely and circumferentially on the longitudinal septa of calcified cartilage. A marked abundance of circumferentially oriented collagen fibers is seen within the perichondrial groove and in the perichondrium-periosteum directly over the groove.
The perichondrial rings is the largest and most prominent of these circumferential groups.The specific detection of collagenous proteins after electrophoresis using enzyme-conjugated collagen-binding fibronectin fragments.Evidence that interfibrillar load transfer in tendon is supported by small diameter fibrils and not extrafibrillar tissue components.Hall, 210 South 33rd St, Philadelphia, Pennsylvania, 19104.Lab, 150 Academy Street, Newark, Delaware, 19716.Hall, 36th St & Hamilton Walk, Philadelphia, Pennsylvania, 19104.Veterans Affairs Medical Center, 3900 Woodland Ave, Philadelphia, Pennsylvania, Collagen fibrils in tendon are believed to be discontinuous and transfer tensile loads through shear forces generated during interfibrillar sliding.
However, the structures that transmit these interfibrillar forces are unknown. Various extrafibrillar tissue components (e.g., glycosaminoglycans, collagens XII and XIV) have been suggested to transmit interfibrillar loads by bridging collagen fibrils. Alternatively, collagen fibrils may interact directly through physical fusions and interfibrillar branching. The objective of this study was to test whether extrafibrillar proteins are necessary to transmit load between collagen fibrils or if interfibrillar load transfer is accomplished directly by the fibrils themselves. Trypsin digestions were used to remove a broad spectrum of extrafibrillar proteins and measure their contribution to the multiscale mechanics of rat tail tendon fascicles.
Additionally, images obtained from serial block-face scanning electron microscopy were used to determine the three-dimensional fibrillar organization in tendon fascicles and identify any potential interfibrillar interactions. While trypsin successfully removed several extrafibrillar tissue components, there was no change in the macroscale fascicle mechanics or fibril:tissue strain ratio. Furthermore, the imaging data suggested that a network of smaller diameter fibrils (<150 nm) wind around and fuse with their neighboring larger diameter fibrils. These findings demonstrate that interfibrillar load transfer is not supported by extrafibrillar tissue components and support the hypothesis that collagen fibrils are capable of transmitting loads themselves. Conclusively determining how ergothioneine skin benefits bear load within tendon is critical for identifying the mechanisms that impair tissue function with degeneration and for restoring tissue properties via cell-mediated Society. Published by ergothioneine supplement , Inc. J Orthop Res 35:2127-2134, 2017.
Relationship of collagen-tailed acetylcholinesterase with basal lamina components. Absence of binding with laminin, fibronectin, and collagen types IV and V and lack of reactivity with different anti-collagen sera.In view of their supposed localization in extracellular structures, such as basal lamina, we have investigated the possible interactions of collagen-tailed forms of acetylcholinesterase from Electrophorus and bovine superior cervical ganglion with matrix proteins: laminin, fibronectin and types IV and V collagens. Using binding and sedimentation assays, with iodinated or non-radioactive matrix proteins, we have not observed any significant interaction, in conditions of high or low ionic strength. We also examined whether the collagen tail of acetylcholinesterase asymmetric forms possessed an immunological relationship with known collagen types (I, III, IV, V) from mammalian sources. We found no specific immunoreactivity with any of the 32 sera studied, either with the iodinated Electrophorus or with the native bovine enzyme.
Five major groups of collagen fibers were demonstrated: transphyseal (longitudinal), perichondrial-periosteal (longitudinal), epiphyseal (radial), perichondrial ring (circumferential), and metaphyseal bone (circumferential). Transphyseal collagen fibers extend from spicules of calcified cartilage in the metaphysis across the growth plate and into the epiphyseal cartilage and secondary ossification center. The transphyseal fibers interdigitate with radially oriented epiphyseal fibers which lie between the secondary ossification center and the zone of resting cells. A radial columnar alignment of cells, similar to the longitudinal cell columns of the growth plate, was correlated with the radial epiphyseal collagen fibers. Collagen fibers that are longitudinally oriented predominate in the perichondrium-periosteum. In the primary spongiosa, bone collagen is oriented obliquely and circumferentially on the longitudinal septa of calcified cartilage. A marked abundance of circumferentially oriented collagen fibers is seen within the perichondrial groove and in the perichondrium-periosteum directly over the groove.
The perichondrial rings is the largest and most prominent of these circumferential groups.The specific detection of collagenous proteins after electrophoresis using enzyme-conjugated collagen-binding fibronectin fragments.Evidence that interfibrillar load transfer in tendon is supported by small diameter fibrils and not extrafibrillar tissue components.Hall, 210 South 33rd St, Philadelphia, Pennsylvania, 19104.Lab, 150 Academy Street, Newark, Delaware, 19716.Hall, 36th St & Hamilton Walk, Philadelphia, Pennsylvania, 19104.Veterans Affairs Medical Center, 3900 Woodland Ave, Philadelphia, Pennsylvania, Collagen fibrils in tendon are believed to be discontinuous and transfer tensile loads through shear forces generated during interfibrillar sliding.
However, the structures that transmit these interfibrillar forces are unknown. Various extrafibrillar tissue components (e.g., glycosaminoglycans, collagens XII and XIV) have been suggested to transmit interfibrillar loads by bridging collagen fibrils. Alternatively, collagen fibrils may interact directly through physical fusions and interfibrillar branching. The objective of this study was to test whether extrafibrillar proteins are necessary to transmit load between collagen fibrils or if interfibrillar load transfer is accomplished directly by the fibrils themselves. Trypsin digestions were used to remove a broad spectrum of extrafibrillar proteins and measure their contribution to the multiscale mechanics of rat tail tendon fascicles.
Additionally, images obtained from serial block-face scanning electron microscopy were used to determine the three-dimensional fibrillar organization in tendon fascicles and identify any potential interfibrillar interactions. While trypsin successfully removed several extrafibrillar tissue components, there was no change in the macroscale fascicle mechanics or fibril:tissue strain ratio. Furthermore, the imaging data suggested that a network of smaller diameter fibrils (<150 nm) wind around and fuse with their neighboring larger diameter fibrils. These findings demonstrate that interfibrillar load transfer is not supported by extrafibrillar tissue components and support the hypothesis that collagen fibrils are capable of transmitting loads themselves. Conclusively determining how ergothioneine skin benefits bear load within tendon is critical for identifying the mechanisms that impair tissue function with degeneration and for restoring tissue properties via cell-mediated Society. Published by ergothioneine supplement , Inc. J Orthop Res 35:2127-2134, 2017.
Relationship of collagen-tailed acetylcholinesterase with basal lamina components. Absence of binding with laminin, fibronectin, and collagen types IV and V and lack of reactivity with different anti-collagen sera.In view of their supposed localization in extracellular structures, such as basal lamina, we have investigated the possible interactions of collagen-tailed forms of acetylcholinesterase from Electrophorus and bovine superior cervical ganglion with matrix proteins: laminin, fibronectin and types IV and V collagens. Using binding and sedimentation assays, with iodinated or non-radioactive matrix proteins, we have not observed any significant interaction, in conditions of high or low ionic strength. We also examined whether the collagen tail of acetylcholinesterase asymmetric forms possessed an immunological relationship with known collagen types (I, III, IV, V) from mammalian sources. We found no specific immunoreactivity with any of the 32 sera studied, either with the iodinated Electrophorus or with the native bovine enzyme.
